Cloning, expression and partial characterization of a novel rat phospholipase A2.
We report the cloning of a novel rat cDNA encoding a Ca(2+)-dependent, low molecular weight phospholipase A2 (PLA2). A rat RNA blot hybridized with the cDNA exhibited a putative 2.4 kb transcript in heart. When the cDNA was expressed in human 293s cells, PLA2 activity accumulated in the culture medium. This conditioned medium optimally hydrolyzed the phospholipids of [1-14C]oleate-labeled Escherichia coli at neutral to alkaline pH with 10 mM or greater Ca2+. When single substrates were tested, L-alpha-palmitoyl-2-oleoyl phosphatidylcholine was more efficiently hydrolyzed than L-alpha-1-palmitoyl-2-arachidonyl phosphatidylcholine, L-alpha-1-palmitoyl-2-arachidonyl phosphatidylethanolamine or L-alpha-1-stearoyl-2-arachidonyl phosphatidylinositol.
Chen
J
J
Department of Medical and Molecular Genetics, Indiana University School of Medicine, Indianapolis 46202-5251.
Engle
S J
SJ
Seilhamer
J J
JJ
Tischfield
J A
JA
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002460:Cell Line; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000737:chemistry; D004926:Escherichia coli; D015870:Gene Expression; D006801:Humans; D008969:Molecular Sequence Data; D009206:Myocardium / Q000201:enzymology*; D010741:Phospholipases A / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D054467:Phospholipases A2; D010743:Phospholipids / Q000378:metabolism; D051381:Rats; D016415:Sequence Alignment
D018076:DNA, Complementary; D010743:Phospholipids; D010741:Phospholipases A; D054467:Phospholipases A2