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Endocrinology Vol. 141, No. 7 2600-2607
Copyright © 2000 by The Endocrine Society

ARTICLES

Structure and Expression of a Membrane Component of the Inhibin Receptor System1

Huira Chong, Stephanie A. Pangas, Daniel J. Bernard, Eileen Wang, Jolee Gitch, Wei Chen, Lawrence B. Draper, Edward T. Cox and Teresa K. Woodruff

Department of Neurobiology and Physiology (H.C., S.A.P., D.J.B., E.W., J.G., L.B.D., T.K.W.), Department of Biochemistry, Molecular Biology, and Cell Biology (W.C.), Northwestern University, Evanston, Illinois 60208-2850; and Genentech, Inc. (E.T.C.), South San Francisco, California 94080-4990

Address all correspondence and requests for reprints to: Teresa K. Woodruff, Ph.D., Northwestern University, Department of Neurobiology and Physiology, O.T. Hogan 4–150, 2153 North Campus Drive, Evanston, Illinois 60208. E-mail: tkw{at}nwu.edu

The purification and cloning of a membrane-anchored proteoglycan with affinity for inhibin A are described. Bovine pituitary membranes were isolated, and membrane-anchored proteins were solubilized and used as an enriched source of inhibin binding protein. The extract was passed over an inhibin A affinity column, and a protein, designated p120, was identified as an inhibin-binding moiety. A partial amino acid sequence was determined for the protein, which matched two human complementary DNAs (cDNAs) in the database. The full-length cDNA predicts a 1336-amino acid glycoprotein. Full-length p120-encoding cDNAs were isolated from human testis RNA and cloned into expression vectors. Two p120 messenger RNA transcripts of 4.6 kb and 2 kb are detected in rat pituitary by RNA blot analysis. Similar analysis of rat testis RNA revealed transcripts of identical molecular mass, albeit at lower abundance. To determine the cellular localization of p120 in pituitary and testis, an antibody directed against the predicted extracellular domain of the protein was generated and used in an immunohistochemical analysis of thin tissue sections. p120 immunostaining is coincident with FSHß immunopositive gonadotrope cells in rat pituitary. p120 staining is intense in the testicular Leydig cells, which bind iodinated inhibin but not iodinated activin. In summary, an inhibin-binding protein has been isolated that is produced in tissues that are targets of inhibin action.




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