Thrombospondin Interaction With Plasminogen . Evidence for Binding to a Specific Region
نویسندگان
چکیده
Platelet thrombospondin interacts with plasminogen in a specific and saturable manner. Thrombospondin was found to specifically bind to plasminogen and the nonenzyme chain of plasmin. Preincubation of 125l-labeled thrombospondin with 30 mmol/L lysine was without effect in the binding of thrombospondin to immobilized plasminogen; preincubation of ‘ l-labeled plasminogen with 30 mmol/L lysine, on the other hand, significantly reduced the binding of plasminogen to immobilized thrombospondin. suggesting that the interaction of thrombospondin with plasminogen is not the direct result of the lysine binding sites of plasminogen. Arginine and benzamidine, ligands known to specifically bind to the kringle 5 domain of plasminogen. blocked the binding of thrombospondin to plasminogen. Limited elastase proteolysis of plasminogen and plasmin resulted in the generation of two distinct thrombospondin
منابع مشابه
Thrombospondin interaction with plasminogen. Evidence for binding to a specific region of the kringle structure of plasminogen.
Platelet thrombospondin interacts with plasminogen in a specific and saturable manner. Thrombospondin was found to specifically bind to plasminogen and the nonenzyme chain of plasmin. Preincubation of 125I-labeled thrombospondin with 30 mmol/L lysine was without effect in the binding of thrombospondin to immobilized plasminogen; preincubation of 125I-labeled plasminogen with 30 mmol/L lysine, o...
متن کاملاثر آنتی بادی های منوکلونال ضد پلاسمینوژن انسانی بر فعال شدن گلو-پلاسمینوژن انسانی بوسیله فعال کننده های پلاسمینوژن
Background: Human plasminogen is a plasma glycoprotein synthesized mainly in the liver. Conversion of plasminogen to plasmin by plasminogen activators is a key event in the fibrinolytic system. In this study, we investigated the effects of two anti-human plasminogen monoclonal antibodies, A1D12 and MC2B8 on Glu-plasminogen activation in presence of u-PA, t-PA and streptokinase. Methods: Produci...
متن کاملVersican-thrombospondin-1 binding in vitro and colocalization in microfibrils induced by inflammation on vascular smooth muscle cells.
We identified a specific interaction between two secreted proteins, thrombospondin-1 and versican, that is induced during a toll-like receptor-3-dependent inflammatory response in vascular smooth muscle cells. Thrombospondin-1 binding to versican is modulated by divalent cations. This interaction is mediated by interaction of the G1 domain of versican with the N-module of thrombospondin-1 but o...
متن کاملELUCIDATION OF pK VALUES FOR ACTIVE SITE OF HORSERADISH PEROXIDASE AND BINDING STUDY OF INTERACTION WITH N-PHENYL BENZHYDROXAMIC ACID USING A SPECIAL DIFFERENCE SPECTROPHOTOMETRIC TECHNIQUE
The binding behavior of a competitive inhibitor, N-phenylbenzhydroxamic acid (BHA) against horseradish peroxidase (HRP) was studied in order to understand and predict the interaction mechanism of hydrogen donors with the enzyme. The dissociation constants of the complexes of HRP-BHA, HRP-donor and HRP-BHA-azide were estimated at specified conditions by difference spectroscopy. The binding s...
متن کاملIn Silico Design and Verification of LAMP-BDNF Chimeric Protein for Presentation of BDNF on the Surface of Exosomes for Drug Delivery Through Blood-Brain Barrier
Background and purpose: The mature form of brain-derived neurotrophic factor (BDNF) binds to BDNF/NT-3 growth factors receptor (Trk-B). This binding leads to activation of Ras–MAPK pathway which is integrated with cell growth and proliferation. The BDNF deficiency is correlated with various diseases and affects aging and miscellaneous. In the present study we aimed to design a chimeric LAMP-BDN...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2005