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Vol. 273, Issue 1, 398-403, January 2, 1998
From the Inhibins and activins are dimeric proteins that
are functional antagonists and are structurally related to the
transforming growth factor-
Identification of an Inhibin Receptor in Gonadal Tumors from
Inhibin
-Subunit Knockout Mice
,
,,, and
Departments of Medicine and Neurobiology and
Physiology, Northwestern University, Chicago, Illinois 60611, the
§ Departments of Pathology, Cell Biology, and Molecular and
Human Genetics, Baylor College of Medicine, Houston, Texas 77030, the
¶ Department of Reproductive Medicine, University of California,
San Diego, California 92093, and Genentech, Inc., South San
Francisco, California 94080
(TGF) family of growth and
differentiation factors. Receptors for activin and TGF have been
identified as dimers of serine-threonine kinase subunits that regulate
cytoplasmic proteins known as Smads. Despite major advances in our
understanding of activin and TGF receptors and signaling pathways,
little is known about inhibin receptors or the mechanism by which this
molecule provides a functionally antagonistic signal to activin.
Studies described in this paper indicate that an independent inhibin
receptor exists. Numerous tissues were examined for inhibin-specific
binding sites, including the developing embryo, in which the spinal
ganglion and trigeminal ganglion-bound iodinated inhibin A. Sex cord
stromal tumors, derived from male and female inhibin
-subunit-deficient mice, were also identified as a source of inhibin
receptor. Abundant inhibin and few activin binding sites were
identified in tumor tissue sections by in situ ligand
binding using iodinated recombinant human inhibin A and
125I-labeled recombinant human inhibin A. Tumor cell
binding was specific for each ligand (competed by excess unlabeled
homologous ligand and not competed by heterologous ligand). Based on
these results and the relative abundance and homogeneity of tumor
tissues versus the embryonic ganglion, tumor tissues were
homogenized, membrane proteins were purified, and putative inhibin
receptors were isolated using an inhibin affinity column. Four proteins were eluted from the column that bind iodinated inhibin but not iodinated activin. These data suggest that inhibin-specific
membrane-associated proteins (receptors) exist.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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