PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 6195265-7 1983 Additionally, heparin was able to reduce the myeloperoxidase release from zymosan-stimulated neutrophils by nearly 50%. Heparin 14-21 myeloperoxidase Homo sapiens 45-60 32863239-6 2020 Exposure of fibronectin to MPO/H2O2/Cl- is shown to result in damage to the functionally important cell-binding and heparin-binding fragments, gross structural changes to the protein, and altered HCAEC adhesion and activity. Heparin 116-123 myeloperoxidase Homo sapiens 27-30 33915354-4 2021 We have previously shown that MPO, a highly cationic protein, regulates coagulation through heteromolecular interactions with various negatively charged structures, including membrane phospholipids and low-molecular-weight heparin. Heparin 223-230 myeloperoxidase Homo sapiens 30-33 32865287-0 2020 Effect of myeloperoxidase on the anticoagulant activity of low-molecular-weight heparin and rivaroxaban in an in-vitro tumor model. Heparin 80-87 myeloperoxidase Homo sapiens 10-25 31444563-5 2020 There was a significant correlation between delta whole blood passage time {(heparin tube) - (EDTA-2Na + heparin)} and serum levels of myeloperoxidase and adhesive leukocyte number, respectively, even in blood from patients with DM or ACS, who suffered from inflammation. Heparin 77-84 myeloperoxidase Homo sapiens 135-150 31444563-5 2020 There was a significant correlation between delta whole blood passage time {(heparin tube) - (EDTA-2Na + heparin)} and serum levels of myeloperoxidase and adhesive leukocyte number, respectively, even in blood from patients with DM or ACS, who suffered from inflammation. Heparin 105-112 myeloperoxidase Homo sapiens 135-150 29460830-0 2018 [Exocytosis of myeloperoxidase from activated neutrophils in the presence of heparin]. Heparin 77-84 myeloperoxidase Homo sapiens 15-30 30237127-6 2018 Here we show, using a newly-developed MS protocol, that HOCl and an enzymatic MPO system, generate site-specific dose-dependent Tyr chlorination and dichlorination (up to 16 of 100 residues modified), and oxidation of Trp (7 of 39 residues), Met (3 of 26) and His (1 of 55) within selected FN domains, and particularly the heparin- and cell-binding regions. Heparin 323-330 myeloperoxidase Homo sapiens 78-81 29460830-3 2018 It was found that after preincubation of cells with heparin (0.1 u/ml) the exocytosis of MPO from neutrophils activated by various stimulants (fMLP, PMA, plant lectins CABA and PHA-L) increased compared to that under the action of activators alone. Heparin 52-59 myeloperoxidase Homo sapiens 89-92 29460830-5 2018 Thus, the use of heparin at a concentration of 0.1 u/ml avoids the artifact caused by the "loss" of MPO in a result of its binding to neutrophils, and increases the accuracy of the method of registration the degranulation of azurophilic granules of neutrophils based on determination of the concentration or peroxidase activity of MPO in cell supernatants. Heparin 17-24 myeloperoxidase Homo sapiens 100-103 29460830-5 2018 Thus, the use of heparin at a concentration of 0.1 u/ml avoids the artifact caused by the "loss" of MPO in a result of its binding to neutrophils, and increases the accuracy of the method of registration the degranulation of azurophilic granules of neutrophils based on determination of the concentration or peroxidase activity of MPO in cell supernatants. Heparin 17-24 myeloperoxidase Homo sapiens 331-334 25867530-8 2015 MPO contributed only in heparin-treated patients, suggesting a more significant role for endothelial-bound MPO than for circulating MPO or elastase with respect to blood pressure regulation. Heparin 24-31 myeloperoxidase Homo sapiens 0-3 16606792-0 2006 Heparins increase endothelial nitric oxide bioavailability by liberating vessel-immobilized myeloperoxidase. Heparin 0-8 myeloperoxidase Homo sapiens 92-107 24837008-2 2014 We studied if low-molecular-weight heparin enoxaparin administered for hemodialysis (HD) anticoagulation causes systemic MPO activation. Heparin 35-42 myeloperoxidase Homo sapiens 121-124 24837008-7 2014 The increase in plasma MPO during systemic heparin-free HD was significantly less pronounced. Heparin 43-50 myeloperoxidase Homo sapiens 23-26 24976018-7 2014 Heparin-induced MPO-release from patient-derived RBCs was