Evidence that agonist-induced activation of calpain causes the shedding of procoagulant-containing microvesicles from the membrane of aggregating platelets-Reference-Cited by-同舟云学术

Evidence that agonist-induced activation of calpain causes the shedding of procoagulant-containing microvesicles from the membrane of aggregating platelets

Published:1991-07 Issue:20 Volume:266 Page:13289-13295
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Fox J.E.,Austin C.D.,Reynolds C.C.,Steffen P.K.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference46 articles.

1. Calcium-dependent proteolysis occurs during platelet aggregation.

2. Calpain I remains intact and intracellular during platelet activation. Immunochemical measurements with monoclonal and polyclonal antibodies

3. Identification of two proteins (actin-binding protein and P235) that are hydrolyzed by endogenous Ca2+-dependent protease during platelet aggregation.

4. Spectrin is associated with membrane-bound actin filaments in platelets and is hydrolyzed by the Ca2+-dependent protease during platelet activation

5. Human platelet calmodulin-binding proteins: identification and calcium-dependent proteolysis upon platelet activation

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