PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2777898-3 1989 Whereas bFGF and aFGF bind tightly to heparin and elute from a heparin-Sepharose column with 2 M NaCl and 1.6 M NaCl, respectively, TGFe binds to heparin with lower affinity and can be eluted from heparin-Sepharose column with 0.5 M NaCl. Heparin 38-45 fibroblast growth factor 1 Homo sapiens 17-21 2777898-3 1989 Whereas bFGF and aFGF bind tightly to heparin and elute from a heparin-Sepharose column with 2 M NaCl and 1.6 M NaCl, respectively, TGFe binds to heparin with lower affinity and can be eluted from heparin-Sepharose column with 0.5 M NaCl. Heparin 63-70 fibroblast growth factor 1 Homo sapiens 17-21 2777882-1 1989 The effects of heparin and other glycosaminoglycans (GAGs) on the mitogenicity and stability of acidic fibroblast growth factor (aFGF) were studied. Heparin 15-22 fibroblast growth factor 1 Homo sapiens 96-127 2777898-3 1989 Whereas bFGF and aFGF bind tightly to heparin and elute from a heparin-Sepharose column with 2 M NaCl and 1.6 M NaCl, respectively, TGFe binds to heparin with lower affinity and can be eluted from heparin-Sepharose column with 0.5 M NaCl. Heparin 63-70 fibroblast growth factor 1 Homo sapiens 17-21 2777898-3 1989 Whereas bFGF and aFGF bind tightly to heparin and elute from a heparin-Sepharose column with 2 M NaCl and 1.6 M NaCl, respectively, TGFe binds to heparin with lower affinity and can be eluted from heparin-Sepharose column with 0.5 M NaCl. Heparin 63-70 fibroblast growth factor 1 Homo sapiens 17-21 2777898-9 1989 The effects of heparin in both monolayer and soft agar were at least partially overcome by TGFe and by basic or acidic FGF. Heparin 15-22 fibroblast growth factor 1 Homo sapiens 119-122 2958303-2 1987 The promotion of normal cell growth by aFGF was suppressed by heparan sulfate but enhanced by heparin, while growth promotion by bFGF was suppressed by both GAGs. Heparin 94-101 fibroblast growth factor 1 Homo sapiens 39-43 2466852-7 1989 In comparison, heparin slightly inhibited the stimulatory effect of aFGF and had no effect on epidermal growth factor (EGF) stimulation in keratinocyte cultures. Heparin 15-22 fibroblast growth factor 1 Homo sapiens 68-72 2466852-8 1989 In fibroblast cultures the addition of heparin enhanced the mitogenic effect of aFGF, had a minimal stimulatory effect on the mitogenic activity of bFGF, and had no effect on EGF-stimulated growth. Heparin 39-46 fibroblast growth factor 1 Homo sapiens 80-84 2461712-1 1988 Pentosan polysulphate (PPS, SP 54, HEMOCLAR), a highly sulphated semi-synthetic polysaccharide of MW 4700 Daltons is as efficient as heparin in potentiating the mitogenic activity of acidic FGF (aFGF) on human umbilical vein endothelial cells (HUVEC). Heparin 133-140 fibroblast growth factor 1 Homo sapiens 183-193 2461712-7 1988 PPS and heparin, which were chemotactic alone on BAEC, potentiated acidic FGF-induced migration but inhibited the chemotactic response of basic FGF. Heparin 8-15 fibroblast growth factor 1 Homo sapiens 67-77 2460964-0 1988 Heparin potentiates endothelial cell growth factor stimulation of plasminogen activator synthesis by diploid human lung fibroblasts. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 20-50 2460964-1 1988 Endothelial cell growth factor (ECGF) stimulates the synthesis of t-PA and u-PA by confluent, diploid human lung fibroblasts, and this activity is potentiated considerably by heparin. Heparin 175-182 fibroblast growth factor 1 Homo sapiens 0-30 2460964-1 1988 Endothelial cell growth factor (ECGF) stimulates the synthesis of t-PA and u-PA by confluent, diploid human lung fibroblasts, and this activity is potentiated considerably by heparin. Heparin 175-182 fibroblast growth factor 1 Homo sapiens 32-36 2460964-4 1988 The mechanism by which heparin potentiates this effect is thought to reside in its ability to prolong or strengthen the interaction of ECGF with cell surface receptors. Heparin 23-30 fibroblast growth factor 1 Homo sapiens 135-139 3353388-4 1988 The action of aFGF on process outgrowth was markedly potentiated by the addition of heparin (10 micrograms/ml) to the medium, but heparin alone had no effect. Heparin 84-91 fibroblast growth factor 1 Homo sapiens 14-18 3353388-4 1988 The action of aFGF on process outgrowth was markedly potentiated by the addition of heparin (10 micrograms/ml) to the medium, but heparin alone had no effect. Heparin 130-137 fibroblast growth factor 1 Homo sapiens 14-18 3353388-5 1988 In the presence of heparin, half-maximal process outgrowth occurred at an aFGF concentration of less than 20 pg/ml (1 pM). Heparin 19-26 fibroblast growth factor 1 Homo sapiens 74-78 3353388-7 1988 Statistical analysis of the increase in process growth revealed that aFGF with heparin contributed to both neurite initiation and elongation. Heparin 79-86 fibroblast growth factor 1 Homo sapiens 69-73 3353388-11 1988 The potentiation of this effect by heparin leads us to speculate that the interaction of aFGF with a heparin-like molecule located in the extracellular matrix (such as heparan sulfate proteoglycan) may produce physiological effects in vivo. Heparin 35-42 fibroblast growth factor 1 Homo sapiens 89-93 3353388-11 1988 The potentiation of this effect by heparin leads us to speculate that the interaction of aFGF with a heparin-like molecule located in the extracellular matrix (such as heparan sulfate proteoglycan) may produce physiological effects in vivo. Heparin 101-108 fibroblast growth factor 1 Homo sapiens 89-93 2550475-1 1989 The minimal structural requirements for the interaction of heparin with acidic fibroblast growth factor (aFGF) were investigated. Heparin 59-66 fibroblast growth factor 1 Homo sapiens 72-103 2550475-1 1989 The minimal structural requirements for the interaction of heparin with acidic fibroblast growth factor (aFGF) were investigated. Heparin 59-66 fibroblast growth factor 1 Homo sapiens 105-109 2524607-5 1989 In the presence of ECGF-heparin, the immediate establishment of an EC layer after sodding was observed, whereas seeded grafts required almost 48 hours for cells to reach the surface. Heparin 24-31 fibroblast growth factor 1 Homo sapiens 19-23 3680267-6 1987 Fluorescence spectroscopy was used to study the interaction between recombinant ECGF and heparin. Heparin 89-96 fibroblast growth factor 1 Homo sapiens 80-84 3680267-7 1987 Heparin-binding resulted in a 40% reduction in the intrinsic fluorescence of ECGF, consistent with a heparin-induced conformational change. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 77-81 3680267-7 1987 Heparin-binding resulted in a 40% reduction in the intrinsic fluorescence of ECGF, consistent with a heparin-induced conformational change. Heparin 101-108 fibroblast growth factor 1 Homo sapiens 77-81 2958303-4 1987 The growth of spontaneously transformed cells was enhanced by heparan sulfate or heparin in the presence of 10% FBS or aFGF, while growth promotion in the presence of bFGF was suppressed by both GAGs. Heparin 81-88 fibroblast growth factor 1 Homo sapiens 119-123 3729956-0 1986 Effect of heparin on the stimulation of non-vascular cells by human acidic and basic FGF. Heparin 10-17 fibroblast growth factor 1 Homo sapiens 85-88 3619892-4 1987 In brain c-aFGF represented 66% of the total mitogenic activity retained on the heparin-sepharose column and c-bFGF 34% while retina contained 16% of c-aFGF and 84% of c-bFGF; vitreous 78% of c-aFGF and 22% of c-bFGF. Heparin 80-87 fibroblast growth factor 1 Homo sapiens 11-15 3619892-5 1987 Like human aFGF, Heparin stimulated purified c-aFGF mitogenic activity in the absence of serum but inhibited the activity of the retina acid soluble extract, in the presence of foetal calf serum (FCS). Heparin 17-24 fibroblast growth factor 1 Homo sapiens 11-15 3619892-5 1987 Like human aFGF, Heparin stimulated purified c-aFGF mitogenic activity in the absence of serum but inhibited the activity of the retina acid soluble extract, in the presence of foetal calf serum (FCS). Heparin 17-24 fibroblast growth factor 1 Homo sapiens 47-51 3518813-4 1986 f-ECGF had a high affinity to heparin-Sepharose CL-6B, and was isolated by the methods of heparin affinity, of ion-exchange and gel filtration chromatography from the serum-free culture-conditioned medium preparation. Heparin 30-37 fibroblast growth factor 1 Homo sapiens 2-6 3518813-4 1986 f-ECGF had a high affinity to heparin-Sepharose CL-6B, and was isolated by the methods of heparin affinity, of ion-exchange and gel filtration chromatography from the serum-free culture-conditioned medium preparation. Heparin 90-97 fibroblast growth factor 1 Homo sapiens 2-6 3729956-2 1986 In both the presence and the absence of foetal calf serum (FCS) heparin cooperates with h-aFGF in a dose dependent manner to stimulate both types of cells. Heparin 64-71 fibroblast growth factor 1 Homo sapiens 90-94 3729956-5 1986 These results indicate that heparin cooperates strongly with h-aFGF to stimulate non-vascular cell proliferation while in a partially purified extract and in the presence of serum it can induce the opposite effect. Heparin 28-35 fibroblast growth factor 1 Homo sapiens 63-67 2412230-3 1985 Heparin interacts structurally with ECGF [Maciag, T., Mehlman, T., Friesel, R. & Schreiber, A. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 36-40 3905825-3 1985 Heparin (10(-8) to 10(-10) M) was also chemotactic and was shown to potentiate the chemotactic activity of ECGF. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 107-111 2412230-6 1985 These data suggest that the association between heparin and ECGF induces a conformational change in the polypeptide that increases or stabilizes the biological activity of the mitogen. Heparin 48-55 fibroblast growth factor 1 Homo sapiens 60-64 30667535-3 2019 In this study, for the first time, microsecond-scale MD simulations are reported for a complex between fibroblast growth factor 1 and heparin. Heparin 134-141 fibroblast growth factor 1 Homo sapiens 103-129 33745974-4 2021 We have demonstrated that oligomerization of FGF1 with coiled-coil motifs largely improves FGF1 affinity for FGFRs and heparin. Heparin 119-126 fibroblast growth factor 1 Homo sapiens 45-49 33745974-4 2021 We have demonstrated that oligomerization of FGF1 with coiled-coil motifs largely improves FGF1 affinity for FGFRs and heparin. Heparin 119-126 fibroblast growth factor 1 Homo sapiens 91-95 32653371-9 2020 Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1. Heparin 113-120 fibroblast growth factor 1 Homo sapiens 124-150 32653371-9 2020 Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1. Heparin 113-120 fibroblast growth factor 1 Homo sapiens 152-156 32653371-9 2020 Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1. Heparin 113-120 fibroblast growth factor 1 Homo sapiens 317-321 32653371-9 2020 Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1. Heparin 176-183 fibroblast growth factor 1 Homo sapiens 124-150 32653371-9 2020 Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1. Heparin 176-183 fibroblast growth factor 1 Homo sapiens 152-156 32653371-9 2020 Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1. Heparin 176-183 fibroblast growth factor 1 Homo sapiens 317-321 31420170-3 2019 Using a wide range of biophysical and biochemical techniques, we demonstrate that reversal of charge on a well-conserved positively charged amino acid, R136, in the heparin binding pocket drastically increases the resistance to proteases, thermal stability, and cell proliferation activity of the human acidic fibroblast growth factor (hFGF1). Heparin 165-172 fibroblast growth factor 1 Homo sapiens 336-341 31420170-7 