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Nucleic Acids Research 2005 33(4):1337-1351; doi:10.1093/nar/gki275
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Published online 1 March 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

{alpha}2(I) collagen gene regulation by protein kinase C signaling in human dermal fibroblasts

Masatoshi Jinnin, Hironobu Ihn*, Kenichi Yamane, Yoshihiro Mimura, Yoshihide Asano and Kunihiko Tamaki

Department of Dermatology, Faculty of Medicine, University of Tokyo 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8655, Japan

*To whom correspondence should be addressed. Tel: +81 3 3815 5411; Fax: +81 3 3814 1503; Email: IN-DER{at}h.u-tokyo.ac.jp

Received January 9, 2005. Accepted February 9, 2005.

We investigated the mechanisms by which protein kinase C (PKC) regulates the expression of the {alpha}2(I) collagen gene in normal dermal fibroblasts. Reduction of PKC-{alpha} activity by treatment with Gö697-6 or by overexpression of a dominant negative (DN) mutant form decreased {alpha}2(I) collagen gene expression. This decrease required a sequence element in the collagen promoter that contains Sp1/Sp3 binding sites. Reduction of PKC-{delta} activity by rottlerin or overexpression of DN PKC-{delta} also decreased {alpha}2(I) collagen gene expression. This effect required a separate sequence element containing Sp1/Sp3-binding sites and an Ets-binding site. In both cases, point mutations within the response elements abrogated the response to PKC inhibition. Forced overexpression of Sp1 rescued the PKC inhibitor-mediated reduction in collagen protein expression. A DNA affinity precipitation assay revealed that inhibition of PKC-{delta} by rottlerin increased the binding activity of endogenous Fli1 and decreased that of Ets1. On the other hand, TGF-ß1, which increased the expression of PKC-{delta}, had the opposite effect, increasing the binding activity of Ets1 and decreasing that of Fli1. Our results suggest that PKC-{delta} is involved in the regulation of the {alpha}2(I) collagen gene in the presence or absence of TGF-ß. Alteration of the balance of Ets1 and Fli1 may be a novel mechanism regulating {alpha}2(I) collagen expression.


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