Studies on Antithrombin III (AT III)
نویسندگان
چکیده
منابع مشابه
Structural studies on the carbohydrate portion of human antithrombin III.
Human antithrombin III has been shown to contain four identical N-glycosidically linked carbohydrate chain per molecule. These carbohydrate chains have been investigated by sugar and methylation analysis before and after removal of N-acetylneuraminic acid residues. The chains have been further investigated by Smith degradation, trifluoroacetolytic degradation, and degradation after chromium tri...
متن کاملEffect of antithrombin III on neutrophil deformability.
As the spherical diameter of pulmonary capillaries is smaller than that of neutrophils, increased neutrophil stiffness or conversely, decreased neutrophil deformability is a key step in the initial sequestration of neutrophils within the lungs during inflammatory processes. Antithrombin III (AT) is known to exert a therapeutic effect against disseminated intravascular coagulation, and accumulat...
متن کاملAntithrombin III Inhibits Mesangial Cell
Thrombin stimulates and heparin and heparan sulfate inhibit mesangial cell proliferation. In addition, heparin has been shown to inhibit thrombin-stimulated smooth muscle cell proliferation. The anticoagulant action of heparin is mediated by antithrombin Ill. This study investigated whether heparin’s antiproliferative action is also mediated by antithrombin Ill. To this end, the effect of antit...
متن کاملAntithrombin III during liver transplantation.
A III (AT-III) is a liver-synthesized plasma glycoprotein of moderate size (58 kD) that can inhibit most of the activated serine proteases involved in coagulation (eg. thrombin. activated factor X. VII. etc). The inactivation involves formation of an irreversible complex. probably filtered from the circulation of the RES. The complex formation is a time-dependent reaction requiring minutes for ...
متن کاملAntimicrobial antithrombin III peptide 1 Antimicrobial effects of helix D-derived peptides of human antithrombin III*
Antithrombin III (ATIII) is a key antiproteinase involved in blood coagulation. Previous investigations have shown that ATIII is degraded by Staphylococcus aureus V8 protease, leading to release of heparin binding fragments derived from its D helix. As heparin binding and antimicrobial activity of peptides frequently overlap, we here set out to explore possible antibacterial effects of intact a...
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ژورنال
عنوان ژورنال: Blood & Vessel
سال: 1979
ISSN: 0386-9717,1884-2372
DOI: 10.2491/jjsth1970.10.59