Cellular Arachidonate-releasing Function of Novel Classes of Secretory Phospholipase A2s (Groups III and XII)

Here we report cellular arachidonate (AA) release and prostaglandin (PG) production by novel classes of secretory phospholipase A 2 s (sPLA 2 s), groups III and XII. Human group III sPLA 2 promoted spontaneous AA release, which was augmented by interleukin-1, in HEK293 transfectants. The central sPL...

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Published inThe Journal of biological chemistry Vol. 278; no. 12; pp. 10657 - 10667
Main Authors Murakami, Makoto, Masuda, Seiko, Shimbara, Satoko, Bezzine, Sofiane, Lazdunski, Michael, Lambeau, Gérald, Gelb, Michael H, Matsukura, Satoshi, Kokubu, Fumio, Adachi, Mitsuru, Kudo, Ichiro
Format Journal Article
LanguageEnglish
Published United States American Society for Biochemistry and Molecular Biology 21.03.2003
Subjects
Arachidonic Acid - metabolism
Cell Line
Cyclooxygenase 2
Dinoprostone - biosynthesis
Group III Phospholipases A2
Heparin - analogs & derivatives
Heparin - pharmacology
Humans
Isoenzymes - biosynthesis
Membrane Proteins
Phospholipases A - analysis
Phospholipases A - physiology
Prostaglandin-Endoperoxide Synthases - biosynthesis
Proteoglycans - pharmacology
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Summary:Here we report cellular arachidonate (AA) release and prostaglandin (PG) production by novel classes of secretory phospholipase A 2 s (sPLA 2 s), groups III and XII. Human group III sPLA 2 promoted spontaneous AA release, which was augmented by interleukin-1, in HEK293 transfectants. The central sPLA 2 domain alone was sufficient for its in vitro enzymatic activity and for cellular AA release at the plasma membrane, whereas either the unique N- or C-terminal domain was required for heparanoid-dependent action on cells to augment AA release, cyclooxygenase-2 induction, and PG production. Group III sPLA 2 was constitutively expressed in two human cell lines, in which other sPLA 2 s exhibited different stimulus inducibility. Human group XII sPLA 2 had a weak enzymatic activity in vitro and minimally affects cellular AA release and PG production. Cells transfected with group XII sPLA 2 exhibited abnormal morphology, suggesting a unique functional aspect of this enzyme. Based on the present results as well as our current analyses on the group I/II/V/X sPLA 2 s, general properties of cellular actions of a full set of mammalian sPLA 2 s in regulating AA metabolism are discussed.
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ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M211325200