Leupeptin does not affect the normal signal transduction mechanism in platelets
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(89)80573-3/fullpdf
Reference14 articles.
1. Calcium‐dependent proteases: an enzyme system active at cellular membranes?
2. Leupeptin selectively inhibits human platelet responses induced by thrombin and trypsin; a role for proteolytic activation of phospholipase C
3. What turns platelets on?
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1. Acceleration of Ca2+ ionophore-induced arachidonic acid liberation by thrombin without the proteolytic action toward the receptor in human platelets;European Journal of Biochemistry;2001-12-25
2. Proteolysis of protein kinase C: mM and μM calcium-requiring calpains have different abilities to generate, and degrade the free catalytic subunit, protein kinase M;FEBS Letters;1995-07-03
3. Degradation of protein kinase Cα and its free catalytic subunit, protein kinase M, in intact human neuroblastoma cells and under cell-free conditions;FEBS Letters;1994-08-22
4. Leupeptin inhibits phospholipases D and C activation in rat hepatocytes;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;1994-08
5. Different patterns of protein kinase C redistribution mediated by α1-adrenoceptor stimulation and phorbol ester in rat isolated left ventricular papillary muscle;British Journal of Pharmacology;1992-09
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