HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal My Folders Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Mann, K. I. Articles by Dias, J. A. Search for Related Content PubMed PubMed Citation Articles by Mann, K. I. Articles by Dias, J. A. Agricola Articles by Mann, K. I. Articles by Dias, J. A.

Deletion of Follicle-Stimulating Hormone (FSH) Receptor Residues Encoded by Exon One Decreases FSH Binding and Signaling in the Rat¹

^a Department of Biological Sciences, and ^b Department of Biomedical Sciences, State University of New York at Albany, Albany, New York 12208 ^c Wadsworth Center, David Axelrod Institute for Public Health, New York State Department of Health, Albany, New York 12208

The rat FSH receptor (rFSHR) shares considerable homology with the rat LH receptor (rLHR), yet binds human FSH (hFSH) with high fidelity, suggesting that the binding determinant encoded by the rFSHR gene shares no homology with the analogous rLHR primary sequence, thereby affording specificity of ligand binding. Two such regions of primary sequence have been previously identified and studied by peptide challenge tests and immunoneutralization studies. We therefore implemented site-directed mutagenesis to delete the regions S9-N30 and D300-F315 of the mature rFSHR sequence. The mutant receptor (rFSHR) cDNAs were expressed in insect cells. The large deletion rFSHRS9-N30 and a smaller deletion, rFSHRS9-S18, did not bind ¹²⁵I-hFSH. However, rFSHRK19-R29 and rFSHRD300-F315 bound ¹²⁵I-hFSH with an affinity indistinguishable from wild-type rFSHR. The deletion mutants rFSHR S9-N30 or rFSHRS9-S18 were not detectable on the cell surface by flow cytometry unless cells were sheared. Although ¹²⁵I-hFSH binding to rFSHRK19-R29 was normal, this form of the receptor was defective for signal transduction whereas rFSHRD300-F315 was not. Furthermore, neither region seems to be a specificity determinant, since their removal did not result in high-affinity binding of hCG to rFSHR.

First decision: 4 January 1999.

¹ Supported by NIH HD-18407. This study was conducted in partial fulfillment of the requirements for a master's degree at the University at Albany, Albany, NY (K.I.M.).

² Correspondence: James A. Dias, Wadsworth Center, David Axelrod Institute for Public Health, New York State Department of Health, 120 New Scotland Avenue, Albany, NY 12208. FAX: 518 474 5978; james.dias{at}wadsworth.org

This article has been cited by other articles:

				P. Thiruppathi, S. Shatavi, J.A. Dias, E. Radwanska, and J.L. Luborsky Gonadotrophin receptor expression on human granulosa cells of low and normal responders to FSH Mol. Hum. Reprod., August 1, 2001; 7(8): 697 - 704. [Abstract] [Full Text] [PDF]