2019 Isothermal titration calorimetry data show that the R136E mutation markedly decreases the heparin binding affinity of hFGF1. Heparin 90-97 fibroblast growth factor 1 Homo sapiens 118-123 31578149-4 2019 Herein, a heparin-immobilized fibroin hydrogel was fabricated to deliver FGF1 (human acidic fibroblast growth factor 1) on top of wound in rats with full-thickness skin excision by performing comprehensive preclinical studies to fully evaluate its safety and effectiveness. Heparin 10-17 fibroblast growth factor 1 Homo sapiens 73-77 31271519-5 2019 Therefore, we analyzed the interactions of FGF1 and FGF2 with four sulfated polysaccharides: heparin, dextran sulfate (DXS), lambda-carrageenan, and chondroitin sulfate. Heparin 93-100 fibroblast growth factor 1 Homo sapiens 43-47 30667535-7 2019 Our data provide novel significant insights into the interactions in the fibroblast growth factor 1 complex with heparin, in particular, and into the physical-chemical nature of protein-glycosaminoglycan systems in general, which have potential applicability for biomaterials development in the area of regenerative medicine. Heparin 113-120 fibroblast growth factor 1 Homo sapiens 73-99 30031837-2 2018 In this study, we investigate the effect(s) of understanding the role of a conserved proline (P135), located in the heparin binding pocket, on the structure, stability, heparin binding affinity, and cell proliferation activity of hFGF1. Heparin 116-123 fibroblast growth factor 1 Homo sapiens 230-235 30031837-4 2018 Interestingly, upon heparin binding, an increase in thermal stability equivalent to that of wt-hFGF1 was observed when P135 was replaced with a positive (P135K) or a negative charge (P135E), or with a polar amino acid (P135Q). Heparin 20-27 fibroblast growth factor 1 Homo sapiens 95-100 30031837-5 2018 Surprisingly, introduction of negative charge in the heparin-binding pocket at position 135 (P135E) increased hFGF1"s affinity for heparin by 3-fold, while the P135K mutation, did not alter the heparin-binding affinity. Heparin 53-60 fibroblast growth factor 1 Homo sapiens 110-115 30031837-5 2018 Surprisingly, introduction of negative charge in the heparin-binding pocket at position 135 (P135E) increased hFGF1"s affinity for heparin by 3-fold, while the P135K mutation, did not alter the heparin-binding affinity. Heparin 131-138 fibroblast growth factor 1 Homo sapiens 110-115 30031837-5 2018 Surprisingly, introduction of negative charge in the heparin-binding pocket at position 135 (P135E) increased hFGF1"s affinity for heparin by 3-fold, while the P135K mutation, did not alter the heparin-binding affinity. Heparin 131-138 fibroblast growth factor 1 Homo sapiens 110-115 30031837-9 2018 Overall, the results of this study suggest that while heparin is useful for stabilizing hFGF1 on the cell surface, this interaction is not mandatory for activation of the FGF receptor. Heparin 54-61 fibroblast growth factor 1 Homo sapiens 88-93 30271699-4 2018 The impact of temperature on the binding of heparin to three representative heparin-binding proteins, antithrombin III (AT III), fibroblast growth factor-1 (FGF1) and fibroblast growth factor-2 (FGF2) are evaluated. Heparin 44-51 fibroblast growth factor 1 Homo sapiens 129-155 29812912-8 2018 We found that FGF1 binds CD44 through its heparin-binding moiety. Heparin 42-49 fibroblast growth factor 1 Homo sapiens 14-18 29645318-5 2018 Crystal structures of FGF-1 in complex with heparin have shown that heparin binds to N-terminal Asn18 and to C-terminal Lys105, Tryp107, Lys112, Lys113, Arg119, Pro121, Arg122, Gln127, and Lys128 indicating electrostatic forces as dominant interactions. Heparin 44-51 fibroblast growth factor 1 Homo sapiens 22-27 29645318-5 2018 Crystal structures of FGF-1 in complex with heparin have shown that heparin binds to N-terminal Asn18 and to C-terminal Lys105, Tryp107, Lys112, Lys113, Arg119, Pro121, Arg122, Gln127, and Lys128 indicating electrostatic forces as dominant interactions. Heparin 68-75 fibroblast growth factor 1 Homo sapiens 22-27 29645318-7 2018 Previous studies have also shown that other polyanions including low MW heparin, phytic acid and ATP dramatically increase the thermal stability of FGF-1. Heparin 72-79 fibroblast growth factor 1 Homo sapiens 148-153 29645318-8 2018 Using HX-MS, we find other poly anions tested bind in a similar manner to heparin, primarily targeting the turns in the lysine rich C-terminal region of FGF-1 along with two distinct N-terminal regions that contains lysines and arginines/histidines. Heparin 74-81 fibroblast growth factor 1 Homo sapiens 153-158 30271699-4 2018 The impact of temperature on the binding of heparin to three representative heparin-binding proteins, antithrombin III (AT III), fibroblast growth factor-1 (FGF1) and fibroblast growth factor-2 (FGF2) are evaluated. Heparin 44-51 fibroblast growth factor 1 Homo sapiens 157-161 29016740-1 2017 Aims: Fibroblast growth factor 1 (FGF1), a heparin/heparan sulfate-binding growth factor, is a potent cardioprotective agent against myocardial infarction (MI). Heparin 43-50 fibroblast growth factor 1 Homo sapiens 6-32 29556563-4 2018 In this context, in this study, the correlation between heparin binding affinity and cell proliferation activity of hFGF1 is examined by extending the heparin binding pocket through selective engineering via charge reversal mutations (D82R, D84R and D82R/D84R). Heparin 56-63 fibroblast growth factor 1 Homo sapiens 116-121 29556563-4 2018 In this context, in this study, the correlation between heparin binding affinity and cell proliferation activity of hFGF1 is examined by extending the heparin binding pocket through selective engineering via charge reversal mutations (D82R, D84R and D82R/D84R). Heparin 151-158 fibroblast growth factor 1 Homo sapiens 116-121 29556563-9 2018 However, despite the increased affinity of D82R for heparin, the cell proliferation activity of the D82R variant is observed to be reduced compared to the wild type hFGF1. Heparin 52-59 fibroblast growth factor 1 Homo sapiens 165-170 29556563-10 2018 The results of this study clearly demonstrate that heparin binding affinity of hFGF1 is not strongly correlated to its cell proliferation activity. Heparin 51-58 fibroblast growth factor 1 Homo sapiens 79-84 29016740-1 2017 Aims: Fibroblast growth factor 1 (FGF1), a heparin/heparan sulfate-binding growth factor, is a potent cardioprotective agent against myocardial infarction (MI). Heparin 43-50 fibroblast growth factor 1 Homo sapiens 34-38 29016740-7 2017 Both native and modified FGF1 restored contractile and relaxation function (P < 0.05 versus saline or heparin). Heparin 105-112 fibroblast growth factor 1 Homo sapiens 25-29 29016740-9 2017 Heparin negatively impacted the cardioprotective effects (infarct size, post-ischemic recovery of function) of FGF1 (P < 0.05) but not of FGF1DeltaHBS. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 111-115 29016740-10 2017 Heparin also reduced the biodistribution of FGF1, but not FGF1DeltaHBS, to the left ventricle. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 44-48 29016740-11 2017 FGF1 and FGF1DeltaHBS bound and triggered FGFR1-induced downstream activation of ERK1/2 (P < 0.05); yet, heparin co-treatment decreased FGF1-produced ERK1/2 activation, but not that activated by FGF1DeltaHBS. Heparin 108-115 fibroblast growth factor 1 Homo sapiens 0-4 29016740-11 2017 FGF1 and FGF1DeltaHBS bound and triggered FGFR1-induced downstream activation of ERK1/2 (P < 0.05); yet, heparin co-treatment decreased FGF1-produced ERK1/2 activation, but not that activated by FGF1DeltaHBS. Heparin 108-115 fibroblast growth factor 1 Homo sapiens 9-13 29016740-11 2017 FGF1 and FGF1DeltaHBS bound and triggered FGFR1-induced downstream activation of ERK1/2 (P < 0.05); yet, heparin co-treatment decreased FGF1-produced ERK1/2 activation, but not that activated by FGF1DeltaHBS. Heparin 108-115 fibroblast growth factor 1 Homo sapiens 9-13 29016740-11 2017 FGF1 and FGF1DeltaHBS bound and triggered FGFR1-induced downstream activation of ERK1/2 (P < 0.05); yet, heparin co-treatment decreased FGF1-produced ERK1/2 activation, but not that activated by FGF1DeltaHBS. Heparin 108-115 fibroblast growth factor 1 Homo sapiens 9-21 29016740-12 2017 Conclusion: These findings demonstrate that modification of the heparin-binding region of FGF1 significantly improves the cardioprotective efficacy, even in the presence of heparin, identifying a novel FGF ligand available for therapeutic use in ischemic heart disease. Heparin 64-71 fibroblast growth factor 1 Homo sapiens 90-94 29016740-12 2017 Conclusion: These findings demonstrate that modification of the heparin-binding region of FGF1 significantly improves the cardioprotective efficacy, even in the presence of heparin, identifying a novel FGF ligand available for therapeutic use in ischemic heart disease. Heparin 64-71 fibroblast growth factor 1 Homo sapiens 90-93 29016740-12 2017 Conclusion: These findings demonstrate that modification of the heparin-binding region of FGF1 significantly improves the cardioprotective efficacy, even in the presence of heparin, identifying a novel FGF ligand available for therapeutic use in ischemic heart disease. Heparin 173-180 fibroblast growth factor 1 Homo sapiens 90-94 29016740-12 2017 Conclusion: These findings demonstrate that modification of the heparin-binding region of FGF1 significantly improves the cardioprotective efficacy, even in the presence of heparin, identifying a novel FGF ligand available for therapeutic use in ischemic heart disease. Heparin 173-180 fibroblast growth factor 1 Homo sapiens 90-93 29091276-3 2017 Based on the structural knowledge available from the FGF1-heparin interaction studies, we have designed a novel heparin-binding peptide (HBP) affinity tag that can be used for the simple, efficient, and cost-effective purification of recombinant proteins of interest. Heparin 58-65 fibroblast growth factor 1 Homo sapiens 53-57 24595027-4 2014 We confirmed a direct nucleolin-FGF1 interaction by surface plasmon resonance and identified residues of FGF1 involved in the binding to be located within the heparin binding site. Heparin 159-166 fibroblast growth factor 1 Homo sapiens 32-36 28629128-2 2017 The overall structure of the ternary complex Heparin:FGF-1:FGFR has been finally elucidated after some controversy and the interactions within the ternary complex have been deeply described. Heparin 45-52 fibroblast growth factor 1 Homo sapiens 53-58 28181797-0 2017 A Thermosensitive Heparin-Poloxamer Hydrogel Bridges aFGF to Treat Spinal Cord Injury. Heparin 18-25 fibroblast growth factor 1 Homo sapiens 53-57 26138239-12 2015 Both alone and in the presence of heparin, FGF1 led to increased MAPK-signaling in primary lung fibroblasts. Heparin 34-41 fibroblast growth factor 1 Homo sapiens 43-47 26138239-14 2015 In addition, FGF1 + heparin increased apoptosis and cell migration. Heparin 20-27 fibroblast growth factor 1 Homo sapiens 13-17 25043635-3 2014 First, acidic fibroblast growth factor (FGF-1) was incubated under conditions known to promote (40 C) and inhibit (heparin addition) molten globule formation. Heparin 115-122 fibroblast growth factor 1 Homo sapiens 40-45 25043635-4 2014 Heat exposed (40 C) FGF-1 exhibited binding to GroEL-biosensors, which was significantly diminished in the presence of heparin. Heparin 119-126 fibroblast growth factor 1 Homo sapiens 20-25 24595027-4 2014 We confirmed a direct nucleolin-FGF1 interaction by surface plasmon resonance and identified residues of FGF1 involved in the binding to be located within the heparin binding site. Heparin 159-166 fibroblast growth factor 1 Homo sapiens 105-109 23601319-0 2013 Cooperative heparin-mediated oligomerization of fibroblast growth factor-1 (FGF1) precedes recruitment of FGFR2 to ternary complexes. Heparin 12-19 fibroblast growth factor 1 Homo sapiens 48-74 28890953-6 2014 The results showed that under non-physiological of metal ion concentration, different metal ions showed different effects on heparin binding to fibroblast growth factor-1 (FGF1) and interleakin-7 (IL7). Heparin 125-132 fibroblast growth factor 1 Homo sapiens 144-170 28890953-6 2014 The results showed that under non-physiological of metal ion concentration, different metal ions showed different effects on heparin binding to fibroblast growth factor-1 (FGF1) and interleakin-7 (IL7). Heparin 125-132 fibroblast growth factor 1 Homo sapiens 172-176 28890953-7 2014 While the effects of individual metal ion at physiological concentrations had little impact on protein binding, the mixed metal ions reduced the FGF1/heparin or IL7/heparin binding affinity, changing its binding profile. Heparin 150-157 fibroblast growth factor 1 Homo sapiens 145-149 24178304-0 2013 3D structure of a heparin mimetic analogue of a FGF-1 activator. Heparin 18-25 fibroblast growth factor 1 Homo sapiens 48-53 23601319-0 2013 Cooperative heparin-mediated oligomerization of fibroblast growth factor-1 (FGF1) precedes recruitment of FGFR2 to ternary complexes. Heparin 12-19 fibroblast growth factor 1 Homo sapiens 76-80 23601319-3 2013 Heparin fragments of defined length are used as chemical analogs of the sulfated domains of heparan sulfate and examined for their ability to oligomerize FGF1. