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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Abstract 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.
AbstractList 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.
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.
Author Seiko Masuda
Ichiro Kudo
Michael H. Gelb
Sofiane Bezzine
Makoto Murakami
Satoko Shimbara
Michael Lazdunski
Mitsuru Adachi
Gérald Lambeau
Satoshi Matsukura
Fumio Kokubu
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  givenname: Makoto
  surname: Murakami
  fullname: Murakami, Makoto
  email: mako@pharm.showa-u.ac.jp
  organization: Department of Health Chemistry, School of Pharmaceutical Sciences, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan. mako@pharm.showa-u.ac.jp
– sequence: 2
  givenname: Seiko
  surname: Masuda
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  givenname: Satoko
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  givenname: Gérald
  surname: Lambeau
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  givenname: Ichiro
  surname: Kudo
  fullname: Kudo, Ichiro
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SSID ssj0000491
Score 2.0783775
Snippet 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...
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...
SourceID hal
proquest
crossref
pubmed
highwire
SourceType Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 10657
SubjectTerms 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
Title Cellular Arachidonate-releasing Function of Novel Classes of Secretory Phospholipase A2s (Groups III and XII)
URI http://www.jbc.org/content/278/12/10657.abstract
https://www.ncbi.nlm.nih.gov/pubmed/12522102
https://search.proquest.com/docview/73102731
https://hal.science/hal-00091064
Volume 278
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