Thrombospondin Interaction With Plasminogen . Evidence for Binding to a Specific Region

نویسندگان

  • Theresa Bacon-Baguley
  • Suzanne Kendra-Franczak
  • Mark T. Cederholm
  • Daniel A. Walz
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

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Thrombospondin interaction with plasminogen. Evidence for binding to a specific region of the kringle structure of plasminogen.

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تاریخ انتشار 2005