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 154-158 23601319-7 2013 The thermodynamics and stoichiometry of the ternary complex suggest that in solution FGF1 binds to heparin in a trans-dimeric manner before FGFR recruitment. Heparin 99-106 fibroblast growth factor 1 Homo sapiens 85-89 19819428-3 2009 Molecular docking calculations showed that the predicted locations of the disaccharide sulfo groups in the binding site of FGF-1 and FGF-2 are similar to the positions observed for co-crystallized heparin-derived oligosaccharides obtained from published crystal structures. Heparin 197-204 fibroblast growth factor 1 Homo sapiens 123-128 22687193-6 2013 RESULTS: Q40P/S47I/H93G could activate all subtypes of FGF receptors in vitro much more strongly than the wild-type without endogenous or exogenous heparin. Heparin 148-155 fibroblast growth factor 1 Homo sapiens 55-58 22687193-9 2013 The level of stability of FGF1 mutants correlated with their mitogenic activities in vitro in the absence of heparin; however, preirradiation treatment with the mutants increased the crypt number to almost the same level as Q40P/S47I/H93G. Heparin 109-116 fibroblast growth factor 1 Homo sapiens 26-30 23133616-2 2012 FGF-1 has low intrinsic thermostability and is characteristically formulated with heparin as a stabilizing agent. Heparin 82-89 fibroblast growth factor 1 Homo sapiens 0-5 23133616-4 2012 Mutations that increase the thermostability of FGF-1 may obviate the need for heparin in formulation and may prove to be useful "2nd-generation" forms for therapeutic use. Heparin 78-85 fibroblast growth factor 1 Homo sapiens 47-52 23133616-7 2012 The addition of heparin to FGF-1 is shown to increase endocrine-like properties of distribution. Heparin 16-23 fibroblast growth factor 1 Homo sapiens 27-32 21185801-3 2011 Using a combination of biophysical and functional assays, we found that the fluorescently labeled mutant aFGF is characterized by essentially the same global folding, mitogenic activity, and association behavior with heparin, its physiological activator, as the unlabeled wild-type protein. Heparin 217-224 fibroblast growth factor 1 Homo sapiens 105-109 21185801-4 2011 We used this new tracer protein mutant to determine the association behavior of aFGF with heparin in the presence of high concentrations of albumin that mimicked more closely the plasma medium in which aFGF is naturally located and in which it has evolved to function. Heparin 90-97 fibroblast growth factor 1 Homo sapiens 80-84 21185801-5 2011 By exposing the aFGF-Cys2-heparin complex to increasing concentrations of albumin up to physiological plasma levels, we were able to demonstrate that macromolecular crowding does not affect the stoichiometry of the interaction. Heparin 26-33 fibroblast growth factor 1 Homo sapiens 16-20 20827464-1 2011 The preparation and characterization of heparin-immobilized microspheres which were used to bind acidic fibroblast growth factor (aFGF), vascular endothelial growth factor (VEGF), monocyte chemoattractant protein 1 (MCP-1/CCL2), and regulation upon activation normal T cell express sequence (RANTES/CCL5) is described. Heparin 40-47 fibroblast growth factor 1 Homo sapiens 97-128 20827464-1 2011 The preparation and characterization of heparin-immobilized microspheres which were used to bind acidic fibroblast growth factor (aFGF), vascular endothelial growth factor (VEGF), monocyte chemoattractant protein 1 (MCP-1/CCL2), and regulation upon activation normal T cell express sequence (RANTES/CCL5) is described. Heparin 40-47 fibroblast growth factor 1 Homo sapiens 130-134 20827464-6 2011 These heparin-immobilized microspheres exhibited broad dynamic ranges for binding to the four cytokines (aFGF, 1.0-1,000 ng/mL; VEGF, 0.5-1,000 ng/mL; CCL2, 1.95-1,000 ng/mL; CCL5, 1.95-500 ng/mL). Heparin 6-13 fibroblast growth factor 1 Homo sapiens 105-109 23019343-5 2012 For interaction with heparin, the FGFs exhibit K(D) values varying between 38 nM (FGF-18) and 620 nM (FGF-9) and association rate constants spanning over 20-fold (FGF-1, 2,900,000 M(-1) s(-1) and FGF-9, 130,000 M(-1) s(-1)). Heparin 21-28 fibroblast growth factor 1 Homo sapiens 82-87 23019343-8 2012 These data suggest that the differences in heparin-binding sites in both the protein and the sugar are greatest between subfamilies and may be more restricted within a FGF subfamily in accord with the known conservation of function within FGF subfamilies. Heparin 43-50 fibroblast growth factor 1 Homo sapiens 168-171 23019343-8 2012 These data suggest that the differences in heparin-binding sites in both the protein and the sugar are greatest between subfamilies and may be more restricted within a FGF subfamily in accord with the known conservation of function within FGF subfamilies. Heparin 43-50 fibroblast growth factor 1 Homo sapiens 239-242 22113934-1 2012 Acidic fibroblast growth factor-1 (FGF-1) is an angiogenic protein which requires binding to a polyanion such as heparin for its mitogenic activity and physicochemical stability. Heparin 113-120 fibroblast growth factor 1 Homo sapiens 35-40 22113934-4 2012 FGF-1 mutants were identified with stability profiles in the absence of heparin comparable to that of wild-type FGF-1 in the presence of heparin while still retaining their biological activity. Heparin 72-79 fibroblast growth factor 1 Homo sapiens 0-5 22113934-4 2012 FGF-1 mutants were identified with stability profiles in the absence of heparin comparable to that of wild-type FGF-1 in the presence of heparin while still retaining their biological activity. Heparin 137-144 fibroblast growth factor 1 Homo sapiens 0-5 20416374-9 2010 This is approached through a few illustrative examples, including the interaction of HS and heparin-derived species with the chemokine IL-8, the growth factors FGF1 and FGF2, and the modulation of the activity of the enzyme heparanase by these species. Heparin 92-99 fibroblast growth factor 1 Homo sapiens 160-164 19034645-4 2009 The assay is applicable to a wide variety of heparin/HS-binding proteins of diverse structure and function (e.g., FGF-1, FGF-2, VEGF, IL-8, MCP-2, ATIII, PF4) and to ligands of varying molecular weight and degree of sulfation (e.g., heparin, PI-88, sucrose octasulfate, naphthalene trisulfonate) and is thus well suited for the rapid screening of ligands in drug discovery applications. Heparin 45-52 fibroblast growth factor 1 Homo sapiens 114-119 19810698-3 2009 The impact of structure and time-dependent changes in the structural elements in FGF1and FGF1-heparin in the presence of the AuNP is probed by a molecular beacon fluorescence assay, circular dichroism, and NMR spectroscopy. Heparin 94-101 fibroblast growth factor 1 Homo sapiens 89-93 19574212-0 2009 Increased protein stability of FGF1 can compensate for its reduced affinity for heparin. Heparin 80-87 fibroblast growth factor 1 Homo sapiens 31-35 19574212-2 2009 Binding to heparin increases the stability of FGF1 and is believed to be important in the formation of FGF1.fibroblast growth factor receptor (FGFR) active complex. Heparin 11-18 fibroblast growth factor 1 Homo sapiens 46-50 19574212-2 2009 Binding to heparin increases the stability of FGF1 and is believed to be important in the formation of FGF1.fibroblast growth factor receptor (FGFR) active complex. Heparin 11-18 fibroblast growth factor 1 Homo sapiens 103-107 19574212-3 2009 In order to reveal the function of heparin in FGF1.FGFR complex formation and signaling, we constructed several FGF1 variants with reduced affinity for heparin and with diverse stability. Heparin 35-42 fibroblast growth factor 1 Homo sapiens 46-50 19574212-3 2009 In order to reveal the function of heparin in FGF1.FGFR complex formation and signaling, we constructed several FGF1 variants with reduced affinity for heparin and with diverse stability. Heparin 35-42 fibroblast growth factor 1 Homo sapiens 112-116 19574212-3 2009 In order to reveal the function of heparin in FGF1.FGFR complex formation and signaling, we constructed several FGF1 variants with reduced affinity for heparin and with diverse stability. Heparin 152-159 fibroblast growth factor 1 Homo sapiens 112-116 19574212-5 2009 Our study showed that increased thermodynamic stability of FGF1 nicely compensates for decreased binding of heparin in FGFR activation, induction of DNA synthesis, and cell proliferation. Heparin 108-115 fibroblast growth factor 1 Homo sapiens 59-63 19574212-6 2009 By stepwise introduction of stabilizing mutations into the K118E (K132E) FGF1 variant that shows reduced affinity for heparin and is inactive in stimulation of DNA synthesis, we were able to restore the full mitogenic activity of this mutant. Heparin 118-125 fibroblast growth factor 1 Homo sapiens 73-77 19574212-7 2009 Our results indicate that the main role of heparin in FGF-induced signaling is to protect this naturally unstable protein against heat and/or proteolytic degradation and that heparin is not essential for a direct FGF1-FGFR interaction and receptor activation. Heparin 43-50 fibroblast growth factor 1 Homo sapiens 54-57 18710495-4 2008 We found that the tagged FGF1s had affinities for heparin that were similar to that of the native form. Heparin 50-57 fibroblast growth factor 1 Homo sapiens 25-29 19400583-2 2009 The conformations of heparin derivatives, as models of HS, are altered via a change in the associated cations, and this can drastically modify their FGF signaling activities. Heparin 21-28 fibroblast growth factor 1 Homo sapiens 149-152 17066397-8 2006 These heparin chips aided in the discovery of novel, sulfated sequences that bind FGF, and in the determination of the structural requirements needed for recognition by using picomoles of protein on a single slide. Heparin 6-13 fibroblast growth factor 1 Homo sapiens 82-85 18441324-6 2008 We found that the integrin-binding site of FGF1 overlaps with the heparin-binding site but is distinct from the FGFR-binding site using docking simulation and mutagenesis. Heparin 66-73 fibroblast growth factor 1 Homo sapiens 43-47 18441324-7 2008 We identified an FGF1 mutant (R50E) that was defective in integrin binding but still bound to heparin and FGFR. Heparin 94-101 fibroblast growth factor 1 Homo sapiens 17-21 17981035-0 2008 Design, synthesis, FGF-1 binding, and molecular modeling studies of conformationally flexible heparin mimetic disaccharides. Heparin 94-101 fibroblast growth factor 1 Homo sapiens 19-24 17094138-9 2007 Both heparin and sucrose appear to enhance the thermal stability of FGF-1, although their effects on the phase diagram are quite distinct. Heparin 5-12 fibroblast growth factor 1 Homo sapiens 68-73 17094138-11 2007 Only heparin appears to protect FGF-1 from acid-induced unfolding to any extent. Heparin 5-12 fibroblast growth factor 1 Homo sapiens 32-37 16995857-3 2006 The use of this well defined synthetic heparin analogue has allowed us to perform a detailed NMR structural analysis of the heparin-FGF interaction, overcoming the limitations of NMR to deal with the high molecular mass and heterogeneity of the FGF-1 oligomers formed in the presence of natural heparin fragments. Heparin 39-46 fibroblast growth factor 1 Homo sapiens 132-135 16794256-7 2006 In contrast, SP-B mRNA abundance was increased by heparin in a dose- and sulfation-dependent manner when used in combination with FGF-1. Heparin 50-57 fibroblast growth factor 1 Homo sapiens 130-135 16766579-4 2006 Heparin was used because it participates in FGF-1 signaling. