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This version published online on April 24, 2007
Molecular Endocrinology, doi:10.1210/me.2007-0050
A more recent version of this article appeared on July 1, 2007
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Submitted on January 25, 2007
Accepted on April 20, 2007

N-linked oligosaccharides direct the differential assembly and secretion of inhibin {alpha}- and {beta}A-subunit dimers

Monica Antenos, Michelle Stemler, Irving Boime, and Teresa K. Woodruff*

Department of Neurobiology and Physiology, Northwestern University, Evanston, IL 60208; Department of Molecular Biology & Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110; Department of Medicine, Northwestern University Medical School, Chicago, IL 60611; Robert H. Lurie Comprehensive Cancer Center of Northwestern University, Chicago, IL 60611

* To whom correspondence should be addressed. E-mail: tkw{at}northwestern.edu.

The biosynthetic pathway governing inhibin heterodimer and activin homodimer ({beta}/{beta}) assembly and secretion from ovarian granulosa cells is not fully understood. Here, we examined the role of inhibin subunit glycosylation in the assembly and secretion of mature inhibin A and activin A. Inhibition of subunit glycosylation by tunicamycin treatment of {alpha}- and {beta}A-expressing CHO cell lines reduced inhibin but not activin secretion. Dimeric inhibin A is preferentially secreted from parental isogenic cell lines ({alpha}wt{beta}wt). Mutation of a single glycosylation site at asparagine 268 ({alpha}{Delta}268{beta}wt) reduces inhibin secretion by 78% and permits {beta}/{beta} assembly and secretion. Conversely, gain of a glycosylation (GOG) site in the analogous region of the {beta}A-subunit ({alpha}wt{beta}GOG327) enhances inhibin A secretion. The present study demonstrates that N-linked glycan sites direct heterodimer versus homodimer assembly, and prevention of glycosylation abrogates inhibin secretion. These data support a definitive role for site-specific N-glycosylation in governing inhibin/activin dimer assembly and secretion.
Key words: inhibin • activin • ovary • granulosa cell • glycosylation • dimers • secretion • FSH • CHO




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[Abstract] [Full Text] [PDF]


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