PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24324963-3 2013 Increasing tyrosine phosphorylation with the phosphatase inhibitor, sodium orthovanadate produced arterial contraction which was lower in tumoral than in control arteries, whereas it reduced the contraction to noradrenaline in tumoral but not in control arteries and reduced the relaxation to bradykinin in control but not in tumoral arteries. Tyrosine 11-19 kininogen 1 Homo sapiens 293-303 24960080-2 2014 Stimulation of different endothelial cell lines with bradykinin (BK) activates the endothelial NO synthase (eNOS) and promotes EGF-R tyrosine phosphorylation. Tyrosine 133-141 kininogen 1 Homo sapiens 53-63 24960080-2 2014 Stimulation of different endothelial cell lines with bradykinin (BK) activates the endothelial NO synthase (eNOS) and promotes EGF-R tyrosine phosphorylation. Tyrosine 133-141 kininogen 1 Homo sapiens 65-67 12594217-0 2003 Differential tyrosine phosphorylation of plasma membrane Ca2+-ATPase and regulation of calcium pump activity by carbachol and bradykinin. Tyrosine 13-21 kininogen 1 Homo sapiens 126-136 12594217-9 2003 An investigation of tyrosine phosphorylation levels of the plasma membrane Ca(2+)-ATPase (PMCA) demonstrated that CCh stimulates an increase in tyrosine phosphorylation levels, which has been reported to inhibit Ca(2+) pump activity, whereas in contrast, BK stimulates a reduction of PMCA tyrosine phosphorylation levels. Tyrosine 144-152 kininogen 1 Homo sapiens 255-257 12594217-9 2003 An investigation of tyrosine phosphorylation levels of the plasma membrane Ca(2+)-ATPase (PMCA) demonstrated that CCh stimulates an increase in tyrosine phosphorylation levels, which has been reported to inhibit Ca(2+) pump activity, whereas in contrast, BK stimulates a reduction of PMCA tyrosine phosphorylation levels. Tyrosine 144-152 kininogen 1 Homo sapiens 255-257 12594217-10 2003 Thus, BK and CCh have a differential effect both on Ca(2+) pump activity and on tyrosine phosphorylation levels of the PMCA. Tyrosine 80-88 kininogen 1 Homo sapiens 6-8 18938142-8 2009 Exposure of HEK293 cells to BK produced a concentration-dependent rise in intracellular Ca(2+) (EC(50)=36.5+/-8.0 x 10(-9)M), a rapid increase in tyrosine phosphorylation of ERK (EC(50)=9.8+/-0.4 x 10(-9)M), and elevation in ECAR by approximately 20%. Tyrosine 146-154 kininogen 1 Homo sapiens 28-30 16898954-8 2006 In vitro tyrosine dephosphorylation of platelet eNOS using a recombinant protein tyrosine phosphatase enhanced thrombin-induced activity compared to thrombin alone, but had no effect on endothelial eNOS activity either at basal or after stimulation with bradykinin. Tyrosine 9-17 kininogen 1 Homo sapiens 254-264 15050422-6 2004 Stimulating cells with dibutyryl-cAMP, cholera toxin and forskolin for 24 h increased (125)I-[Tyr(8)]-bradykinin (90 pM) binding with approximately 50%. Tyrosine 94-97 kininogen 1 Homo sapiens 102-112 15050422-9 2004 These results suggest, that the dibutyryl-cAMP stimulated increase in (125)I-[Tyr(8)]-bradykinin binding is probably due to increased B(1) receptor affinity with no change in receptor capacity. Tyrosine 78-81 kininogen 1 Homo sapiens 86-96 11711543-4 2002 At the same time, BK produced the tyrosine phosphorylation and internalization of KDR/Flk-1 as did VEGF itself. Tyrosine 34-42 kininogen 1 Homo sapiens 18-20 12675336-8 2003 The reversible labeling of Tyr-containing peptide was demonstrated with [Tyr8]-bradykinin as a model for high-molecular-mass peptides and proteins. Tyrosine 27-30 kininogen 1 Homo sapiens 79-89 10614983-2 1999 The principal idea for this hypothesis stems from