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 44-49 16995857-3 2006 The use of this well defined synthetic heparin analogue has allowed us to perform a detailed NMR structural analysis of the heparin-FGF interaction, overcoming the limitations of NMR to deal with the high molecular mass and heterogeneity of the FGF-1 oligomers formed in the presence of natural heparin fragments. Heparin 39-46 fibroblast growth factor 1 Homo sapiens 245-250 16995857-3 2006 The use of this well defined synthetic heparin analogue has allowed us to perform a detailed NMR structural analysis of the heparin-FGF interaction, overcoming the limitations of NMR to deal with the high molecular mass and heterogeneity of the FGF-1 oligomers formed in the presence of natural heparin fragments. Heparin 124-131 fibroblast growth factor 1 Homo sapiens 132-135 16995857-3 2006 The use of this well defined synthetic heparin analogue has allowed us to perform a detailed NMR structural analysis of the heparin-FGF interaction, overcoming the limitations of NMR to deal with the high molecular mass and heterogeneity of the FGF-1 oligomers formed in the presence of natural heparin fragments. Heparin 124-131 fibroblast growth factor 1 Homo sapiens 245-250 16995857-4 2006 Our results confirm that glycosaminoglycans induced FGF-1 dimerization either in a cis or trans disposition with respect to the heparin chain is not an absolute requirement for biological activity. Heparin 128-135 fibroblast growth factor 1 Homo sapiens 52-57 16937240-0 2006 Backbone dynamics of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue, by 15N NMR relaxation methods. Heparin 94-101 fibroblast growth factor 1 Homo sapiens 49-54 16417632-7 2006 RESULTS: Our results show that the binding of VEGF, FGF-1, and certain chemokines (SDF-1 and SLC) to immobilized heparin was abolished or greatly diminished by pre-treating the heparin with HSulf-2. Heparin 113-120 fibroblast growth factor 1 Homo sapiens 52-57 16223363-4 2006 In the present study, we demonstrate that, in the FGF (fibroblast growth factor)-FGFR (FGF receptor) system, multimers of the minimal complex composed of two FGF1 and two FGFR2 protomers can form on a single chain of the co-receptor heparin. Heparin 233-240 fibroblast growth factor 1 Homo sapiens 158-162 16223363-7 2006 However, the doublet of complexes appears to be less co-operative than the formation of the 2:2:1 FGF1:FGFR2:heparin complex, suggesting that this mechanism is one of a number of weaker interactions that might be involved in the formation of a focal complex on the cell surface. Heparin 109-116 fibroblast growth factor 1 Homo sapiens 98-102 16219767-0 2005 Cooperative dimerization of fibroblast growth factor 1 (FGF1) upon a single heparin saccharide may drive the formation of 2:2:1 FGF1.FGFR2c.heparin ternary complexes. Heparin 76-83 fibroblast growth factor 1 Homo sapiens 28-54 16417632-7 2006 RESULTS: Our results show that the binding of VEGF, FGF-1, and certain chemokines (SDF-1 and SLC) to immobilized heparin was abolished or greatly diminished by pre-treating the heparin with HSulf-2. Heparin 177-184 fibroblast growth factor 1 Homo sapiens 52-57 16219767-0 2005 Cooperative dimerization of fibroblast growth factor 1 (FGF1) upon a single heparin saccharide may drive the formation of 2:2:1 FGF1.FGFR2c.heparin ternary complexes. Heparin 76-83 fibroblast growth factor 1 Homo sapiens 56-60 16219767-0 2005 Cooperative dimerization of fibroblast growth factor 1 (FGF1) upon a single heparin saccharide may drive the formation of 2:2:1 FGF1.FGFR2c.heparin ternary complexes. Heparin 76-83 fibroblast growth factor 1 Homo sapiens 128-132 16219767-1 2005 The related glycosaminoglycans heparin and heparan sulfate are essential for the activity of the fibroblast growth factor (FGF) family as they form an integral part of the signaling complex at the cell surface. Heparin 31-38 fibroblast growth factor 1 Homo sapiens 123-126 16219767-6 2005 Heparin hexasaccharide and various selectively desulfated heparin dp12s failed to bind FGFR2c and could only interact with FGF1 monomerically. Heparin 58-65 fibroblast growth factor 1 Homo sapiens 123-127 16219767-8 2005 We found that FGF1 dimerization upon heparin was favored over monomeric interactions even when a large excess of saccharide was present. Heparin 37-44 fibroblast growth factor 1 Homo sapiens 14-18 15839662-1 2005 FGF-1 recognizes both the (1)C(4) and (2)S(O) conformations of a bioactive heparin-like hexasaccharide. Heparin 75-82 fibroblast growth factor 1 Homo sapiens 0-5 16126225-11 2005 A more detailed analysis of the biological behavior of stable FGF-1 mutants revealed that, compared with the wild-type, their mitogenic properties, as probed by the DNA synthesis assay, were significantly increased in the absence of heparin, and that their half-lives were extensively prolonged. Heparin 233-240 fibroblast growth factor 1 Homo sapiens 62-67 16173813-2 2005 Acid fibroblast growth factor (aFGF) in the presence of heparin was used as negatively charged polyelectrolytes, while poly(ethyleneimine) (PEI) was chosen as a positively charged counterpart. Heparin 56-63 fibroblast growth factor 1 Homo sapiens 31-35 16039522-3 2005 The minimum heparin binding sequence for FGF1 and FGF2 necessary to promote signaling was investigated. Heparin 12-19 fibroblast growth factor 1 Homo sapiens 41-45 15839662-2 2005 The first direct NMR determination of the conformation of a conformationally flexible heparin-like hexasaccharide bound to a key receptor, FGF-1, is described. Heparin 86-93 fibroblast growth factor 1 Homo sapiens 139-144 11724555-9 2001 In contrast, an FGF-1 affinity matrix enriched the fraction of crude heparin with low anti-factor Xa activity. Heparin 69-76 fibroblast growth factor 1 Homo sapiens 16-21 15767480-5 2005 Tyrosine phosphorylation of FGFR1 induced by FGF was examined by immunoprecipitation after stimulation with FGF-1 in the presence or absence of heparin. Heparin 144-151 fibroblast growth factor 1 Homo sapiens 28-31 15767480-9 2005 The FGFR1 was differentially phosphorylated in a time- and heparin-dependent manner by FGF-1. Heparin 59-66 fibroblast growth factor 1 Homo sapiens 87-92 15533444-7 2004 The apparent inserted regions are shown to be associated with heparin-binding functionality; however, despite a marked reduction in heparin-binding affinity the mutant form of FGF-1 is surprisingly approximately 70 times more potent in 3T3 fibroblast mitogenic assays. Heparin 62-69 fibroblast growth factor 1 Homo sapiens 176-181 15533444-7 2004 The apparent inserted regions are shown to be associated with heparin-binding functionality; however, despite a marked reduction in heparin-binding affinity the mutant form of FGF-1 is surprisingly approximately 70 times more potent in 3T3 fibroblast mitogenic assays. Heparin 132-139 fibroblast growth factor 1 Homo sapiens 176-181 14502551-5 2003 The diversity of heparin-binding motifs within the large FGF family of polypeptides and receptors provides a repertoire of diverse templates for capture of diverse heparin/heparan sulfate motifs in biology. Heparin 17-24 fibroblast growth factor 1 Homo sapiens 57-60 14502551-5 2003 The diversity of heparin-binding motifs within the large FGF family of polypeptides and receptors provides a repertoire of diverse templates for capture of diverse heparin/heparan sulfate motifs in biology. Heparin 164-171 fibroblast growth factor 1 Homo sapiens 57-60 14502551-6 2003 We show here that, similar to antithrombin, a member of the FGF family, FGF7, selectively captures anti-Factor Xa and anti-Factor IIa activity from commercially and clinically applied heparin mixtures. Heparin 184-191 fibroblast growth factor 1 Homo sapiens 60-63 12756357-0 2003 R136K fibroblast growth factor-1 mutant induces heparin-independent migration of endothelial cells through fibrin glue. Heparin 48-55 fibroblast growth factor 1 Homo sapiens 6-32 12756357-15 2003 CONCLUSION: Site-directed mutagenesis of FGF-1 to R136K enables induction of heparin-independent migration of EC through fibrin glue at an optimal concentration of 100 ng/mL. Heparin 77-84 fibroblast growth factor 1 Homo sapiens 41-46 12656349-2 2003 Heparin is generally thought to play an extremely important role in regulating aFGF and bFGF bioactivities through its strong binding with them. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 79-83 12656349-9 2003 These methods established here can be used for analysing the effect of sulfate groups in heparin on the binding with other human FGF members or other heparin-binding proteins. Heparin 89-96 fibroblast growth factor 1 Homo sapiens 129-132 12059036-3 2002 Acidic fibroblast growth factor (aFGF) belongs to a family of growth factors that show a high affinity for heparin sulfate proteoglycans. Heparin 107-114 fibroblast growth factor 1 Homo sapiens 0-31 12059036-3 2002 Acidic fibroblast growth factor (aFGF) belongs to a family of growth factors that show a high affinity for heparin sulfate proteoglycans. Heparin 107-114 fibroblast growth factor 1 Homo sapiens 33-37 12115937-5 2002 Wound epithelium thickened when recombinant newt FGF-1 was provided on heparin-coated beads, demonstrating that the FGF-1 was biologically active and that the wound epithelium is a possible target tissue of FGF. Heparin 71-78 fibroblast growth factor 1 Homo sapiens 49-54 12115937-5 2002 Wound epithelium thickened when recombinant newt FGF-1 was provided on heparin-coated beads, demonstrating that the FGF-1 was biologically active and that the wound epithelium is a possible target tissue of FGF. Heparin 71-78 fibroblast growth factor 1 Homo sapiens 116-121 11890696-0 2002 Minimal heparin/heparan sulfate sequences for binding to fibroblast growth factor-1. Heparin 8-15 fibroblast growth factor 1 Homo sapiens 57-83 11890696-1 2002 The glycosaminoglycans heparin and heparan sulfate (HS) bind to fibroblast growth factor FGF1 and promote its dimerization, a proposed prerequisite for binding to a cellular receptor and triggering mitogenic signals. Heparin 23-30 fibroblast growth factor 1 Homo sapiens 89-93 11890696-5 2002 Furthermore, MALDI experiments show