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,
*
Laboratory Animal Research Center, RIKEN, Wako, Saitama, Japan;
Department of Nutrition, Azabu University School of Veterinary Medicine, Sagamihara, Kanagawa, Japan; and
Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109
The role of activin, a dimer of inhibin ß subunit, in mouse
peritoneal macrophages was evaluated. Activin activity in the cultured
macrophages was augmented in response to activation by LPS. In Western
blot analysis, immunoreactive activin A was detected in the culture
medium only when the macrophages were stimulated by LPS. Although mRNA
expression of ßA subunit was detected, that of 
and ßB subunit
was not found in macrophages by reverse RT-PCR. The activin ßA mRNA
level was increased in macrophages by LPS, suggesting that the activin
production augmented by LPS is regulated at the mRNA level of the ßA
gene. The mRNAs of four activin receptors (ActRI, ActRIB, ActRII, and
ActRIIB) were also detected in the peritoneal macrophages, and the mRNA
levels, except for ActRIB, were decreased during the LPS treatment.
Exogenous activin A stimulated the mRNA expression and gelatinolytic
activity of matrix metalloproteinase-2 (MMP-2) in macrophages in both
the presence and the absence of LPS. In contrast, activin did not
affect the production of MMP-9 in macrophages. These results suggested
that 1) mouse peritoneal macrophages produced activin A; 2) expression
of activin A was enhanced with activation of the macrophages; 3) the
macrophages also expressed activin receptors; and 4) exogenous activin
A stimulated MMP-2 expression and activity, implicating activin A as an
positive regulator of MMP-2 expression. Considering that MMP-2
constitutes the rate-limiting proteinase governing the degradation of
basement membrane collagens, activin A may be involved in migration and
infiltration of macrophages through the basement membrane in an
inflammatory state.
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