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PMID: 2827632 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Ca2+ regulation of 1-(3-sn-phosphatidyl)-1D-myo-inositol 4-phosphate formation and hydrolysis on sarcoplasmic-reticular Ca2+-transport ATPase. A new principle of phospholipid turnover regulation.

The Biochemical journal ·Vol. 247 ·No. 3 ·1987-11-01 ·Pages 579-87

Schäfer M, Behle G, Varsányi M, Heilmeyer LM

Abstract

Lipid phosphorylation was shown to occur on the isolated sarcoplasmic-reticulum (SR) Ca2+-transport ATPase. More than 95% of the radioactivity incorporated on incubation of the SR ATPase with [gamma-32P]ATPMg can be extracted with acidic organic solvents and was identified as 1-(3-sn-phosphatidyl)-1D-myo-inositol 4-phosphate (PtdIns4P) [Varsányi, Toelle, Heilmeyer, Dawson & Irvine (1983) EMBO J. 2, 1543-1548]. This lipid phosphorylation is only observed at nanomolar concentrations of free Ca2+; in the presence of micromolar free Ca2+ PtdIns4P disintegrates rapidly. Also, upon blockade of the kinase reaction PtdIns4P decomposes, indicating a PtdIns/PtdIns4P turnover. The PtdIns4P concentration is dependent on the free Ca2+ concentration, being half-maximal at 35 nM-Ca2+. PtdIns4P hydrolysis is catalysed by a PtdIns4P phosphomonoesterase; accordingly no diacylglycerol is formed, which would be a product of a phosphodiesteratic cleavage. Fluoride inhibits this phosphomonoesterase. Ca2+ does not influence directly either the PtdIns kinase or the PtdIns4P phosphomonoesterase. PtdIns4P forms a tight complex with the transport ATPase, from which it can be removed only by chromatography on heparin-agarose in the presence of Triton X-100. It is concluded that Ca2+ regulates the PtdIns/PtdIns4P turnover by availability of substrate, depending on the Ca2+-transport-ATPase conformation, which traps or exposes the respective lipid head groups.

MeSH Terms
1-Phosphatidylinositol 4-Kinase Animals Calcium/pharmacology Calcium-Transporting ATPases/metabolism Chromatography, Agarose Chromatography, Ion Exchange Fluorides/pharmacology Hydrolysis Phosphatidylinositol Phosphates Phosphatidylinositols/biosynthesis,metabolism Phospholipids/metabolism Phosphoric Monoester Hydrolases/metabolism Phosphotransferases/metabolism Sarcoplasmic Reticulum/drug effects,enzymology,metabolism
Chemicals
Phosphatidylinositol Phosphates Phosphatidylinositols Phospholipids phosphatidylinositol 4-phosphate Phosphotransferases 1-Phosphatidylinositol 4-Kinase Phosphoric Monoester Hydrolases phosphatidylinositol-3,4-bisphosphate 4-phosphatase Calcium-Transporting ATPases Fluorides Calcium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Schäfer M
Lehrstuhl für Physiologische Chemie, Ruhr-Universität Bochum, Federal Republic of Germany.
Behle G
Varsányi M
Heilmeyer L M
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2470579
Published
1987-11-01
Pages
579-87
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1148452
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2470579 PMC Full Text View journal details
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