that, in addition to 1:1 protein:tetrasaccharide complexes, AA and BA are able to form 2:1 complexes, indicating that heparin/HS-induced dimerization of FGF1 requires only one 6-OSO(3) group per tetrasaccharide. Heparin 154-161 fibroblast growth factor 1 Homo sapiens 189-193 11714710-7 2002 In addition, both 6-O- and 2-O-desulfated heparin activated FGF-1 signaling via FGFR2 IIIb, whereas neither one stimulated FGF-1 signaling via FGFR1 or FGF-7 via FGFR2 IIIb. Heparin 42-49 fibroblast growth factor 1 Homo sapiens 60-65 14657241-4 2004 We found that FGF-2 translocation occurred in endothelial cells and fibroblasts, which express FGF receptors, and that the efficiency of translocation was increased in the presence of heparin. Heparin 184-191 fibroblast growth factor 1 Homo sapiens 14-17 14695513-1 2004 Six synthetic heparin-like oligosaccharides have been used to investigate the effect of the oligosaccharide sulfation pattern on the stimulation of acidic fibroblast growth factor (FGF-1) induced mitogenesis signaling and the biological significance of FGF-1 trans dimerization in the FGF-1 activation process. Heparin 14-21 fibroblast growth factor 1 Homo sapiens 181-186 12692004-4 2003 The FGF-1/oxLDL complex had a dramatically decreased ability to bind heparin and was nonmitogenic on cultured smooth muscle cells. Heparin 69-76 fibroblast growth factor 1 Homo sapiens 4-9 12484774-7 2002 Among the 12 beta-strands constituting the beta-barrel architecture of hFGF-1, beta-strand XI, located in the heparin binding domain, exhibits the lowest average protection factor value. Heparin 110-117 fibroblast growth factor 1 Homo sapiens 71-77 11724555-4 2001 In contrast, a decrease and dispersion of the positive surface charge density characterized the heparin-binding domain of FGF-7 defined by homology to that of FGF-1 and FGF-2 in complexes with heparin. Heparin 96-103 fibroblast growth factor 1 Homo sapiens 159-164 11724555-4 2001 In contrast, a decrease and dispersion of the positive surface charge density characterized the heparin-binding domain of FGF-7 defined by homology to that of FGF-1 and FGF-2 in complexes with heparin. Heparin 193-200 fibroblast growth factor 1 Homo sapiens 159-164 11043400-3 2000 CECs grown in the presence of ECGF and its cofactor heparin exhibit an epithelial-like morphology (type I CECs). Heparin 52-59 fibroblast growth factor 1 Homo sapiens 30-34 11828504-6 2001 Both compounds 1 and 2 induce the mitogenic activity of acid fibroblast growth factor (FGF1), with the half-maximum activating concentration of 2 being equivalent to that of heparin. Heparin 174-181 fibroblast growth factor 1 Homo sapiens 87-91 11828504-7 2001 Sedimentation equilibrium analysis with compound 2 suggests that heparin-induced FGF1 dimerization is not an absolute requirement for biological activity. Heparin 65-72 fibroblast growth factor 1 Homo sapiens 81-85 11241127-1 2001 OBJECTIVE: Cardiovascular tissue engineering approaches to vessel wall restoration have focused on the potent but relatively nonspecific and heparin-dependent mesenchymal cell mitogen fibroblast growth factor 1 (FGF-1). Heparin 141-148 fibroblast growth factor 1 Homo sapiens 184-210 11241127-1 2001 OBJECTIVE: Cardiovascular tissue engineering approaches to vessel wall restoration have focused on the potent but relatively nonspecific and heparin-dependent mesenchymal cell mitogen fibroblast growth factor 1 (FGF-1). Heparin 141-148 fibroblast growth factor 1 Homo sapiens 212-217 11241127-7 2001 RESULTS: In the presence of heparin the HB-GAM/FGF-1 chimera stimulated less SMC proliferation than did the wild-type FGF-1 with a median effective dose of approximately 0.3 nmol versus approximately 0.1 nmol (P <.001). Heparin 28-35 fibroblast growth factor 1 Homo sapiens 47-52 11241127-11 2001 CONCLUSIONS: The HB-GAM/FGF-1 chimera displays significantly greater and uniquely heparin-independent mitogenic activity for both cell types, and in the presence of heparin it displays a significantly greater EC specificity. Heparin 82-89 fibroblast growth factor 1 Homo sapiens 24-29 11457455-4 2001 We have analysed the sequences of worm and fly FGFs and FGFRs and used the recently determined crystal structure of the human FGF1-FGFR2-heparin ternary complex [Pellegrini, L., Burke, D.F., von Delft, F., Mulloy, B. and Blundell, T.L. Heparin 137-144 fibroblast growth factor 1 Homo sapiens 126-130 11087710-1 2000 The interaction of heparan sulfate (HS) (and the closely related molecule heparin) with FGF-1 is a requirement for enabling the growth factor to activate its cell surface tyrosine kinase receptor. Heparin 74-81 fibroblast growth factor 1 Homo sapiens 88-93 11069186-6 2000 The complex is assembled around a central heparin molecule linking two FGF1 ligands into a dimer that bridges between two receptor chains. Heparin 42-49 fibroblast growth factor 1 Homo sapiens 71-75 11069186-7 2000 The asymmetric heparin binding involves contacts with both FGF1 molecules but only one receptor chain. Heparin 15-22 fibroblast growth factor 1 Homo sapiens 59-63 11069186-8 2000 The structure of the FGF1-FGFR2-heparin ternary complex provides a structural basis for the essential role of heparan sulphate in FGF signalling. Heparin 32-39 fibroblast growth factor 1 Homo sapiens 21-25 10852713-4 2000 Mutant forms of FGF-1 that substitute a serine residue at these cysteine positions have been reported to increase the protein"s half-life and specific activity as well as decrease the dependence upon heparin for full activity. Heparin 200-207 fibroblast growth factor 1 Homo sapiens 16-21 10664506-2 2000 S130K is a mutation of fibroblast growth factor-1 (FGF-1), with lysine replacing serine in the heparin-binding site. Heparin 95-102 fibroblast growth factor 1 Homo sapiens 23-49 10835602-8 2000 By constructing a biologically active proteoglycan-FGF-1 fusion protein, we have demonstrated an approach that may prove effective for engineering not only FGF family members, but other HP-binding molecules as well. Heparin 186-188 fibroblast growth factor 1 Homo sapiens 51-56 10860838-3 2000 Here we show that when both isolated FGFR2betaIIIb and FGFR2betaIIIc or their common Ig module II are allowed to affinity select heparin from a mixture, the resultant binary complexes bound FGF-1, FGF-2, and FGF-7 with nearly equal affinity. Heparin 129-136 fibroblast growth factor 1 Homo sapiens 190-195 11032250-1 2000 Acid fibroblast growth factor (aFGF) binds to its cell-surface receptors in a heparin-dependent manner. Heparin 78-85 fibroblast growth factor 1 Homo sapiens 31-35 11032250-3 2000 To retain the natural conformation of aFGF during screening, we used biotinylated heparin to immobilize aFGF on a streptavidin-coated dish. Heparin 82-89 fibroblast growth factor 1 Homo sapiens 104-108 10664506-2 2000 S130K is a mutation of fibroblast growth factor-1 (FGF-1), with lysine replacing serine in the heparin-binding site. Heparin 95-102 fibroblast growth factor 1 Homo sapiens 51-56 10664506-9 2000 S130K is also significantly more potent than FGF-1 in the presence of heparin. Heparin 70-77 fibroblast growth factor 1 Homo sapiens 45-50 10664506-16 2000 CONCLUSIONS: Site-directed mutagenesis changed the potency and the heparin dependency on cellular proliferation of FGF-1 in vitro. Heparin 67-74 fibroblast growth factor 1 Homo sapiens 115-120 10561907-7 1999 The addition of heparin to cultures stimulated by FGF-1 or FGF-2 resulted in a 2-fold increase in the number of megakaryocyte colonies compared to the culture containing FGF alone. Heparin 16-23 fibroblast growth factor 1 Homo sapiens 50-55 10413500-0 1999 Site-directed mutagenesis and molecular modeling identify a crucial amino acid in specifying the heparin affinity of FGF-1. Heparin 97-104 fibroblast growth factor 1 Homo sapiens 117-122 10413500-1 1999 Heparin potentiates the mitogenic activity of FGF-1 by increasing the affinity for its receptor and by extending its biological half-life. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 46-51 10413500-2 1999 During the course of labeling human FGF-1 with Na(125)I and chloramine T, it was observed that the protein lost its ability to bind to heparin. Heparin 135-142 fibroblast growth factor 1 Homo sapiens 36-41 10413500-5 1999 The results showed that the C-terminal region of human FGF-1 was responsible for the loss of heparin affinity. Heparin 93-100 fibroblast growth factor 1 Homo sapiens 55-60 10413500-9 1999 In contrast, a mutant human FGF-1 that has cysteine-131 replaced with serine (C131S) was able to bind to heparin even after iodination while bovine FGF-1 (S131C) lost its binding affinity to heparin upon iodination. Heparin 105-112 fibroblast growth factor 1 Homo sapiens 28-33 10413500-9 1999 In contrast, a mutant human FGF-1 that has cysteine-131 replaced with serine (C131S) was able to bind to heparin even after iodination while bovine FGF-1 (S131C) lost its binding affinity to heparin upon iodination. Heparin 191-198 fibroblast growth factor 1 Homo sapiens 28-33 10413500-11 1999 Molecular modeling showed that the heparin-binding domain of FGF-1 includes cysteine-131 and that cysteine-131, upon oxidation to cysteic acid during the iodination procedures, would interact with lysine-126 and lysine-132. Heparin 35-42 fibroblast growth factor 1 Homo sapiens 61-66 10226073-14 1999 These findings demonstrate that FGF-1, mostly in the presence of heparin, upregulates collagenase and downregulates type I collagen expression that might have a protective role in avoiding collagen accumulation during lung ECM remodeling. Heparin 65-72 fibroblast growth factor 1 Homo sapiens 32-37 10404599-0 1999 A dimeric ternary complex of FGFR [correction of FGFR1], heparin and FGF-1 leads to an "electrostatic sandwich" model for heparin binding. Heparin 122-129 fibroblast growth factor 1 Homo sapiens 69-74 10226073-4 1999 Heparin was used because it enhances the biologic activities of FGF-1. