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Journal of Endocrinology (2009) 202, 199-205       DOI: 10.1677/JOE-08-0363
© 2009 Society for Endocrinology
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Angiotensin II enhances the increase in monocyte chemoattractant protein-1 production induced by tumor necrosis factor-{alpha} from 3T3-L1 preadipocytes

 Sachie Asamizu, Masaharu Urakaze, Chikaaki Kobashi, Manabu Ishiki, Amal Khalifa Norel Din, Shiho Fujisaka, Yukiko Kanatani, Agussalim Bukahari, Satoko Senda, Hikari Suzuki, Yuh Yamazaki, Minoru Iwata, Isao Usui, Katsuya Yamazaki, Hiroshi Ogawa, Masashi Kobayashi and Kazuyuki Tobe

1st Department of Medicine, Toyama University, Sugitani 2630, Toyama-shi 930-0194, Japan

(Correspondence should be addressed to M Urakaze; Email: murakaze{at}med.u-toyama.ac.jp)

Monocyte chemoattractant protein-1 (MCP-1) and angiotensin II (Ang II) in adipose tissue are thought to induce systemic insulin resistance in rodents; but the precise mechanism is not fully clarified. We examined the mechanism of Ang II-induced and/or tumor necrosis factor-{alpha} (TNF-{alpha})-induced MCP-1 production from 3T3-L1 preadipocytes. The MCP-1 protein and MCP-1 mRNA expression in 3T3-L1 preadipocytes were increased significantly by stimulation with TNF-{alpha}. We found no significant increase in MCP-1 concentrations by Ang II alone; but it enhanced the TNF-{alpha}-induced MCP-1 mRNA expression in a dose-dependent manner. Then, we examined the effect of Ang II and/or TNF-{alpha} on phosphorylation of extracellular signal-regulated kinase (ERK), p38MAPK, and I{kappa}B-{alpha}. Ang II and TNF-{alpha} clearly enhanced ERK and p38MAPK phosphorylation. I{kappa}B-{alpha} phosphorylation was enhanced by TNF-{alpha}, but not by Ang II. The MCP-1 mRNA expression induced by TNF-{alpha} and co-stimulation with Ang II was inhibited by either ERK inhibitor, p38MAPK inhibitor or NF-{kappa}B inhibitor. Moreover, Ang II enhanced the activation of AP-1 (c-fos) induced by TNF-{alpha}. Our results suggest that Ang II may serve as an additional stimulus on the TNF-{alpha}-induced MCP-1 production through the ERK-and p38MAPK-dependent pathways probably due to AP-1 activation.






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