Inositol Polyphosphate 4-Phosphatase Is Inactivated by Calpain-mediated Proteolysis in Stimulated Human Platelets
Open Access
- 1 April 1997
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (17) , 10987-10989
- https://doi.org/10.1074/jbc.272.17.10987
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Direct Regulation of the Akt Proto-Oncogene Product by Phosphatidylinositol-3,4-bisphosphateScience, 1997
- Phosphorylation of the Platelet p47 Phosphoprotein Is Mediated by the Lipid Products of Phosphoinositide 3-KinaseJournal of Biological Chemistry, 1995
- Calpain Cleavage of the Cytoplasmic Domain of the Integrin β2 SubunitPublished by Elsevier ,1995
- Phosphatidylinositol( , , ) -Trisphosphate Stimulates Phosphorylation of Pleckstrin in Human PlateletsPublished by Elsevier ,1995
- Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transductionNature, 1995
- The Isolation and Characterization of cDNA Encoding Human and Rat Brain Inositol Polyphosphate 4-PhosphatasePublished by Elsevier ,1995
- Endogenous Cleavage of Phospholipase C-β3 by Agonist-induced Activation of Calpain in Human PlateletsPublished by Elsevier ,1995
- Evidence that activation of platelet calpain is induced as a consequence of binding of adhesive ligand to the integrin, glycoprotein IIb-IIIa.The Journal of cell biology, 1993
- PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cellsCell, 1989
- Amino Acid Sequences Common to Rapidly Degraded Proteins: The PEST HypothesisScience, 1986