significantly increased compared to controls. Heparin 0-7 myeloperoxidase Homo sapiens 16-19 22107692-7 2011 In the heparin group, the post-filter serum MPO levels were significantly higher than the pre-filter (median 49.0 vs. 60.5 ng/mL, P<0.05) at 6 h. There were no significant differences between pre- and post-dialyzer MPO levels in the citrate group. Heparin 7-14 myeloperoxidase Homo sapiens 44-47 22107692-7 2011 In the heparin group, the post-filter serum MPO levels were significantly higher than the pre-filter (median 49.0 vs. 60.5 ng/mL, P<0.05) at 6 h. There were no significant differences between pre- and post-dialyzer MPO levels in the citrate group. Heparin 7-14 myeloperoxidase Homo sapiens 218-221 20643239-7 2010 Administration of heparin caused a marked increase of plasma MPO. Heparin 18-25 myeloperoxidase Homo sapiens 61-64 20643239-8 2010 Even so, it was still possible to detect an increase of plasma MPO at culprit lesion in patients with STEMI (n = 54, 171 ng/ml, 122 to 230) versus controls (n = 12, 136 ng/ml, 109 to 151, p <0.05) after heparin and before PCI. Heparin 206-213 myeloperoxidase Homo sapiens 63-66 19524564-0 2009 Myeloperoxidase concentrations in EDTA-plasma of healthy subjects are discordant with concentrations in heparin-plasma and serum. Heparin 104-111 myeloperoxidase Homo sapiens 0-15 19524564-2 2009 DESIGN AND METHODS: MPO was measured in EDTA-plasma and matched heparin-plasma and serum samples collected from healthy volunteers. Heparin 64-71 myeloperoxidase Homo sapiens 20-23 19524564-3 2009 RESULTS: MPO concentrations in heparin-plasma and serum were higher than in EDTA-plasma (both P<0.001). Heparin 31-38 myeloperoxidase Homo sapiens 9-12 19362143-8 2009 Heparin, which is known to increase MPO plasma levels in patients with stable CAD, had no effect on MPO plasma levels in AMI patients. Heparin 0-7 myeloperoxidase Homo sapiens 36-39 24438360-6 2014 There was also net production of elastase and MPO across the filter during heparin anticoagulation (P = 0.049 or lower), while production was minimal and absent in the no anticoagulation and citrate group, respectively. Heparin 75-82 myeloperoxidase Homo sapiens 46-49 24438360-7 2014 During heparin anticoagulation, plasma concentrations of MPO at the inlet increased in the first 10 minutes of CVVH (P = 0.024). Heparin 7-14 myeloperoxidase Homo sapiens 57-60 24267251-8 2013 CONCLUSION: Our data demonstrate that heparin-induced mobilization of vessel-bound MPO is closely linked to coronary plaque burden and thus further corroborate the evidence for the intimate involvement of this enzyme in vascular pathophysiology, as well as the importance of inflammation in atherosclerosis. Heparin 38-45 myeloperoxidase Homo sapiens 83-86 19049846-2 2010 Unfractionated heparins release vessel-bound MPO and increase endothelial NO bioavailability. Heparin 15-23 myeloperoxidase Homo sapiens 45-48 19049846-3 2010 Whether low molecular weight heparins also affect circulating MPO levels and NO dependent vasoreactivity however remains elusive. Heparin 29-37 myeloperoxidase Homo sapiens 62-65 19049846-7 2010 DISCUSSION: This study confirms the concept that heparins improve endothelial function, an established read-out of vascular NO bioavailability, by mobilizing vessel bound MPO. Heparin 49-57 myeloperoxidase Homo sapiens 171-174 19961422-6 2009 The identified proteinases contained heparin-binding motifs inherent in the complex-forming partners of CP, such as lactoferrin, myeloperoxidase, and serprocidines. Heparin 37-44 myeloperoxidase Homo sapiens 129-144 18509013-8 2008 MPO concentrations were consistently higher in samples collected in serum and heparin plasma tubes than in samples in EDTA or citrate tubes. Heparin 78-85 myeloperoxidase Homo sapiens 0-3 17525363-5 2007 In the UFH+eptifibatide, but not the bivalirudin group, myeloperoxidase (MPO) levels were elevated 2.3-fold above baseline (P=0.004) immediately after PCI. Heparin 7-10 myeloperoxidase Homo sapiens 56-71 17525363-5 2007 In the UFH+eptifibatide, but not the bivalirudin group, myeloperoxidase (MPO) levels were elevated 2.3-fold above baseline (P=0.004) immediately after PCI. Heparin 7-10 myeloperoxidase Homo sapiens 73-76 17525363-6 2007 In an in vitro assay, heparin and to a lesser extent enoxaparin, but