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 64-69 10336501-4 1999 Cell-free complexes of heparin and recombinant FGFR4 bound FGF-1 and FGF-2 equally. Heparin 23-30 fibroblast growth factor 1 Homo sapiens 59-64 9755102-4 1998 Desulfated heparin significantly elevated FGF-1- and FGF-2-stimulated DNA synthesis, whereas desulfated CS and N-desulfated heparin elevated FGF-7-stimulated DNA synthesis by type II cells on laminin substrata. Heparin 11-18 fibroblast growth factor 1 Homo sapiens 42-47 10070748-5 1999 From the chemical shift differences between free aFGF and aFGF-heparin complex, we concluded that the major heparin binding site was located on the regions 110-131 and 17-21. Heparin 63-70 fibroblast growth factor 1 Homo sapiens 58-62 10070748-5 1999 From the chemical shift differences between free aFGF and aFGF-heparin complex, we concluded that the major heparin binding site was located on the regions 110-131 and 17-21. Heparin 108-115 fibroblast growth factor 1 Homo sapiens 49-53 10070748-5 1999 From the chemical shift differences between free aFGF and aFGF-heparin complex, we concluded that the major heparin binding site was located on the regions 110-131 and 17-21. Heparin 108-115 fibroblast growth factor 1 Homo sapiens 58-62 9843417-2 1998 In the presence of heparin, FGF-1 binds and activates in vitro all FGFR subtypes, while FGF-7 exhibits absolute specificity for the IIIb splice variant of FGFR2. Heparin 19-26 fibroblast growth factor 1 Homo sapiens 28-33 10226073-8 1999 Our results show that FGF-1 induced collagenase mRNA expression, which was strongly enhanced when FGF-1 was used with heparin. Heparin 118-125 fibroblast growth factor 1 Homo sapiens 22-27 10226073-8 1999 Our results show that FGF-1 induced collagenase mRNA expression, which was strongly enhanced when FGF-1 was used with heparin. Heparin 118-125 fibroblast growth factor 1 Homo sapiens 98-103 10051565-0 1999 Fibroblast growth factors 1 and 2 are distinct in oligomerization in the presence of heparin-like glycosaminoglycans. Heparin 85-92 fibroblast growth factor 1 Homo sapiens 0-33 9700949-1 1998 The fibroblast growth factor (FGF) family is a group of homologous heparin-binding polypeptides that has been implicated in a variety of human neoplasms and presently includes 14 members. Heparin 67-74 fibroblast growth factor 1 Homo sapiens 30-33 24194252-3 1996 Western blot analysis of these heparin-binding fractions was carried out using monoclonal antibodies against human acidic and basic fibroblast growth factors (FGF-1 and-2). Heparin 31-38 fibroblast growth factor 1 Homo sapiens 159-170 9466688-8 1997 Differences in response to heparin and alterations in the BULK heparan sulfate content of cells likely reflect FGF-specific differences in the cellular repertoire of multivalent heparan sulfate chains required for assembly and activation of the FGF signal transduction complex. Heparin 27-34 fibroblast growth factor 1 Homo sapiens 111-114 9288226-4 1997 Both aFGF and bFGF, each with a molecular weight of 18 kDa, were identified in PA using heparin-sepharose chromatography and Western blot analysis. Heparin 88-95 fibroblast growth factor 1 Homo sapiens 5-9 8878902-0 1996 Potentiation of the growth-stimulatory effects of aFGF by heparin in Rama 27 fibroblasts. Heparin 58-65 fibroblast growth factor 1 Homo sapiens 50-54 9600090-8 1998 In the presence of exogenous heparin, the mitogenic activity of ovine FGF-1 is potentiated slightly. Heparin 29-36 fibroblast growth factor 1 Homo sapiens 70-75 8900171-3 1996 Concurrent with a marked increase in dependence on exogenous heparin for optimal activity, sequential deletion of residues in the NYKKPKL sequence in FGF-1 resulted in a progressive loss of thermal stability, resistance to protease, mitogenic activity, and affinity for the transmembrane receptor. Heparin 61-68 fibroblast growth factor 1 Homo sapiens 150-155 8900171-5 1996 In the presence of sufficiently high concentrations of heparin, the deletion mutants exhibited mitogenic activity equal to wild-type FGF-1. Heparin 55-62 fibroblast growth factor 1 Homo sapiens 133-138 8591858-1 1996 Although fibroblast growth factor 1 (FGF-1) (formerly known as acidic FGF) but not FGF-2 (or basic FGF), has been suggested to play a pathophysiological role in liver regeneration, its clinical application has been restricted by its limited mitogenecity and heparin dependence. Heparin 258-265 fibroblast growth factor 1 Homo sapiens 9-35 8613463-2 1996 Acidic fibroblast growth factor (aFGF) in the presence of heparin has effects opposite to IL-1 on cultured human umbilical vein endothelial cells (HUVEC); therefore, we have investigated the modulation of IL-1-induced effects by the c combination of aFGF and heparin (aFGF/heparin). Heparin 58-65 fibroblast growth factor 1 Homo sapiens 0-31 8613463-2 1996 Acidic fibroblast growth factor (aFGF) in the presence of heparin has effects opposite to IL-1 on cultured human umbilical vein endothelial cells (HUVEC); therefore, we have investigated the modulation of IL-1-induced effects by the c combination of aFGF and heparin (aFGF/heparin). Heparin 58-65 fibroblast growth factor 1 Homo sapiens 33-37 8591858-1 1996 Although fibroblast growth factor 1 (FGF-1) (formerly known as acidic FGF) but not FGF-2 (or basic FGF), has been suggested to play a pathophysiological role in liver regeneration, its clinical application has been restricted by its limited mitogenecity and heparin dependence. Heparin 258-265 fibroblast growth factor 1 Homo sapiens 37-42 9070372-3 1996 The potentiating activity of heparin upon FGF-1 has shown to be dependent on the oligosaccharide size, degree of sulfation and carboxylation. Heparin 29-36 fibroblast growth factor 1 Homo sapiens 42-47 7493920-7 1995 Heparin inhibits the association between FGF-1 and PS, and synthetic peptide competition assays suggest that the PS-binding domain of FGF-1 lies between residues 114 and 137. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 41-46 7493920-7 1995 Heparin inhibits the association between FGF-1 and PS, and synthetic peptide competition assays suggest that the PS-binding domain of FGF-1 lies between residues 114 and 137. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 134-139 7537691-3 1995 Cross-linking experiments reveal that binding of FGF-1 to the hepatocyte cell surface receptors can be accomplished in the absence of exogenous heparin, in contrast to human endothelial cells for which it remains as a limiting factor. Heparin 144-151 fibroblast growth factor 1 Homo sapiens 49-54 7592764-8 1995 The heparin-binding peptide could antagonize the mitogenic activity of FGF-1, probably because of the heparin dependence of this activity. Heparin 4-11 fibroblast growth factor 1 Homo sapiens 71-76 7592764-9 1995 Together these data demonstrate that the heparin binding properties of fibroblast growth factor-1 are dictated by structural features more complex than clusters of basic amino acids. Heparin 41-48 fibroblast growth factor 1 Homo sapiens 71-97 7845032-7 1995 We found that two cell lines were responsive to bFGF in different biological assays: (i) in K562 myeloid cells induced to differentiate by hemin, preincubation with bFGF and heparin increased cell viability and decreased hemin-induced DNA fragmentation, without affecting erythroid differentiation; and (ii) in U937 monocytic cells, the production of plasminogen activator was increased by bFGF or aFGF in combination with heparin. Heparin 174-181 fibroblast growth factor 1 Homo sapiens 398-402 7536241-4 1995 Native, non-deamidated aFGF (complexed with heparin) has a half-life of 16 weeks at pH 7, 30 degrees C, and 4 weeks at pH 8, 40 degrees C. The mitogenic activity and biophysical properties of deamidated aFGF were compared to the non-deamidated protein. Heparin 44-51 fibroblast growth factor 1 Homo sapiens 23-27 8679245-6 1995 Heparin potentiated the mitogenic and metabolic effects of both bFGF and aFGF. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 73-77 7694075-0 1993 Mitogenic activity of acidic fibroblast growth factor is enhanced by highly sulfated oligosaccharides derived from heparin and heparan sulfate. Heparin 115-122 fibroblast growth factor 1 Homo sapiens 22-53 7537556-0 1994 Structural requirements in heparin for binding and activation of FGF-1 and FGF-4 are different from that for FGF-2. Heparin 27-34 fibroblast growth factor 1 Homo sapiens 65-70 7514646-9 1994 aFGF (20 ng/ml) plus heparin (17 micrograms/ml) induced a maximal 30-kDa increase at 8 h, which stayed stable for up to 24 h. The effect of aFGF was concentration dependent. Heparin 21-28 fibroblast growth factor 1 Homo sapiens 140-144 8175651-9 1994 Both bFGF and aFGF inhibited the binding when low concentrations of heparin were added to the binding reaction. Heparin 68-75 fibroblast growth factor 1 Homo sapiens 14-18 7528103-3 1994 Heparin exerts its effect by binding to many molecules of aFGF. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 58-62 7528103-4 1994 The resulting aFGF-heparin complex can bind to several receptor molecules, leading to FGFR dimerization. Heparin 19-26 fibroblast growth factor 1 Homo sapiens 14-18 7528103-6 1994 Moreover, a synthetic heparin analog that binds monovalently to aFGF blocks FGFR dimerization, activation, and signaling via FGFR. Heparin 22-29 fibroblast growth factor 1 Homo sapiens 64-68 7528103-7 1994 We propose that heparin causes oligomerization of aFGF such that its binding to FGFR results in dimerization and activation. Heparin 16-23 fibroblast growth factor 1 Homo sapiens 50-54 7507851-7 1994 Although basic FGF showed little activity on rat hepatocytes, acidic FGF stimulated DNA synthesis by approximately twofold and was substantially enhanced by heparin. Heparin 157-164 fibroblast growth factor 1 Homo sapiens 69-72 7530465-1 1994 The fluorescence emission of a single tryptophan residue present in both FGF-1 and FGF-2 was used as a structural probe to directly assess the interaction of the growth factors with heparin or beta-cyclodextran tetradecasulfate. Heparin 182-189 fibroblast growth factor 1 Homo sapiens 73-78 7530465-4 1994 The equilibrium dissociation constants, determined by this method, for heparin or beta-cyclodextrin tetradecasulfate binding to FGF-1 are about 1 nM, whereas the values for FGF-2 are 1 and 23 nM, respectively. Heparin 71-78 fibroblast growth factor 1 Homo sapiens 128-133 7692970-6 1993 Similar to the well-described interaction and stabilization of aFGF by heparin, soluble sucrose octasulfate (SOS) stabilizes aFGF against thermal, urea and acidic pH-induced unfolding as determined by a combination of circular dichroism, fluorescence spectroscopy and differential scanning calorimetry. Heparin 71-78 fibroblast growth factor 1 Homo sapiens 63-67 7692970-8 1993 SOS competes with heparin and suramin for the aFGF polyanion binding site as measured by both fluorescence and light scattering based competitive binding assays. Heparin 18-25 fibroblast growth factor 1 Homo sapiens 46-50 7694075-1 1993 The mitogenic activity of acidic fibroblast growth factor (aFGF) is potentiated by the highly sulfated hexasaccharide [IdoUA,2S-GlcNS,6S]2-[GlcUA-GlcNS,6S] the structural repetitive unit of lung heparin chains. Heparin 195-202 fibroblast growth factor 1 Homo sapiens 26-57 7694075-1 1993 The mitogenic activity of acidic fibroblast growth factor (aFGF) is potentiated by the highly sulfated hexasaccharide [IdoUA,2S-GlcNS,6S]2-[GlcUA-GlcNS,6S] the structural repetitive unit of lung heparin chains. Heparin 195-202 fibroblast growth factor 1 Homo sapiens 59-63 7684608-0 1993 Nature of the interaction of heparin with acidic fibroblast growth factor. Heparin 29-36 fibroblast growth factor 1 Homo sapiens 42-73 7686045-3 1993 The presence of equimolar or greater amounts of heparin stabilizes aFGF from unfolding by more than 2.5 kcal mol-1 and slows the rate of unfolding by greater than 2000-fold. Heparin 48-55 fibroblast growth factor 1 Homo sapiens 67-71 7686045-4 1993 The ability of heparin to stabilize aFGF is critically dependent upon many factors including the number of aFGF molecules bound to the heparin chain, ionic strength, temperature, and the extent of sulfation of the polysaccharide. Heparin 15-22 fibroblast growth factor 1 Homo sapiens 36-40 7686045-4 1993 The ability of heparin to stabilize aFGF is critically dependent upon many factors including the number of aFGF molecules bound to the heparin chain, ionic strength, temperature, and the extent of sulfation of the polysaccharide. Heparin 15-22 fibroblast growth factor 1 Homo sapiens 107-111 7686045-4 1993 The ability of heparin to stabilize aFGF is critically dependent upon many factors including the number of aFGF molecules bound to the heparin chain, ionic strength, temperature, and the extent of sulfation of the polysaccharide. Heparin 135-142 fibroblast growth factor 1 Homo sapiens 36-40 7686045-4 1993 The ability of heparin to stabilize aFGF is critically dependent upon many factors including the number of aFGF molecules bound to the heparin chain, ionic strength, temperature, and the extent of sulfation of the polysaccharide. Heparin 135-142 fibroblast growth factor 1 Homo sapiens 107-111 7686045-6 1993 Additional experiments demonstrate that increasing charge density enhances the ability of polyanions such as sulfated beta-cyclodextrins, phosphorylated