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Molecular and Cellular Biology, July 2003, p. 4882-4891, Vol. 23, No. 14
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.14.4882-4891.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Normal Reproductive Function in InhBP/p120-Deficient Mice

Daniel J. Bernard,1,2* Kathleen H. Burns,3,4 Bisong Haupt,3 Martin M. Matzuk,3,4,5 and Teresa K. Woodruff1,6

Department of Neurobiology and Physiology, Northwestern University, Evanston, Illinois 60201,1 Center for Biomedical Research, Population Council and Rockefeller University, New York, New York 10021,2 Departments of Pathology,3 Molecular and Human Genetics,4 Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030,5 Department of Medicine, Northwestern University School of Medicine, Chicago, Illinois 606576

Received 24 February 2003/ Returned for modification 10 April 2003/ Accepted 30 April 2003

The inhibins are gonadal transforming growth factor ß superfamily protein hormones that suppress pituitary follicle-stimulating hormone (FSH) synthesis. Recently, betaglycan and inhibin binding protein (InhBP/p120, also known as the product of immunoglobulin superfamily gene 1 [IGSF1]) were identified as candidate inhibin coreceptors, shedding light on the molecular basis of how inhibins may affect target cells. Activins, which are structurally related to the inhibins, act within the pituitary to stimulate FSH production. Betaglycan increases the affinity of inhibins for the activin type IIA (ACVR2) receptor, thereby blocking activin binding and signaling through this receptor. InhBP/p120 may not directly bind inhibins but may interact with the activin type IB receptor, ALK4, and participate in inhibin B's antagonism of activin signaling. To better understand the in vivo functions of InhBP/p120, we characterized the InhBP/p120 mRNAs and gene in mice and generated InhBP/p120 mutant mice by gene targeting in embryonic stem cells. InhBP/p120 mutant male and female mice were viable and fertile. Moreover, they showed no alterations in FSH synthesis or secretion or in ovarian or testicular function. These data contribute to a growing body of evidence indicating that InhBP/p120 does not play an essential role in inhibin biology.

* Corresponding author. Mailing address: Population Council, Center for Biomedical Research, 1230 York Ave., New York, NY 10021. Phone: (212) 327-8761. Fax: (212) 327-7678. E-mail: dbernard{at}popcbr.rockefeller.edu.

Molecular and Cellular Biology, July 2003, p. 4882-4891, Vol. 23, No. 14
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.14.4882-4891.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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