not bivalirudin or eptifibatide, stimulated MPO release from and binding to neutrophils and neutrophil activation. Heparin 22-29 myeloperoxidase Homo sapiens 113-116 16606792-3 2006 In the present study, we investigated whether heparin mobilizes MPO from vascular compartments in humans and defined whether this translates into increased vascular NO bioavailability and function. Heparin 46-53 myeloperoxidase Homo sapiens 64-67 16606792-5 2006 Whereas baseline plasma MPO levels did not differ between patients with or without angiographically detectable coronary artery disease (CAD), the increase in MPO plasma content on bolus heparin administration was higher in patients with CAD (P=0.01). Heparin 186-193 myeloperoxidase Homo sapiens 158-161 16606792-7 2006 The extent of heparin-induced MPO release was correlated with improvement in endothelial function (r=0.69, P<0.01). Heparin 14-21 myeloperoxidase Homo sapiens 30-33 16606792-8 2006 Moreover, and consistent with this tenet, ex vivo heparin treatment of extracellular matrix proteins, cultured endothelial cells, and saphenous vein graft specimens from CAD patients decreased MPO burden. Heparin 50-57 myeloperoxidase Homo sapiens 193-196 16606792-9 2006 CONCLUSIONS: Mobilization of vessel-associated MPO may represent an important mechanism by which heparins exert antiinflammatory effects and increase vascular NO bioavailability. Heparin 97-105 myeloperoxidase Homo sapiens 47-50 16377383-4 2006 In this review, a novel and growing body of evidence indicating that MPO also is a potent blood vessel-bound enzyme that can be mobilized rapidly and extensively into circulating blood by exogenous heparin is discussed. Heparin 198-205 myeloperoxidase Homo sapiens 69-72 16464886-0 2006 Myeloperoxidase up-regulation during haemodialysis: is heparin the missing link? Heparin 55-62 myeloperoxidase Homo sapiens 0-15 16377383-7 2006 In view of the plausible clinical importance of the novel MPO-oxidative stress-heparin interaction in this population, the need for additional studies assessing different dialyzer membranes, various heparin types (unfractionated heparin versus low-molecular-weight heparins versus pentasaccharides), as well as different anticoagulation regimens, is emphasized. Heparin 79-86 myeloperoxidase Homo sapiens 58-61 16377383-7 2006 In view of the plausible clinical importance of the novel MPO-oxidative stress-heparin interaction in this population, the need for additional studies assessing different dialyzer membranes, various heparin types (unfractionated heparin versus low-molecular-weight heparins versus pentasaccharides), as well as different anticoagulation regimens, is emphasized. Heparin 265-273 myeloperoxidase Homo sapiens 58-61 11958287-3 2000 During routine HD with a cuprophane membrane and high molecular weight (HMW) heparin, plasma MPO was rapidly upregulated to maximal levels within 15 min after starting extracorporeal circulation. Heparin 77-84 myeloperoxidase Homo sapiens 93-96 16139336-7 2006 Platelet-leukocyte aggregation in vivo was greater (PMA=2-fold, p=0.04; PNA=3-fold, p=0.006) with UFH+E as was the concentration in blood of MPO (1.5-fold, p=0.007). Heparin 98-101 myeloperoxidase Homo sapiens 141-144 11742862-0 2001 Myeloperoxidase and hypochlorite, but not copper ions, oxidize heparin-bound LDL particles and release them from heparin. Heparin 63-70 myeloperoxidase Homo sapiens 0-15 11742862-0 2001 Myeloperoxidase and hypochlorite, but not copper ions, oxidize heparin-bound LDL particles and release them from heparin. Heparin 113-120 myeloperoxidase Homo sapiens 0-15 11742862-5 2001 In contrast, myeloperoxidase and hypochlorite, a product of myeloperoxidase, were able to oxidize heparin-bound LDL, and this oxidation led to the release of the oxidized particles from heparin. Heparin 98-105 myeloperoxidase Homo sapiens 13-28 11742862-5 2001 In contrast, myeloperoxidase and hypochlorite, a product of myeloperoxidase, were able to oxidize heparin-bound LDL, and this oxidation led to the release of the oxidized particles from heparin. Heparin 98-105 myeloperoxidase Homo sapiens 60-75 11742862-5 2001 In contrast, myeloperoxidase and hypochlorite, a product of myeloperoxidase, were able to oxidize heparin-bound LDL, and this oxidation led to the release of the