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Molecular Endocrinology Vol. 3, No. 9 1352-1358
doi:10.1210/mend-3-9-1352
Copyright © 1989 by the Endocrine Society.
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Activin B: Precursor Sequences, Genomic Structure and in Vitro Activities

Anthony J. Mason, Lucy M. Berkemeier, Charles H. Schmelzer and Ralph H. Schwall

Department of Developmental Biology, Recovery Process R & D, Sciences, Genentech Inc. South San Francisco, California 94080
Pharmacological Sciences, Genentech Inc. South San Francisco, California 94080

Address requests for reprints to: Dr. Anthony J. Mason, Department of Developmental Biology, Genentech, Inc., 450 Point San Bruno Boulevard, South San Francisco, California 94080.

Abstract

We report here the complete amino acid sequence of the human inhibin βB-subunit as deduced from the sequence of cDNA and genomic clones. The primary translation product of the βB mRNA predicts a protein of 407 amino acids, containing a prepro region of 292 amino acids separated by basic amino acids from the mature C-terminal 115 amino acids. Mammalian tissue culture cells transfected with a βB-subunit expression plasmid secreted an activin B homodimer of approximately 22K mol wt. Coexpression of the βA- and βB-subunit mRNAs resulted in the secretion of the three forms of activin, A, AB, and B. Purified activin B was shown to elicit FSH release in an in vitro pituitary assay and trigger the accumulation of hemoglobin in K562 cells. The potency of activin B in both of these assays (ED50 ~2 ng/ml) was indistinguishable from that observed for activin A.

Received for publication June 1, 1989. Accepted for publication June 4, 1989.




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