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Am J Physiol Endocrinol Metab (March 23, 2004). doi:10.1152/ajpendo.00390.2003
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Submitted on August 28, 2003
Accepted on December 12, 2003

Assessment of the Function of the {beta}C Subunit of Activin in Cultured Heptocytes

Wataru Wada1, Akito Maeshima2, You-Qing Zhang2, Yoshihisa Hasegawa3, Hiroyuki Kuwano4, and Itaru Kojima2*

1 Institute for Molecular and Cellular Regulation, Gunma University, Japan; Department of General Surgical Science, Gunma University Graduate School of Medicine, Japan
2 Institute for Molecular and Cellular Regulation, Gunma University, Japan
3 School of Veterinary Medicine and Animal Science, Kitasato University, Japan
4 Department of General Surgical Science, Gunma University Graduate School of Medicine, Japan

* To whom correspondence should be addressed. E-mail: ikojima{at}showa.gunma-u.ac.jp.

We assessed the function of the {beta}C subunit of activin in hepatocytes. We studied the effect of conditioned medium of CHO cell line stably expressing the {beta}C gene (CHO-{beta}C) on growth of AML12 hepatocytes. We also examined the effect of recombinant activin C and transfection of the {beta}C gene using adenovirus vector. CHO-{beta}C secreted activin C, a homodimer of the {beta}C, as well as precursors of the {beta}C. The conditioned medium of CHO-{beta}C increased both [3H]thymidine incorporation and the cell number in AML12 cells. It also supported survival of AML12 cells in a serum-free condition. Recombinant human activin C also increased both [3H]thymidine incorporation and the number of AML12 cells. Transfection of AML12 cells with the {beta}C subunit led to the stimulation of [3H]thymidine incorporation. Analysis of the conditioned medium revealed that the {beta}C subunit formed a heterodimer with the endogenous {beta}A, the formation of which was dependent on the amount of the {beta}C expressed. Recombinant activin C did not affect the binding of [125I]activin A to its receptor or follistatin. These results indicate that activin C stimulates growth of AML12 cells. The {beta}C subunit modifies the function of the {beta}A subunit by multiple mechanisms.




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