oxidized particles from heparin. Heparin 186-193 myeloperoxidase Homo sapiens 13-28 11742862-5 2001 In contrast, myeloperoxidase and hypochlorite, a product of myeloperoxidase, were able to oxidize heparin-bound LDL, and this oxidation led to the release of the oxidized particles from heparin. Heparin 186-193 myeloperoxidase Homo sapiens 60-75 10334872-5 1999 Heparin, at high concentrations, can prevent the inhibition of tryptase by MPO. Heparin 0-7 myeloperoxidase Homo sapiens 75-78 10334872-7 1999 These data suggest that MPO inhibits tryptase by interfering with the heparin stabilization of tryptase tetramer. Heparin 70-77 myeloperoxidase Homo sapiens 24-27 9655178-0 1998 Association of myeloperoxidase with heparin: oxidative inactivation of proteins on the surface of endothelial cells by the bound enzyme. Heparin 36-43 myeloperoxidase Homo sapiens 15-30 9655178-1 1998 Chromatography of human myeloperoxidase (MPO) on a heparin-agarose column demonstrated a tight association of the protein with the resin. Heparin 51-58 myeloperoxidase Homo sapiens 24-39 9655178-1 1998 Chromatography of human myeloperoxidase (MPO) on a heparin-agarose column demonstrated a tight association of the protein with the resin. Heparin 51-58 myeloperoxidase Homo sapiens 41-44 9655178-6 1998 The oxidative modification of FIXBP was only partially dependent on the addition of hydrogen peroxide and was abolished by exogenous heparin which displaced MPO from the cell surface, emphasizing the functional differences between cell-bound and free enzyme. Heparin 133-140 myeloperoxidase Homo sapiens 157-160 9477462-13 1997 MPO was also affected by heparin-coating. Heparin 25-32 myeloperoxidase Homo sapiens 0-3 9423940-9 1997 Heparin-coating diminished myeloperoxidase and lactoferrin release. Heparin 0-7 myeloperoxidase Homo sapiens 27-42 8864022-11 1996 Release of MPO at CPB end and of LF 45 min after start of CPB and at CPB end were significantly lower in the heparin-coated CPB circuits. Heparin 109-116 myeloperoxidase Homo sapiens 11-14 9131716-8 1997 The increases in plasma myeloperoxidase, lactoferrin, C3bc and TCC were lower in the heparin-coated group compared to the control group. Heparin 85-92 myeloperoxidase Homo sapiens 24-39 9127328-2 1997 MPO levels were markedly elevated during the entire HD procedure with heparin. Heparin 70-77 myeloperoxidase Homo sapiens 0-3 9127328-9 1997 MPO levels with heparin alone were shown to markedly rise in the closed system. Heparin 16-23 myeloperoxidase Homo sapiens 0-3 8787476-11 1995 Also for myeloperoxidase a higher level was observed in the high heparin dose group. Heparin 65-72 myeloperoxidase Homo sapiens 9-24 8668917-0 1996 Heparin in clinical doses "primes" granulocytes to subsequent activation as measured by myeloperoxidase release. Heparin 0-7 myeloperoxidase Homo sapiens 88-103 8740352-3 1996 The heparin coating significantly reduced the concentrations of C3bc, TCC, fibrinopeptide A, lactoferrin, myeloperoxidase and beta-thromboglobulin. Heparin 4-11 myeloperoxidase Homo sapiens 106-121 8526620-6 1995 RESULTS: Heparin coating by either method reduced the formation of terminal SC5b-9 complement complex and the release of lactoferrin and myeloperoxidase compared with uncoated systems. Heparin 9-16 myeloperoxidase Homo sapiens 137-152 8389063-5 1993 Myeloperoxidase (MPO) released by PMNL was found to be significantly HMW- and LMW-heparins dose-dependent. Heparin 82-90 myeloperoxidase Homo sapiens 0-15 8406134-4 1993 Heparin administration preceding renal artery clamping resulted in a twofold significant increase of baseline plasma myeloperoxidase (MPO) level (523 +/- 214 ng/ml). Heparin 0-7 myeloperoxidase Homo sapiens 117-132 8406134-4 1993 Heparin administration preceding renal artery clamping resulted in a twofold significant increase of baseline plasma myeloperoxidase (MPO) level (523 +/- 214 ng/ml). Heparin 0-7 myeloperoxidase Homo sapiens 134-137 8067851-5 1994 The maximum myeloperoxidase levels were significantly lower in the heparin-coated group than those in the uncoated group (p = 0.03). Heparin 67-74 myeloperoxidase Homo sapiens 12-27 8389063-5 1993 Myeloperoxidase (MPO) released by PMNL was found to be significantly HMW- and LMW-heparins dose-dependent. Heparin 82-90 myeloperoxidase Homo sapiens 17-20