inositols, and modified heparins to protect aFGF from urea-induced unfolding. Heparin 177-185 fibroblast growth factor 1 Homo sapiens 197-201 7684608-2 1993 Static and dynamic light scattering as well as analytical ultracentrifugation analyses indicates that 14-15 molecules of a FGF can bind to a 16-kDa heparin chain, with approximately 10 of these bound relatively uniformly to high-affinity sites. Heparin 148-155 fibroblast growth factor 1 Homo sapiens 123-126 7684608-3 1993 The dissociation constants of these latter sites are estimated to be approximately 50-140 nM on the basis of surface plasmon resonance experiments in which the association and dissociation rates of aFGF interaction with immobilized heparin were measured. Heparin 232-239 fibroblast growth factor 1 Homo sapiens 198-202 7684608-4 1993 The size of the binding site of a FGF on heparin was also determined by heparin lyase digestion of a FGF/heparin complexes followed by isolation and characterization of protected oligosaccharides. Heparin 41-48 fibroblast growth factor 1 Homo sapiens 34-37 7684608-4 1993 The size of the binding site of a FGF on heparin was also determined by heparin lyase digestion of a FGF/heparin complexes followed by isolation and characterization of protected oligosaccharides. Heparin 41-48 fibroblast growth factor 1 Homo sapiens 101-104 7684608-4 1993 The size of the binding site of a FGF on heparin was also determined by heparin lyase digestion of a FGF/heparin complexes followed by isolation and characterization of protected oligosaccharides. Heparin 72-79 fibroblast growth factor 1 Homo sapiens 34-37 7684608-6 1993 Thus, aFGF appears to bind at high density (one molecule every 4-5 polysaccharide units) and with high affinity to heparin. Heparin 115-122 fibroblast growth factor 1 Homo sapiens 6-10 1383494-8 1992 Pretreatment of NFlg26 cell membranes with pertussis toxin resulted in a heparin-dependent decrease in the binding affinity (Kd values of 0.57-1.15 nM) of [125I]aFGF. Heparin 73-80 fibroblast growth factor 1 Homo sapiens 161-165 7678726-1 1993 Acidic fibroblast growth factor (aFGF) is markedly stabilized by heparin. Heparin 65-72 fibroblast growth factor 1 Homo sapiens 0-31 7678726-1 1993 Acidic fibroblast growth factor (aFGF) is markedly stabilized by heparin. Heparin 65-72 fibroblast growth factor 1 Homo sapiens 33-37 7678726-8 1993 A tetrasaccharide fragment of heparin is the smallest unit of heparin capable of stabilizing aFGF against thermal denaturation. Heparin 30-37 fibroblast growth factor 1 Homo sapiens 93-97 7678726-8 1993 A tetrasaccharide fragment of heparin is the smallest unit of heparin capable of stabilizing aFGF against thermal denaturation. Heparin 62-69 fibroblast growth factor 1 Homo sapiens 93-97 7678726-10 1993 These results are discussed in the context of a model of human aFGF based on the X-ray crystal structure of the bovine protein and previous studies by others of the heparin binding site of both acidic and basic FGF. Heparin 165-172 fibroblast growth factor 1 Homo sapiens 63-67 7678726-10 1993 These results are discussed in the context of a model of human aFGF based on the X-ray crystal structure of the bovine protein and previous studies by others of the heparin binding site of both acidic and basic FGF. Heparin 165-172 fibroblast growth factor 1 Homo sapiens 64-67 7688519-5 1993 However, if heparin was present during the chase, readily detectable amounts (about 10-20% of total) of aFGF were found in the medium during the 15 hr chase. Heparin 12-19 fibroblast growth factor 1 Homo sapiens 104-108 7688519-8 1993 Further analyses indicated that heparin both stabilized the protein from degradation and prevented the binding of released aFGF to extracellular heparan-sulfate proteoglycans. Heparin 32-39 fibroblast growth factor 1 Homo sapiens 123-127 7688519-9 1993 Thus, both factors contributed to the increased recovery of aFGF in the presence of heparin. Heparin 84-91 fibroblast growth factor 1 Homo sapiens 60-64 1280262-10 1992 Heparin or HS glycosaminoglycans are a prerequisite for the FGF receptor encoded by flg gene to bind basic FGF (Yayon, A., Klagsbrun, M., Esko, J. D., Leder, P., and Ornitz, D. M. (1991) Cell 64, 841-848). Heparin 0-7 fibroblast growth factor 1 Homo sapiens 60-63 7678885-7 1993 These results support the promising angiogenic effect of ECGF-heparin in previously irradiated surgical wounds. Heparin 62-69 fibroblast growth factor 1 Homo sapiens 57-61 1279690-6 1992 The form of FGF-1 exposed by ammonium sulfate fractionation is similar in size to cytosolic FGF-1 and can bind and be eluted from immobilized heparin similarly to the recombinant human FGF-1 polypeptide. Heparin 142-149 fibroblast growth factor 1 Homo sapiens 12-17 1383494-2 1992 In the presence of 5 U/ml of heparin to block [125I]aFGF binding to membrane bound heparan sulfate proteoglycans, specific [125I]aFGF binding was optimal in the presence of 0.2 M NaCl and in a pH range of 7 to 9. Heparin 29-36 fibroblast growth factor 1 Homo sapiens 52-56 1383494-2 1992 In the presence of 5 U/ml of heparin to block [125I]aFGF binding to membrane bound heparan sulfate proteoglycans, specific [125I]aFGF binding was optimal in the presence of 0.2 M NaCl and in a pH range of 7 to 9. Heparin 29-36 fibroblast growth factor 1 Homo sapiens 129-133 1383494-7 1992 Additional saturation studies, conducted in the presence of a lower (0.1 U/ml) heparin concentration, indicated that [125I] aFGF labeled both the high affinity (Kd = 0.02 nM) FGF-flg receptor and a separate class of lower affinity (Kd = 2 nM) recognition sites. Heparin 79-86 fibroblast growth factor 1 Homo sapiens 124-128 1383494-10 1992 Guanine nucleotides were also found to significantly reduce 0.1 nM [125I]aFGF binding in a heparin-dependent fashion. Heparin 91-98 fibroblast growth factor 1 Homo sapiens 73-77 1383494-11 1992 The present data demonstrate that, in the presence of heparin, [125I]aFGF binds with high affinity to the cloned FGF-flg receptor on NFlg26 cell membranes. Heparin 54-61 fibroblast growth factor 1 Homo sapiens 69-73 1383494-12 1992 However, at a low heparin concentration (0.1 U/ml), [125I]aFGF binds to the FGF-flg receptor with higher affinity than was observed in the presence of 5 U/ml of heparin, and also binds a class of lower affinity recognition sites which are consistent with the labeling of cell surface heparan sulfate proteoglycans. Heparin 18-25 fibroblast growth factor 1 Homo sapiens 58-62 1383494-12 1992 However, at a low heparin concentration (0.1 U/ml), [125I]aFGF binds to the FGF-flg receptor with higher affinity than was observed in the presence of 5 U/ml of heparin, and also binds a class of lower affinity recognition sites which are consistent with the labeling of cell surface heparan sulfate proteoglycans. Heparin 161-168 fibroblast growth factor 1 Homo sapiens 58-62 1375939-7 1992 Further, in contrast to FGF-1 monomers, which dissociate from immobilized heparin in 1.0 M NaCl, preformed FGF-1 homodimers had reduced apparent affinity for immobilized heparin and eluted at 0.4 M NaCl. Heparin 170-177 fibroblast growth factor 1 Homo sapiens 107-112 1390688-9 1992 In the case of aFGF, suramin interacts at or near its heparin binding site. Heparin 54-61 fibroblast growth factor 1 Homo sapiens 15-19 1375939-9 1992 Heparin appeared to modulate the formation of copper-induced intermolecular disulfide bonds for FGF-1 but not FGF-2, since co-incubation of heparin and copper with FGF-1 monomers resulted in dimers and other oligomeric complexes. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 96-101 1375939-9 1992 Heparin appeared to modulate the formation of copper-induced intermolecular disulfide bonds for FGF-1 but not FGF-2, since co-incubation of heparin and copper with FGF-1 monomers resulted in dimers and other oligomeric complexes. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 164-169 1375939-9 1992 Heparin appeared to modulate the formation of copper-induced intermolecular disulfide bonds for FGF-1 but not FGF-2, since co-incubation of heparin and copper with FGF-1 monomers resulted in dimers and other oligomeric complexes. Heparin 140-147 fibroblast growth factor 1 Homo sapiens 96-101 1375939-9 1992 Heparin appeared to modulate the formation of copper-induced intermolecular disulfide bonds for FGF-1 but not FGF-2, since co-incubation of heparin and copper with FGF-1 monomers resulted in dimers and other oligomeric complexes. Heparin 140-147 fibroblast growth factor 1 Homo sapiens 164-169 1509415-5 1992 It has been postulated that heparin acts by potentiating the effect of ECGF, but heparin inhibited thrombospondin release and enhanced that of von Willebrand factor in the absence of ECGS, while ECGS alone inhibited release of plasminogen activator inhibitor. Heparin 28-35 fibroblast growth factor 1 Homo sapiens 71-75 1721064-3 1991 In contrast, the endothelial cell mitogen, heparin-binding (acidic fibroblast) growth factor-1 (HBGF-1) inhibits the synthesis of prostacyclin in HUVEC. Heparin 43-50 fibroblast growth factor 1 Homo sapiens 96-102 1382772-6 1992 aFGF alone accelerated lesion coverage and this effect was enhanced by 40% over control values when heparin was added with aFGF. Heparin 100-107 fibroblast growth factor 1 Homo sapiens 0-4 1721051-4 1991 When heparin, inositol hexasulfate, or sulfate ion are present, aFGF refolds below 30 degrees C with a slightly reduced activation energy (10-11 kcal/mol). Heparin 5-12 fibroblast growth factor 1 Homo sapiens 64-68 1721064-7 1991 Further, HBGF-1, in the presence of heparin, down-regulates the levels of the Cox transcript in a dose- and time-dependent manner. Heparin 36-43 fibroblast growth factor 1 Homo sapiens 9-15 1885605-2 1991 This protein, designated HBp17, was found to bind the heparin-binding peptide growth factors HBGF-1 and HBGF-2 in a noncovalent, reversible manner. Heparin 54-61 fibroblast growth factor 1 Homo sapiens 93-99 1885605-4 1991 Both the binding and inactivation of HBGF-1 and HBGF-2 by HBp17 were abolished by heparin. Heparin 82-89 fibroblast growth factor 1 Homo sapiens 37-43 1705837-1 1991 We have extended our earlier observation that growing primary cultures of human umbilical vein endothelial cells (HUVEC) with heparin binding growth factor 1 (HBGF-1) 20 micrograms/mL and heparin 12 U/mL inhibits expression of tissue factor (TF) activity on HUVC monolayers perturbed with thrombin. Heparin 126-133 fibroblast growth factor 1 Homo sapiens 159-165 1716876-0 1991 The structure of human acidic fibroblast growth factor and its interaction with heparin. Heparin 80-87 fibroblast growth factor 1 Homo sapiens 23-54 2005115-1 1991 Incubation of 16-kDa 125I-labeled heparin binding (acidic fibroblast) growth factor type one (HBGF-1) with human hepatoma cells and normal rat hepatocytes resulted in the appearance of a stable 125I-labeled complex with an apparent molecular mass of 40 kDa. Heparin 34-41 fibroblast growth factor 1 Homo sapiens 94-100 1706340-1 1991 Acidic fibroblast growth factor (aFGF) is a broad spectrum mitogen that is stabilized by complexation with heparin and heparan proteoglycans. Heparin 107-114 fibroblast growth factor 1 Homo sapiens 0-31 1706340-1 1991 Acidic fibroblast growth factor (aFGF) is a broad spectrum mitogen that is stabilized by complexation with heparin and heparan proteoglycans. Heparin 107-114 fibroblast growth factor 1 Homo sapiens 33-37 1706340-4 1991 Mutants of aFGF in which either any 2 or all 3 cysteine residues are substituted by serines are more active, have longer activity half-lives, and are less heparin dependent than wild-type aFGF. Heparin 155-162 fibroblast growth factor 1 Homo sapiens 11-15 1706340-5 1991 In contrast, wild-type aFGF and the three mutants that each retain 2 cysteine residues inactivate more rapidly in the absence of heparin by a nonproteolytic mechanism but are markedly stabilized by heparin. Heparin 129-136 fibroblast growth factor 1 Homo sapiens 23-27 1706340-5 1991 In contrast, wild-type aFGF and the three mutants that each retain 2 cysteine residues inactivate more rapidly in the absence of heparin by a nonproteolytic mechanism but are markedly stabilized by heparin. Heparin 198-205 fibroblast growth factor 1 Homo sapiens 23-27 1706340-6 1991 This cysteine-mediated destabilization of aFGF not only diminishes its activity in the absence of heparin in tissue culture but also could functionally restrict its activity in vivo to the vicinity of mast cell-derived heparins and heparan proteoglycans associated with cell surfaces and basement membranes. Heparin 98-105 fibroblast growth factor 1 Homo sapiens 42-46 1706340-6 1991 This cysteine-mediated destabilization of aFGF not only diminishes its activity in the absence of heparin in tissue culture but also could functionally restrict its activity in vivo to the vicinity of mast cell-derived heparins and heparan proteoglycans associated with cell surfaces and basement membranes. Heparin 219-227 fibroblast growth factor 1 Homo sapiens 42-46 1705837-8 1991 These data establish that growing primary cultures of HUVEC with HBGF-1/heparin impairs their ability to synthesize TF apoprotein after perturbation. Heparin 72-79 fibroblast growth factor 1 Homo sapiens 65-71 1705837-9 1991 This may be part of a generalized response of endothelial cells to HBGF-1/heparin facilitating migration during angiogenesis. Heparin 74-81 fibroblast growth factor 1 Homo sapiens 67-73 1711526-4 1991 In this report, we summarize evidence that indicates that the heparin-binding and mitogenic activities of HBGF-1 can be dissociated from the receptor-binding activities of the growth factor by site-directed mutagenesis of a single lysine residue. Heparin 62-69 fibroblast growth factor 1 Homo sapiens 106-112 1699446-9 1990 In addition, we use the procedure to characterize the heparin-binding properties of heparin-binding growth factor 1 (acidic fibroblast growth factor) with synthetic peptide competitors and site-directed mutants of the growth factor. Heparin 54-61 fibroblast growth factor 1 Homo sapiens 84-115 1999476-3 1991 The addition of EGF, TGF alpha, or aFGF reversed heparin-induced growth inhibition, while bFGF partially negated this effect. Heparin 49-56 fibroblast growth factor 1 Homo sapiens 35-39 1699952-8 1990 Replacement of this lysine with glutamic acid reduces the apparent affinity of HBGF-1 for immobilized heparin (elutes at 0.45 M NaCl vs. 1.1 M NaCl for wild-type). Heparin 102-109 fibroblast growth factor 1 Homo sapiens 79-85 1706698-2 1990 The stimulation of endothelial cell growth by HBGF type one (HBGF-1) in particular requires heparin or a similar glycosaminoglycan. Heparin 92-99 fibroblast growth factor 1 Homo sapiens 61-67 1699952-9 1990 Mitogenic assays established two points: (a) human recombinant HBGF-1 is highly dependent on the presence of heparin for optimal mitogenic activity, and (b) the change of lysine 132 to glutamic acid drastically reduces the specific mitogenic activity of HBGF-1. Heparin 109-116 fibroblast growth factor 1 Homo sapiens 63-69 1700197-3 1990 A uniform concentration of 1 micrograms/ml of heparin was included in most experiments to exploit heparin"s potentiating effect on aFGF activity. Heparin 98-105 fibroblast growth factor 1 Homo sapiens 131-135 1699533-1 1990 Heparin potentiates the mitogenic activity of acidic fibroblast growth factor (aFGF) by 20-100 fold but mechanisms detailing this potentiation have not yet been fully elucidated. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 46-77 1699533-1 1990 Heparin potentiates the mitogenic activity of acidic fibroblast growth factor (aFGF) by 20-100 fold but mechanisms detailing this potentiation have not yet been fully elucidated. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 79-83 1699533-2 1990 We report that heparin increases the binding affinity of aFGF for the two cloned and overexpressed human FGF receptors, flg and bek, by 2-3 fold. Heparin 15-22 fibroblast growth factor 1 Homo sapiens 57-61 1699533-3 1990 This increase in binding affinity, together with previous data demonstrating a 3-5 fold increase in the stability of aFGF, are likely to account for a significant portion of heparin"s potentiation of aFGF activity observed in biological assay systems. Heparin 174-181 fibroblast growth factor 1 Homo sapiens 117-121 1699533-3 1990 This increase in binding affinity, together with previous data demonstrating a 3-5 fold increase in the stability of aFGF, are likely to account for a significant portion of heparin"s potentiation of aFGF activity observed in biological assay systems. Heparin 174-181 fibroblast growth factor 1 Homo sapiens 200-204 2298919-2 1990 In this report we describe the purification from several normal human hearts (including a very fresh, nonischemic sample) of heparin-binding, acid-, heat- and trypsin-sensitive 14-18-kD peptides that crossreact with antisera against aFGF and bFGF. Heparin 125-132 fibroblast growth factor 1 Homo sapiens 233-237 2318909-3 1990 In the presence of heparin (90 micrograms/ml), this effect is reproduced upon treatment with acidic fibroblast growth factor (aFGF, 6 ng/ml) or endothelial cell growth supplement (ECGS, 100 micrograms/ml), in both human umbilical vein endothelial cells (HUVEC) and BAEC. Heparin 19-26 fibroblast growth factor 1 Homo sapiens 93-124 2318909-3 1990 In the presence of heparin (90 micrograms/ml), this effect is reproduced upon treatment with acidic fibroblast growth factor (aFGF, 6 ng/ml) or endothelial cell growth supplement (ECGS, 100 micrograms/ml), in both human umbilical vein endothelial cells (HUVEC) and BAEC. Heparin 19-26 fibroblast growth factor 1 Homo sapiens 126-130 2107185-2 1990 We observed a marked diminution in both spontaneous and inducible production of prostacyclin (PGI2) by human umbilical vein and saphenous vein endothelial cells when they were cultured in the presence of the heparin-binding growth factor, acidic fibroblast growth factor (aFGF) and heparin, compared with PGI2 production during culture in medium lacking these factors. Heparin 208-215 fibroblast growth factor 1 Homo sapiens 239-270 2107185-2 1990 We observed a marked diminution in both spontaneous and inducible production of prostacyclin (PGI2) by human umbilical vein and saphenous vein endothelial cells when they were cultured in the presence of the heparin-binding growth factor, acidic fibroblast growth factor (aFGF) and heparin, compared with PGI2 production during culture in medium lacking these factors. Heparin 208-215 fibroblast growth factor 1 Homo sapiens 272-276 2107185-4 1990 Heparin (1-100 micrograms/ml) strongly potentiated the effects of aFGF but had a limited and variable effect alone. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 66-70 2107185-8 1990 These studies indicate that heparin acts as a modulator of prostaglandin synthesis in endothelial cells through its interaction with aFGF, mediated by alterations in two key enzymes in the arachidonate metabolic pathway. Heparin 28-35 fibroblast growth factor 1 Homo sapiens 133-137 1706557-5 1990 Mitogenic activity in the 1.2 M NaCl fraction of Heparin-Sepharose chromatography suggests the presence of acidic FGF (aFGF). Heparin 49-56 fibroblast growth factor 1 Homo sapiens 107-117 1706557-5 1990 Mitogenic activity in the 1.2 M NaCl fraction of Heparin-Sepharose chromatography suggests the presence of acidic FGF (aFGF). Heparin 49-56 fibroblast growth factor 1 Homo sapiens 119-123 1688801-2 1990 Using pulse-labeling and ELISA techniques, we found that EC grown in the presence of heparin (90 micrograms/ml) and endothelial cell growth factor (ECGF) synthesized 50% less fibronectin (FN) than did ECGF-treated control cultures. Heparin 85-92 fibroblast growth factor 1 Homo sapiens 201-205 1688801-5 1990 However, ECGF modulates the effect of heparin on EC synthesis of FN. Heparin 38-45 fibroblast growth factor 1 Homo sapiens 9-13 34762427-0 2021 Mechanistic Picture for Monomeric Human Fibroblast Growth Factor 1 Stabilization by Heparin Binding. Heparin 84-91 fibroblast growth factor 1 Homo sapiens 40-66 34762427-2 2021 hFGF1, which is associated with low stability in vivo, is known to be stabilized by binding heparin sulfate, a glycosaminoglycan that aids the protein in the activation of its cell surface receptor. Heparin 92-99 fibroblast growth factor 1 Homo sapiens 0-5 34762427-3 2021 The poor thermal and proteolytic stability of hFGF1 and the stabilizing role of heparin have long been observed experimentally; however, the mechanistic details of these phenomena are not well understood. Heparin 80-87 fibroblast growth factor 1 Homo sapiens 46-51 34762427-5 2021 We have observed a conformational change in the heparin-binding pocket of hFGF1 that occurs only in the absence of heparin. Heparin 48-55 fibroblast growth factor 1 Homo sapiens 74-79 34762427-5 2021 We have observed a conformational change in the heparin-binding pocket of hFGF1 that occurs only in the absence of heparin. Heparin 115-122 fibroblast growth factor 1 Homo sapiens 74-79 34762427-6 2021 Several intramolecular interactions were also identified within the heparin-binding pocket that form only when hFGF1 interacts with heparin. Heparin 68-75 fibroblast growth factor 1 Homo sapiens 111-116 34762427-6 2021 Several intramolecular interactions were also identified within the heparin-binding pocket that form only when hFGF1 interacts with heparin. Heparin 132-139 fibroblast growth factor 1 Homo sapiens 111-116 34762427-8 2021 This conformational transition results in increased flexibility of the heparin-binding pocket and provides an explanation for the susceptibility of apo hFGF1 to proteolytic degradation and thermal instability. Heparin 71-78 fibroblast growth factor 1 Homo sapiens 152-157 34762427-9 2021 This study provides a glimpse into mechanistic details of the heparin-mediated stabilization of hFGF1 and encourages the use of microsecond-level MD in studying the effect of binding on protein structure and dynamics. Heparin 62-69 fibroblast growth factor 1 Homo sapiens 96-101 34762427-10 2021 In addition, the observed differential behavior of hFGF1 in the absence and presence of heparin provides an example, where microsecond-level all-atom MD simulations are necessary to see functionally relevant biomolecular phenomena that otherwise will not be observed on sub-microsecond time scales. Heparin 88-95 fibroblast growth factor 1 Homo sapiens 51-56 34341408-4 2021 Systematic analyses of the thermal and chemical denaturation data on hFGF1 variants (Q54P, K126N, R136E, K126N/R136E, Q54P/K126N, Q54P/R136E, and Q54P/K126N/R136E) indicate that nullification of charges in the heparin-binding pocket can significantly increase the stability of wtFGF1. Heparin 210-217 fibroblast growth factor 1 Homo sapiens 69-74 34933004-1 2022 Human fibroblast growth factor 1 (hFGF1) binding to its receptor and heparin play critical roles in cell proliferation, angiogenesis and wound healing but is also implicated in cancer. Heparin 69-76 fibroblast growth factor 1 Homo sapiens 6-32 34933004-1 2022 Human fibroblast growth factor 1 (hFGF1) binding to its receptor and heparin play critical roles in cell proliferation, angiogenesis and wound healing but is also implicated in cancer. Heparin 69-76 fibroblast growth factor 1 Homo sapiens 34-39