Document Detail


Cell surface activities of the human type 2b phosphatidic acid phosphatase.
MedLine Citation:
PMID:  10739957     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Several isozymes of mammalian type 2, Mg(2+)-independent phosphatidic acid phosphatase (PAP-2) have recently been cloned, and they are predicted to have their catalytic sites exposed at the cell surface membranes. We investigated the mode of utilization of extracellular lipid substrates by the human PAP-2b expressed in HEK293 cells as a green fluorescent fusion protein. We first confirmed the plasma membrane localization of the expressed PAP-2b. PAP-2b actively hydrolyzed exogenously added lysophosphatidic acid and short-chain phosphatidic acid. In the case of dephosphorylation of lysophosphatidic acid, the reaction products, including inorganic phosphate and monoacylglycerol, were recovered exclusively in the extracellular medium. Interestingly, PAP-2b exhibited negligible activities toward long-chain phosphatidic acid either exogenously when added or generated within the membranes by treating the cells with bacterial phospholipase D. These findings indicate that PAP-2b acts at the outer leaflet of cell surface bilayers and can account for the ecto-PAP activities previously described for various types of cells.
Authors:
T Ishikawa; M Kai; I Wada; H Kanoh
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of biochemistry     Volume:  127     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  2000 Apr 
Date Detail:
Created Date:  2000-07-27     Completed Date:  2000-07-27     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  645-51     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Sapporo Medical University School of Medicine, Japan.
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MeSH Terms
Descriptor/Qualifier:
Cell Line
Cell Membrane / chemistry,  enzymology*
Cell Membrane Permeability
Green Fluorescent Proteins
Humans
Luminescent Proteins
Lysophospholipids / metabolism
Membrane Proteins / metabolism
Microscopy, Confocal
Phosphatidate Phosphatase / genetics,  metabolism*
Phosphatidic Acids / metabolism
Phospholipase D / metabolism
Phosphorylation
Recombinant Fusion Proteins / metabolism
Transfection
Chemical
Reg. No./Substance:
0/Luminescent Proteins; 0/Lysophospholipids; 0/Membrane Proteins; 0/Phosphatidic Acids; 0/Recombinant Fusion Proteins; 147336-22-9/Green Fluorescent Proteins; EC 3.1.3.-/phosphatidic acid phosphatase type 2; EC 3.1.3.4/Phosphatidate Phosphatase; EC 3.1.4.4/Phospholipase D

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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