observation that two bradykinin B2 receptor-activated signal pathways, protein tyrosine phosphorylation and formation of inositol tetrakisphosphate, merge during the Ca2+ influx process and that GTPase activating-protein 1 (GAP 1) is inositol tetrakisphosphate binding protein. Tyrosine 129-137 kininogen 1 Homo sapiens 71-81 10749673-4 2000 Three lines of evidence suggest the activation of a protein tyrosine phosphatase (PTP) by bradykinin: (i) treatment of A431 cells with bradykinin decreases both basal and EGF-induced EGFR tyrosine phosphorylation, (ii) this effect of bradykinin can be blocked by two different PTP inhibitors, and (iii) bradykinin significantly increased the PTP activity in total A431 cell lysates when measured in vitro. Tyrosine 60-68 kininogen 1 Homo sapiens 90-100 10749673-4 2000 Three lines of evidence suggest the activation of a protein tyrosine phosphatase (PTP) by bradykinin: (i) treatment of A431 cells with bradykinin decreases both basal and EGF-induced EGFR tyrosine phosphorylation, (ii) this effect of bradykinin can be blocked by two different PTP inhibitors, and (iii) bradykinin significantly increased the PTP activity in total A431 cell lysates when measured in vitro. Tyrosine 60-68 kininogen 1 Homo sapiens 135-145 10749673-4 2000 Three lines of evidence suggest the activation of a protein tyrosine phosphatase (PTP) by bradykinin: (i) treatment of A431 cells with bradykinin decreases both basal and EGF-induced EGFR tyrosine phosphorylation, (ii) this effect of bradykinin can be blocked by two different PTP inhibitors, and (iii) bradykinin significantly increased the PTP activity in total A431 cell lysates when measured in vitro. Tyrosine 60-68 kininogen 1 Homo sapiens 135-145 10749673-4 2000 Three lines of evidence suggest the activation of a protein tyrosine phosphatase (PTP) by bradykinin: (i) treatment of A431 cells with bradykinin decreases both basal and EGF-induced EGFR tyrosine phosphorylation, (ii) this effect of bradykinin can be blocked by two different PTP inhibitors, and (iii) bradykinin significantly increased the PTP activity in total A431 cell lysates when measured in vitro. Tyrosine 60-68 kininogen 1 Homo sapiens 135-145 11557555-5 2001 Treatment with [Hyp(3),Tyr(Me)(8)]bradykinin, a B(2) receptor agonist, stimulated thymidine incorporation by 146%, whereas B(1)-selective Lys-des-Arg(9)-bradykinin had no effect. Tyrosine 23-26 kininogen 1 Homo sapiens 34-44 10978247-6 2000 Western blots of immunoprecipitated eNOS showed the presence of a major tyrosine-phosphorylated protein band at a mass corresponding to approximately 125 kDa and 2 minor bands corresponding to approximately 105 and 75 kDa after treatment with vanadate/Bk. Tyrosine 72-80 kininogen 1 Homo sapiens 252-254 8940106-5 1996 Here, we present several lines of evidence indicating the ability of epidermal growth factor (EGF) to suppress BK-induced activation of the cAMP pathway in A431 cells via tyrosine phosphorylation of Gsalpha. Tyrosine 171-179 kininogen 1 Homo sapiens 111-113 10510297-4 1999 Furthermore, the B2 receptor is transiently phosphorylated on tyrosine residues in cultured endothelial cells in response to BK stimulation. Tyrosine 62-70 kininogen 1 Homo sapiens 125-127 10444401-5 1999 Addition of 10(-10)-10(-7) M BK to VSMC resulted in a rapid and concentration-dependent increase in tyrosine phosphorylation of several 144- to 40-kDa proteins. Tyrosine 100-108 kininogen 1 Homo sapiens 29-31 10444401-7 1999 Immunoprecipitation with anti-phosphotyrosine antibodies followed by immunoblot revealed that 10(-9) M BK induced tyrosine phosphorylation of focal adhesion