Cloning of a novel inhibin alpha cDNA from rhesus monkey testis
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Cloning of a novel inhibin alpha cDNA from rhesus monkey testis Daniel J Bernard*1,2, Teresa K Woodruff1 and Tony M Plant3 Address: 1Department of Neurobiology and Physiology, Northwestern University, 2205 Tech Drive, Evanston, IL 60208, USA, 2Center for Biomedical Research, Population Council and The Rockefeller University, 1230 York Ave., New York, NY 10021, USA and 3University of Pittsburgh School of Medicine, Departments of Cell Biology and Physiology, and Obstetrics, Gynecology and Reproductive Sciences, 3550 Terrace Street, Pittsburgh, PA 15261, USA Email: Daniel J Bernard* - [email protected]; Teresa K Woodruff - [email protected]; Tony M Plant - [email protected] * Corresponding author
Published: 07 October 2004 Reproductive Biology and Endocrinology 2004, 2:71
doi:10.1186/1477-7827-2-71
Received: 16 September 2004 Accepted: 07 October 2004
This article is available from: http://www.rbej.com/content/2/1/71 © 2004 Bernard et al; licensee BioMed Central Ltd. This is an open-access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract Background: Inhibins are dimeric gonadal protein hormones that negatively regulate pituitary FSH synthesis and secretion. Inhibin B is produced by testicular Sertoli cells and is the primary circulating form of inhibin in most adult male mammals. Inhibin B is comprised of the inhibin alpha subunit disulfide-linked to the inhibin/activin betaB subunit. Here we describe the cloning of the cDNAs encoding these subunits from adult rhesus monkey testis RNA. Methods: The subunit cDNAs were cloned by a combination of reverse transcriptase polymerase chain reaction (RT-PCR) and 5' rapid amplification of cDNA ends (RACE) RT-PCR from adult rhesus monkey testis RNA. Results: Both the inhibin alpha and betaB subunit nucleotide and predicted protein sequences are highly conserved with other mammalian species, particularly with humans. During the course of these investigations, a novel inhibin alpha mRNA isoform was also identified. This form, referred to as rhesus monkey inhibin alpha-variant 2, appears to derive from both alternative transcription initiation as well as alternative splicing. rmInhibin alpha-variant 2 is comprised of a novel 5' exon (exon 0), which is spliced in-frame with exon 2 of the conventional inhibin alpha isoforms (variant 1). Exon 1 is skipped in its entirety such that the pro-alpha and part of the alpha N regions are not included in the predicted protein. rmInhibin alpha -variant 2 is of relatively low abundance and its biological function has not yet been ascertained. Conclusion: The data show that the predicted inhibin B protein is very similar between monkeys and humans. Therefore, studies in monkeys using recombinant human inhibins are likely to reflect actions of the homologous ligands. In addition, we
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