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BOR - Papers in Press, published online ahead of print October 15, 2003.
Biol Reprod 2003, 10.1095/biolreprod.103.022459
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BIOLOGY OF REPRODUCTION 70, 319–328 (2004)
DOI: 10.1095/biolreprod.103.022459
© 2004 by the Society for the Study of Reproduction, Inc.

Male Reproductive Tract

Identification of a Member of a New RNase A Family Specifically Secreted by Epididymal Caput Epithelium1

Sandrine Castella3, Sophie Fouchécourt3, Ana Paula Teixeira-Gomes4, Joëlle Vinh5, Maya Belghazi6, Françoise Dacheux3, and Jean-Louis Dacheux2,3

Equipe "Gamète Mâle et Fertilité" UMR INRA-CNRS 6073,3 PRC, INRA, 37 380 Nouzilly, France Atelier d'Electrophorèse et de Microséquençage de Protéines,4 INRA, 37 380 Nouzilly, France Laboratoire de Neurobiologie,5 ESPCI, 75 231 Paris, France Service de Spectrométrie de Masse pour la Protéomique,6 37 380 Nouzilly, France

In this study, we purified the first member of a new ribonuclease (RNase) A family from fluid of the proximal caput of the boar epididymis. This protein, named "Train A," is the most abundant compound secreted in the anterior part of the boar epididymis. After 2D electrophoresis, it is characterized by more than 10 isoforms ranging in size from 26 to 33 kDa and pI from 5 to 8.5. Several tryptic peptides were N-terminal sequenced, and an antiserum against one of these peptides was obtained. The protein was immunolocalized in the epididymal epithelium of the proximal caput, especially in the Golgi zone and the apical cytoplasm of the principal cells. In the lumen, spermatozoa were negative but droplets of reaction product were observed within the lumen. Full lengths of Train A cDNA were obtained from a {lambda}gt11 boar caput epididymis library and sequenced. The deduced protein is composed of 213 amino acids, including a 23-amino acid peptide signal and a potential N-glycosylation site. The mRNA of this protein has been retrieved and partially sequenced in the bull, horse, and ram, and homologous cDNA is found in databanks for the rat, mouse, and human. All the sequences are highly conserved between species. This protein and its mRNA are male-specific and exclusively expressed in the proximal caput of the epididymis, the only site where they have been found. Train A presents an RNase A family motif in its sequence. The RNase A family is a group of several short proteins (20–14 kDa) with greater and lesser degrees of ribonucleolytic activity and with supposed different roles in vivo. However, the presence of a long-conserved N-terminal specific sequence and the absence of RNase catalytic site for Train A indicate that Train A protein is a member of a new family of RNase A.

1 Supported by grants from the Institut National de la Recherche Agronomique (INRA, France) and from the Région Centre (France).

2 Correspondence: Jean-Louis Dacheux, UMR INRA-CNRS 6073, Nouzilly, France 37380. FAX: 33 2 47 42 77 43; jdacheux{at}tours.inra.fr




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