The heparin binding site of human extracellular-superoxide dismutase

1992 ◽  
Vol 297 (1) ◽  
pp. 155-161 ◽  
Author(s):  
Tetsuo Adachi ◽  
Tsutomu Kodera ◽  
Hideki Ohta ◽  
Kyozo Hayashi ◽  
Kazuyuki Hirano
Keyword(s):  
Superoxide Dismutase ◽  
Binding Site ◽  
Extracellular Superoxide Dismutase ◽  
Heparin Binding ◽  
Heparin Binding Site

Antithrombin-mediated Inhibition of Factor Vlla-Tissue Factor Complex by the Synthetic Pentasaccharide Representing the Heparin Binding Site to Antithrombin

1996 ◽  
Vol 76 (01) ◽  
pp. 005-008 ◽  
Author(s):  
Jean Claude Lormeau ◽  
Jean Pascal Herault ◽  
Jean Marc Herbert
Keyword(s):  
Binding Site ◽  
Tissue Factor ◽  
Residual Activity ◽  
Coagulation Factors ◽  
Heparin Binding ◽  
Experimental Conditions ◽  
First Order ◽  
Heparin Binding Site ◽  
Coagulant Activity

SummaryWe examined the effect of the synthetic pentasaccharide representing the minimal binding site of heparin to antithrombin on the antithrombin-mediated inactivation of factor Vila bound to tissue factor. This effect was compared to the effect of unfractionated heparin. Using purified recombinant human coagulation factors and either a clotting or an amidolytic assay for the determination of the residual activity of factor Vila, we showed that the pentasaccharide was an efficient antithrombin-dependent inhibitor of the coagulant activity of tissue factor-factor Vila complex. In our experimental conditions, assuming a mean MW of 14,000 for heparin, the molar pseudo-first order rate constants for ATIII-mediated FVIIa inhibition by ATIII-binding heparin and by the synthetic pentasaccharide were found to be similar with respective values of 104,000 ± 10,500 min-1 and 112,000 ± 12,000 min-1 (mean ± s.e.m., n = 3)

scholarly journals Localization of the major heparin-binding site in fibronectin.

1991 ◽  
Vol 266 (12) ◽  
pp. 7812-7818 ◽  
Author(s):  
F J Barkalow ◽  
J E Schwarzbauer
Keyword(s):  
Binding Site ◽  
Heparin Binding ◽  
Heparin Binding Site

scholarly journals Proteolytic modification of the heparin-binding affinity of extracellular superoxide dismutase

1993 ◽  
Vol 290 (2) ◽  
pp. 623-626 ◽  
Author(s):  
K Karlsson ◽  
A Edlund ◽  
J Sandström ◽  
S L Marklund
Keyword(s):  
Superoxide Dismutase ◽  
Binding Affinity ◽  
Heparan Sulphate ◽  
Limited Proteolysis ◽  
Size Exclusion ◽  
Extracellular Superoxide Dismutase ◽  
Heparin Binding ◽  
Binding Domains ◽  
Heparin Affinity

The heparin-binding affinity of the tetrameric extracellular superoxide dismutase (EC-SOD) is a result of the cooperative effect of the heparin-binding domains of the subunits, located in the hydrophilic, strongly positively charged C-terminal ends. EC-SOD C, the high-heparin-affinity type, exposed to immobilized trypsin and plasmin was found to rapidly lose its affinity for heparin, without any loss of enzymic activity or major change in molecular mass as judged by size-exclusion chromatography. Heparin and dextran sulphate 5000 inhibited the proteolysis, suggesting that EC-SOD C sequestered by heparan sulphate proteoglycan in vivo is partially protected against proteolysis. The loss of heparin-affinity occurred with the stepwise formation of intermediates, and the pattern upon chromatography on heparin-Sepharose and subsequent immunoblotting was compatible with the notion that the changes are due to sequential truncations of heparin-binding domains from subunits composing the EC-SOD tetramers. A similar pattern with intermediates and apparent truncations has previously been found with EC-SOD of human plasma. The findings show that the unique design of the heparin-binding domain of EC-SOD allows easy modification of the heparin-affinity by means of limited proteolysis, and suggest that such proteolysis is a major contributor to the heterogeneity in heparin-affinity of EC-SOD in mammalian plasma.

Structural Analysis of the Heparin-Binding Site of the NC1 Domain of Collagen XIV by CD and NMR†,‡

Biochemistry ◽  
1999 ◽  
Vol 38 (20) ◽  
pp. 6479-6488 ◽  
Author(s):  
Roland Montserret ◽  
Elisabeth Aubert-Foucher ◽  
Michael J. McLeish ◽  
Joanna M. Hill ◽  
Damien Ficheux ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Binding Site ◽  
Heparin Binding ◽  
Heparin Binding Site ◽  
Nc1 Domain

Pulmonary arterial thrombosis in a neonate with homozygous deficiency of antithrombin III: successful outcome following pulmonary thrombectomy and infusions of antithrombin III concentrate

2000 ◽  
Vol 10 (3) ◽  
pp. 275-278 ◽  
Author(s):  
K. Roman ◽  
E. Rosenthal ◽  
R. Razavi
Keyword(s):  
Binding Site ◽  
Arterial Thrombosis ◽  
Antithrombin Iii ◽  
Pulmonary Trunk ◽  
Successful Outcome ◽  
Heparin Binding ◽  
The Third ◽  
Heparin Binding Site ◽  
Surgical Thrombectomy ◽  
Pulmonary Arterial

AbstractWe report a newborn male who presented with severe central cyanosis on the third day of life. Partial thrombotic obstruction of the pulmonary trunk secondary to Antithrombin III (homozygous defect of heparin binding site) deficiency was subsequently diagnosed. Surgical thrombectomy, and infusions of Antithrombin III concentrate, led to a successful outcome. We postulate that intrauterine thrombosis occurred to give this unusual presentation.

A collagen Vα1-derived fragment inhibits FGF-2 induced-angiogenesis by modulating endothelial cells plasticity through its heparin-binding site

2020 ◽  
Vol 94 ◽  
pp. 18-30 ◽  
Author(s):  
Tao Jia ◽  
Elisabeth Vaganay ◽  
Gilles Carpentier ◽  
Pauline Coudert ◽  
Veronica Guzman-Gonzales ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Binding Site ◽  
Heparin Binding ◽  
Heparin Binding Site
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