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Originally published In Press as doi:10.1074/jbc.M010201200 on March 23, 2001

J. Biol. Chem., Vol. 276, Issue 24, 21854-21862, June 15, 2001
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Secretory Phospholipase A2 Mediates Cooperative Prostaglandin Generation by Growth Factor and Cytokine Independently of Preceding Cytosolic Phospholipase A2 Expression in Rat Gastric Epithelial Cells*

Satoshi AkibaDagger , Ryo Hatazawa, Kyoko Ono, Kazuyuki Kitatani, Misako Hayama, and Takashi Sato

From the Department of Pathological Biochemistry, Kyoto Pharmaceutical University, Misasagi, Yamashina-ku, Kyoto 607-8414, Japan

Transforming growth factor (TGF)-alpha and interleukin (IL)-1beta are responsible for the healing of gastric lesions through, in part, prostaglandin (PG) generation. We examined the contribution of cytosolic and secretory phospholipase A2s (cPLA2 and sPLA2) to the PG generation by rat gastric epithelial cells in response to both stimuli. Stimulation with TGF-alpha for 24 h increased cPLA2 and cyclooxygenase (COX)-2 markedly, PGE2 slightly, and type IIA sPLA2 and COX-1 not at all, whereas IL-1beta increased sPLA2 only. Both stimuli synergistically increased PGE2, sPLA2, and the two COXs but not cPLA2. The onset of the PGE2 generation paralleled the sPLA2 release but was apparently preceded by increases in cPLA2 and the two COXs. The increase in PGE2 was impaired by inhibitors for sPLA2 and COX-2 but not COX-1. cPLA2 inhibitors suppressed PGE2 generation by TGF-alpha alone but not augmentation of PGE2 generation or sPLA2 release by IL-1beta in combination with TGF-alpha . Furthermore, despite an increase in cPLA2 including its phosphorylated form (phosphoserine), A23187-induced arachidonic acid liberation was impaired in the TGF-alpha /IL-1beta -stimulated cells, in which p11, a putative cPLA2 inhibitory molecule, was also increased and co-immunoprecipitated with cPLA2. These results suggest that synergistic stimulation of sPLA2 and COX-2 expression by TGF-alpha and IL-1beta results in an increase in PGE2. Presumably, the preceding cPLA2 expression is not involved in the PGE2 generation, because of impairment of its hydrolytic activity in the stimulated cells.

* This work was supported by a grant-in-aid for scientific research and the Frontier Research Program of the Ministry of Education, Science, Sports and Culture of Japan.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dept. of Pathological Biochemistry, Kyoto Pharmaceutical University Misasagi, Yamashina-ku, Kyoto 607-8414, Japan. Fax: 81-75-595-4759; E-mail: akiba@mb.kyoto-phu.ac.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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