kinase (p125(FAK)). Tyrosine 37-45 kininogen 1 Homo sapiens 103-105 10444401-10 1999 Protein kinase C downregulation by phorbol 12-myristate 13-acetate and/or inhibitors to protein kinase C, p60(src) kinase, and MAPK kinase inhibited BK-induced MAPK tyrosine phosphorylation. Tyrosine 165-173 kininogen 1 Homo sapiens 149-151 10484429-2 1999 Exposure of vascular smooth muscle cells (VSMC) to BK (10(-7) M) produced a rapid and transient rise in intracellular calcium, which preceded an increase in tyrosine phosphorylation of mitogen-activated protein kinase (MAPK). Tyrosine 157-165 kininogen 1 Homo sapiens 51-53 9600070-0 1998 Bradykinin stimulates the tyrosine phosphorylation and bradykinin B2 receptor association of phospholipase C gamma 1 in vascular endothelial cells. Tyrosine 26-34 kininogen 1 Homo sapiens 0-10 9600070-4 1998 In the present study, however, we have found that BK stimulation of IP3 production and the Ca2+ signal in endothelial cells is dependent on tyrosine phosphorylation. Tyrosine 140-148 kininogen 1 Homo sapiens 50-52 9830506-0 1998 Bradykinin-induced tyrosine phosphorylation of proteins in cultured human keratinocytes. Tyrosine 19-27 kininogen 1 Homo sapiens 0-10 9830506-1 1998 The stimulating effect of bradykinin on phosphorylation of proteins at tyrosine residues was visualized on human keratinocytes in primary culture. Tyrosine 71-79 kininogen 1 Homo sapiens 26-36 9830506-8 1998 After short-time stimulation with bradykinin tyrosine phosphorylation was confined to distinct bands at 82, 76, 70, 57, 54, 48, 40 and 39 kDa and a diffuse band at 62 kDa. Tyrosine 45-53 kininogen 1 Homo sapiens 34-44 9830506-10 1998 Among these proteins, MAP kinase, actin, paxillin and the EGF receptor were the most likely candidates for bradykinin-induced tyrosine phosphorylation. Tyrosine 126-134 kininogen 1 Homo sapiens 107-117 9435680-5 1997 In the present study, we utilized immunofluorescence, immunoprecipitation, and immunoblotting techniques to identify substrates that are tyrosine phosphorylated in response to bradykinin action in mesangial cells. Tyrosine 137-145 kininogen 1 Homo sapiens 176-186 9435680-8 1997 Confocal microscopy of mesangial cells stained for MAPK indicated that bradykinin stimulation resulted in translocation of MAPK from the cytoplasm to the nucleus by 2 h. These data demonstrate that bradykinin action results in the tyrosine phosphorylation of cellular proteins in mesangial cells and suggest a role for tubulin and MAPK in the signaling cascade of bradykinin leading to altered mesangial function. Tyrosine 231-239 kininogen 1 Homo sapiens 71-81 9435680-8 1997 Confocal microscopy of mesangial cells stained for MAPK indicated that bradykinin stimulation resulted in translocation of MAPK from the cytoplasm to the nucleus by 2 h. These data demonstrate that bradykinin action results in the tyrosine phosphorylation of cellular proteins in mesangial cells and suggest a role for tubulin and MAPK in the signaling cascade of bradykinin leading to altered mesangial function. Tyrosine 231-239 kininogen 1 Homo sapiens 198-208 9435680-8 1997 Confocal microscopy of mesangial cells stained for MAPK indicated that bradykinin stimulation resulted in translocation of MAPK from the cytoplasm to the nucleus by 2 h. These data demonstrate that bradykinin action results in the tyrosine phosphorylation of cellular proteins in mesangial cells and suggest a role for tubulin and MAPK in the signaling cascade of bradykinin leading to altered mesangial function. Tyrosine 231-239 kininogen 1 Homo sapiens 198-208 9293962-3 1997 In cultured human endothelial cells, bradykinin