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Volume 12, Issue 3 (May 2010) 12, 422–430; 10.1038/aja.2010.8
POSVP21, a major secretory androgen-dependent protein from sand rat seminal vesicles, identifi ed as a transgelin
Naïma Kaci-Ouchfoun1, Anne Incamps2, Fatima Hadj-Bekkouche3, Mohamed Cherif Abbadi4, Laurent Bellanger2 and Thérèse Gernigon-Spychalowicz1
1 Laboratory of Arid Areas, Biological Sciences Institute, USTHB, BP 132 El Alia, 16100 Algiers, Algeria
2 Department of biochemistry and nuclear toxicology (SBTN), CEA Marcoule BP 17171. F-30207 Bagnols-sur-Cèze, France
3 Laboratory of Biology and Organisms Physiology, USTHB, BP 132 El Alia, 16100 Algiers, Algeria
4 Department of Immunology, Algerian Pasteur Institute, 16000 Algiers, Algeria
Correspondence: Dr Naïma Kaci-Ouchfoun, kacinaima@yahoo.fr
Received 2 October 2009; Revised 26 December 2009; Accepted 2 February 2010; Published online 19 April 2010.
| Abstract |
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The seminal vesicles of adult sand rat contain a major secretory protein band (MW 21 kDa) designated as Psammomys obesus seminal vesicles protein of 21 kDa (POSVP21). This protein is abundant in secretions, regulated by androgens and also present in the vaginal plug. POSVP21 accounts for over 22.3% of soluble proteins from homogenate during the breeding season, 13.3% during the middle season and 5.3% during the hormonal regression season. It is absent during the non-breeding season. POSVP21 is localized in the cytoplasm of epithelial cells and in secretory products in the lumen. It presents an immunological homology with two epididymal proteins with the same molecular weight and a high degree of homology with transgelin from rat (Rattus norvegicus).
Keywords: androgen-dependent; Psammomys obesus; seminal vesicles; transgelin
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