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Originally published In Press as doi:10.1074/jbc.M001220200 on July 12, 2000

J. Biol. Chem., Vol. 275, Issue 39, 29955-29959, September 29, 2000
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Thrombin Induces NO Release from Cultured Rat Microglia via Protein Kinase C, Mitogen-activated Protein Kinase, and NF-kappa B*

Jooyoung RyuDagger , Hankyoung PyoDagger , Ilo Jou, and Eunhye Joe§

From the Department of Pharmacology, Ajou University School of Medicine, Suwon, 442-721, Korea

Microglia, brain resident macrophages, become activated in brains injured due to trauma, ischemia, or neurodegenerative diseases. In this study, we found that thrombin treatment of microglia induced NO release/inducible nitric-oxide synthase expression, a prominent marker of activation. The effect of thrombin on NO release increased dose-dependently within the range of 5-20 units/ml. In immunoblot analyses, inducible nitric-oxide synthase expression was detected within 9 h after thrombin treatment. This effect of thrombin was significantly reduced by protein kinase C inhibitors, such as Go6976, bisindolylmaleimide, and Ro31-8220. Within 15 min, thrombin activated three subtypes of mitogen-activated protein kinases: extracellular signal-regulated kinase, p38, and c-Jun N-terminal kinase/stress-activated protein kinase. Inhibition of the extracellular signal-regulated kinase pathway and p38 reduced the NO release of thrombin-treated microglia. Thrombin also activated nuclear factor kappa B (NF-kappa B) within 5 min, and N-acetyl cysteine, an inhibitor of NF-kappa B, reduced NO release. However, thrombin receptor agonist peptide (an agonist of protease activated receptor-1 (PAR-1)), could not mimic the effect of thrombin, and cathepsin G, a PAR-1 inhibitor, did not reduce the effect of thrombin. These results suggest that thrombin can activate microglia via protein kinase C, mitogen-activated protein kinases, and NF-kappa B but that this occurs independently of PAR-1.

* This work was supported by Grant HMP-98-N-6-0010 from the 98 Good Health R & D Program Ministry of Health and Welfare Korea, Grant 1999-2-207-004-5 from the interdisciplinary research program of the Korea Science and Engineering Foundation (KOSEF), and KOSEF through the Brain Disease Research Center at Ajou University (to E. J.).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 These authors contributed equally to this work.

§ To whom correspondence should be addressed: san-5 Woncheon-dong Paldal-gu Suwon, Kyunggi-do, 442-721, Korea. Tel.: 82-31-219-5062; Fax: 82-31-219-5069; E-mail: ehjoe@madang.ajou.ac.kr.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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