induced a rapid increase in the tyrosine phosphorylation of several Triton-soluble proteins. Tyrosine 80-88 kininogen 1 Homo sapiens 37-47 9293962-4 1997 Immunoprecipitation of tyrosine-phosphorylated proteins from bradykinin-stimulated cells followed by Western blotting using the respective antibodies facilitated the identification of a 77 kiloDalton (kDa) protein as paxillin, a 130 kDa protein as PLC-gamma1, and a 42/44 kDa doublet as mitogen-activated protein (MAP) kinase. Tyrosine 23-31 kininogen 1 Homo sapiens 61-71 9293962-5 1997 The bradykinin-induced tyrosine phosphorylation of PLC-gamma1 was relatively transient and was associated with an increase in intracellular levels of IP3. Tyrosine 23-31 kininogen 1 Homo sapiens 4-14 8665918-0 1996 Bradykinin induces tyrosine phosphorylation in human foreskin fibroblasts and 293 cells transfected with rat B2 kinin receptor. Tyrosine 19-27 kininogen 1 Homo sapiens 0-10 8631922-5 1996 In bradykinin-stimulated cells the tyrosine phosphorylation of the same cytoskeletal proteins (most notably 85- and 100-kDa proteins) was transient when cells were stimulated in the presence of extracellular Ca2+, was maintained under Ca2+-free conditions, and was reversed following readdition of extracellular Ca2+. Tyrosine 35-43 kininogen 1 Homo sapiens 3-13 8967444-0 1996 Tyrosine phosphorylation and activation of pp60c-src and pp125FAK in bradykinin-stimulated fibroblasts. Tyrosine 0-8 kininogen 1 Homo sapiens 69-79 8967444-1 1996 Bradykinin (BK) stimulates protein tyrosine phosphorylation in human foreskin fibroblasts (K.-M. Lee, K. Toscas, and M. L. Villereal, J. Biol. Tyrosine 35-43 kininogen 1 Homo sapiens 0-10 8967444-1 1996 Bradykinin (BK) stimulates protein tyrosine phosphorylation in human foreskin fibroblasts (K.-M. Lee, K. Toscas, and M. L. Villereal, J. Biol. Tyrosine 35-43 kininogen 1 Homo sapiens 12-14 8967444-6 1996 The BK-stimulated pp125FAK tyrosine phosphorylation level is well correlated with increased kinase activity, as assessed by in vitro immune complex kinase assays. Tyrosine 27-35 kininogen 1 Homo sapiens 4-6 8967444-8 1996 In addition to identifying the two proteins responsible for the major phosphotyrosine bands, we also report that pp60c-src is tyrosine phosphorylated and activated in response to BK, as analyzed by immunoblotting and in vitro kinase assays, respectively. Tyrosine 77-85 kininogen 1 Homo sapiens 179-181 8665918-3 1996 We studied whether in human foreskin fibroblasts bradykinin treatment induces tyrosine phosphorylation of cellular proteins. Tyrosine 78-86 kininogen 1 Homo sapiens 49-59 8665918-5 1996 The effect evoked by 10 nM bradykinin was rapid (2 min) and it was partially reduced by the B2-kinin-receptor antagonist Hoe 140 which was shown to be a weak inducer of tyrosine phosphorylation. Tyrosine 169-177 kininogen 1 Homo sapiens 27-37 8665918-6 1996 The bradykinin-mediated tyrosine phosphorylation events were reproduced in human embryonal kidney 293 fibroblasts which were transiently transfected with the rat B2 kinin receptor, but they were not observed in untransfected 293 control cells. Tyrosine 24-32 kininogen 1 Homo sapiens 4-14 8665918-10 1996 While IGF-I, insulin and EGF were almost ineffective, PDGF stimulated the tyrosine phosphorylation of 130-kDa bands with a similar pattern to that produced by bradykinin. Tyrosine 74-82 kininogen 1 Homo sapiens 159-169 7683685-2 1993 Immunoblots with anti-phosphotyrosine antibodies following BK stimulation of human fibroblasts showed tyrosine phosphorylation of specific proteins that could be inhibited by the tyrosine kinase inhibitors genistein and