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      N-linked oligosaccharides direct the differential assembly and secretion of inhibin alpha- and betaA-subunit dimers.

      Molecular Endocrinology

      Activins, chemistry, genetics, metabolism, Amino Acid Sequence, Animals, Base Sequence, Binding Sites, CHO Cells, Cricetinae, Cricetulus, DNA Primers, Dimerization, Evolution, Molecular, Glycosylation, Inhibin-beta Subunits, Inhibins, Models, Biological, Molecular Sequence Data, Mutagenesis, Site-Directed, Oligosaccharides, Protein Structure, Quaternary, Subcellular Fractions, Transforming Growth Factor beta, antagonists & inhibitors, Tunicamycin, pharmacology

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          The biosynthetic pathway governing inhibin heterodimer (alpha/beta) 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 wild-type (wt) cell lines (alpha(wt)beta(wt)). Mutation of a single glycosylation site at asparagine 268 (alpha(Delta268)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 vs. 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.

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