RGD Reference Report - Serine phospholipid-specific phospholipase A that is secreted from activated platelets. A new member of the lipase family. - Rat Genome Database

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Serine phospholipid-specific phospholipase A that is secreted from activated platelets. A new member of the lipase family.

Authors: Sato, T  Aoki, J  Nagai, Y  Dohmae, N  Takio, K  Doi, T  Arai, H  Inoue, K 
Citation: Sato T, etal., J Biol Chem 1997 Jan 24;272(4):2192-8.
RGD ID: 633839
Pubmed: PMID:8999922   (View Abstract at PubMed)

Rat platelets secrete two types of phospholipases upon stimulation; one is type II phospholipase A2 and the other is serine-phospholipid-selective phospholipase A. In the current study we purified serine-phospholipid-selective phospholipase A and cloned its cDNA. The final preparation, purified from extracellular medium of activated rat platelets, gave a 55-kDa protein band on SDS-polyacrylamide gel electrophoresis. [3H]Diisopropyl fluorophosphate, an inhibitor of the enzyme, labeled the 55-kDa protein, suggesting that this polypeptide possesses active serine residues. The cDNA for the enzyme was cloned from a rat megakaryocyte cDNA library. The predicted 456-amino acid sequence contains a putative short N-terminal signal sequence and a GXSXG sequence, which is a motif of an active serine residue of serine esterase. Amino acid sequence homology analysis revealed that the enzyme shares about 30% homology with mammalian lipases (lipoprotein lipase, hepatic lipase, and pancreatic lipase). Regions surrounding the putative active serine, histidine, and aspartic acid, which may form a "lipase triad," were highly conserved among these enzymes. The recombinant protein, which we expressed in Sf9 insect cells using the baculovirus system, hydrolyzed a fatty acyl residue at the sn-1 position of lysophosphatidylserine and phosphatidylserine, but did not appreciably hydrolyze phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, phosphatidic acid, and triglyceride. The present enzyme, named phosphatidylserine-phospholipase A1, is the first phospholipase that exclusively hydrolyses the sn-1 position and has a strict head group specificity for the substrate.

Objects referenced in this article
Gene Pla1a phospholipase A1 member A Rattus norvegicus

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