Calpain-induced down-regulation of protein kinase C inhibits dense-granule secretion in human platelets. Inhibition of platelet aggregation or calpain activity preserves protein kinase C and restores full secretion-Reference-Cited by-同舟云学术

Calpain-induced down-regulation of protein kinase C inhibits dense-granule secretion in human platelets. Inhibition of platelet aggregation or calpain activity preserves protein kinase C and restores full secretion

Published:1994-12 Issue:3 Volume:1224 Page:480-488
ISSN:0167-4889
Container-title:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Author:

Patel Yatin,Kakkar Vijay V.,Authi Kalwant S.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology

Reference43 articles.

1. Inositol trisphosphate and diacylglycerol as second messengers

2. Inositol 1,4,5-trisphosphate releases Ca2+ from a Ca2+-transporting membrane vesicle fraction derived from human platelets.

3. Inositol 1,4,5-trisphosphate-induced release of sequestered Ca2+ from highly purified human platelet intracellular membranes

4. The molecular heterogeneity of protein kinase C and its implications for cellular regulation

5. Direct activation of calcium-activated, phospholipid-dependent protein kinase by tumor-promoting phorbol esters.

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