Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Molina y Vedia, L. M.
Right arrow Articles by Lapetina, E. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Molina y Vedia, L. M.
Right arrow Articles by Lapetina, E. G.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 261, Issue 23, 10493-10495, 08, 1986

Phorbol 12,13-dibutyrate and 1-oleyl-2-acetyldiacylglycerol stimulate inositol trisphosphate dephosphorylation in human platelets

LM Molina y Vedia and EG Lapetina

Inositol trisphosphate (IP3) is formed in response to specific agonists that cause activation of phospholipase C and degradation of phosphatidylinositol bisphosphate. IP3 is a second messenger that releases Ca2+ from the dense tubular system to the cytosol in stimulated platelets. Our present information indicates that [3H]IP3 is dephosphorylated to [3H]inositol bisphosphate (IP2) and [3H]inositol monophosphate (IP) by human platelets treated with 0.05-0.10% Triton X- 100. This dephosphorylation of [3H]IP3 to [3H]IP2 and [3H]IP is also observed when platelets are permeabilized by electrical stimulation or by 20 micrograms/ml saponin. These detergents or electropermeabilization allow IP3 to access cytosolic IP3 phosphatase. Pretreatment of intact platelets with phorbol dibutyrate and 1-oleyl-2- acetyldiacylglycerol for 30 s, at concentrations that maximally activate protein kinase C, stimulates the conversion of IP3 to IP2 and IP. This suggests a role for protein kinase C in the regulation of IP3 degradation.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
BloodHome page
M. M. Teixeira, M. A. Giembycz, M. A. Lindsay, and P. G. Hellewell
Pertussis Toxin Shows Distinct Early Signalling Events in Platelet-Activating Factor-, Leukotriene B4-, and C5a-Induced Eosinophil Homotypic Aggregation In Vitro and Recruitment In Vivo
Blood, June 15, 1997; 89(12): 4566 - 4573.
[Abstract] [Full Text] [PDF]


Home page
ScienceHome page
P. Majerus, T. Connolly, H Deckmyn, T. Ross, T. Bross, H Ishii, V. Bansal, and D. Wilson
The metabolism of phosphoinositide-derived messenger molecules
Science, December 19, 1986; 234(4783): 1519 - 1526.
[Abstract] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1986 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement