Document Detail


Hydrolysis of short acyl chain inositol lipids by phospholipase C-delta 1.
MedLine Citation:
PMID:  8380575     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We investigated the relationship between substrate aggregation and activation of phosphoinositide-specific phospholipase C-delta 1 (PLC-delta 1), isolated from bovine brain cytosol. The inositol lipids 1,2-dibutyryl-sn-glycero-3-phosphoinositol (di-C4-PI), 1,2-dihexanoyl-sn-glycero-3-phosphoinositol (di-C6-PI), and 1,2-dioctanoyl-sn-glycero-3-phosphoinositol (di-C8-PI) were prepared from synthetic cytidine diphosphate diglyceride analogs in a reaction with myo-inositol catalyzed by yeast phosphatidylinositol synthase. All three lipids served as substrates for PLC-delta 1 at concentrations significantly below their critical micelle concentration (cmc). Under these conditions, steps that might limit the reaction rate, such as membrane adsorption or penetration into the phospholipid surface, were eliminated. Below the cmc, the concentration of lipid substrate required to produce hydrolysis followed the order: di-C8-PI < di-C6-PI << di-C4-PI. Calcium was essential for hydrolysis of the short chain substrates at all lipid concentrations tested. The dependence of the reaction on calcium suggests that this ion activates PLC-delta 1 at a step other than adsorption to or penetration of the membrane surface. As the concentration of di-C8-PI was raised above the cmc, the reaction velocity increased 2-3-fold. These results are consistent with the idea that micellar or bilayer aggregates of phosphoinositol are not required for PLC-catalyzed hydrolysis, although the reaction rate is enhanced by micelle formation.
Authors:
M J Rebecchi; R Eberhardt; T Delaney; S Ali; R Bittman
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  268     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1993 Jan 
Date Detail:
Created Date:  1993-02-18     Completed Date:  1993-02-18     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1735-41     Citation Subset:  IM    
Affiliation:
Department of Physiology and Biophysics, State University of New York, Stony Brook 11794.
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MeSH Terms
Descriptor/Qualifier:
Animals
Brain / enzymology
CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase
Calcium / pharmacology
Cattle
Cytosol / enzymology
Enzyme Activation / drug effects
Hydrolysis
Kinetics
Phosphatidylinositols / metabolism*
Phosphotransferases / metabolism
Saccharomyces cerevisiae / enzymology
Substrate Specificity
Transferases (Other Substituted Phosphate Groups)*
Type C Phospholipases / metabolism*
Grant Support
ID/Acronym/Agency:
GM-43422/GM/NIGMS NIH HHS; HL-16660/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Phosphatidylinositols; 105172-95-0/1,2-dioctanoyl-sn-glycero-3-phosphoinositol; 148437-41-6/1,2-dihexanoyl-sn-glycero-3-phosphoinositol; 148504-92-1/1,2-dibutyryl-sn-glycero-3-phosphoinositol; 7440-70-2/Calcium; EC 2.7.-/Phosphotransferases; EC 2.7.8.-/Transferases (Other Substituted Phosphate Groups); EC 2.7.8.11/CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase; EC 3.1.4.-/Type C Phospholipases

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