tyrphostin. Tyrosine 29-37 kininogen 1 Homo sapiens 59-61 7539258-0 1995 Bradykinin induces tyrosine phosphorylation of epidermal growth factor-receptor and focal adhesion proteins in human keratinocytes. Tyrosine 19-27 kininogen 1 Homo sapiens 0-10 7539258-2 1995 In the HaCaT human keratinocyte cell line, we observed bradykinin-stimulated tyrosine phosphorylation of several cellular proteins with peak response at 15 min. Tyrosine 77-85 kininogen 1 Homo sapiens 55-65 7539258-3 1995 The focal adhesion proteins paxillin and p125FAK were tyrosine phosphorylated in response to bradykinin but not in response to epidermal growth factor. Tyrosine 54-62 kininogen 1 Homo sapiens 93-103 7539258-4 1995 Interestingly, we identified the epidermal growth factor receptor as a novel target for bradykinin-induced tyrosine phosphorylation. Tyrosine 107-115 kininogen 1 Homo sapiens 88-98 7539258-5 1995 The tyrosine kinase inhibitor genistein and the protein kinase C inhibitors staurosporine and Ro31-7549, all blocked bradykinin-induced tyrosine phosphorylation. Tyrosine 4-12 kininogen 1 Homo sapiens 117-127 8529791-14 1996 Bradykinin-induced tyrosine phosphorylation of proteins of approximately 130 and 70 kDa was inhibited by insulin treatment of rat-1 fibroblasts. Tyrosine 19-27 kininogen 1 Homo sapiens 0-10 8529791-15 1996 These data suggest that signals from the insulin receptor modify signaling from the bradykinin receptor to tyrosine phosphorylation of different cellular proteins. Tyrosine 107-115 kininogen 1 Homo sapiens 84-94 8804078-1 1996 Stimulation of small cell lung cancer (SCLC) cells with neuropeptides bombesin, bradykinin, gastrin, and neurotensin resulted in increased tyrosine kinase activity and tyrosine phosphorylation of a number of polypeptides including a p120 kDa polypeptide identified by immunoblotting as focal adhesion kinase (p125FAK). Tyrosine 139-147 kininogen 1 Homo sapiens 80-90 7498312-3 1995 Competition experiments revealed a rank order of potency with bradykinin being most effective (bradykinin = [Lys]bradykinin > [Met- Lys]bradykinin > [Tyr]bradykinin > [des-Arg9]bradykinin), whereas [des-Arg9]bradykinin was ineffective. Tyrosine 156-159 kininogen 1 Homo sapiens 62-72 7895328-3 1995 Stimulation of endothelial cells with either bradykinin (100 nmol/L), histamine (1 mumol/L), or the Ca(2+)-ATPase inhibitor thapsigargin (30 nmol/L) resulted in a slightly delayed but prolonged tyrosine phosphorylation of two low molecular weight proteins (approximately 42 and approximately 44 kD). Tyrosine 194-202 kininogen 1 Homo sapiens 45-55 7504289-0 1993 Human bradykinin B2 receptors isolated by receptor-specific monoclonal antibodies are tyrosine phosphorylated. Tyrosine 86-94 kininogen 1 Homo sapiens 6-16 7504289-1 1993 We report the immunoaffinity isolation of bradykinin B2 receptors in a tyrosine-phosphorylated state from WI-38 human lung fibroblasts. Tyrosine 71-79 kininogen 1 Homo sapiens 42-52 3436959-6 1987 In the presence of 5 x 10(-4) M zinc ions, typical difference spectra due to a red shift of tryptophan and/or tyrosine residues were observed for HMW kininogen and its derivatives but not low-molecular-weight (LMW) kininogen. Tyrosine 110-118 kininogen 1 Homo sapiens 146-159 6140924-2 1983 125I-Labeled derivatives of [Tyr1]-kallidin and [Tyr-8]-bradykinin bound to the EDTA-inhibited enzyme, and binding was inhibited by nonradioactive BK. Tyrosine 29-32 kininogen 1 Homo sapiens 147-149 6997175-3 1980 As insulin, bradykinin lessened the release of 9 amino acids: Glycine, serine, ornithin, valine, leucine, isoleucine and tyrosine. Tyrosine 121-129 kininogen 1 Homo sapiens 12-22