Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (14)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Hammami-Hamza, S.
Right arrow Articles by Finaz, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hammami-Hamza, S.
Right arrow Articles by Finaz, C.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Molecular Human Reproduction, Vol. 7, No. 7, 625-632, July 2001
© 2001 European Society of Human Reproduction and Embryology


Testis and spermatogenesis

Cloning and sequencing of SOB3, a human gene coding for a sperm protein homologous to an antimicrobial protein and potentially involved in zona pellucida binding

Sonia Hammami-Hamza1, Mireille Doussau1, Jérôme Bernard2, Edith Rogier2, Clotilde Duquenne1, Yolande Richard2, Annick Lefèvre3 and Catherine Finaz1,4

1 INSERM U 355, Maturation Gamétique et Fécondation, Institut Paris-sud sur les Cytokines, 32 rue des Carnets, 92140 Clamart, France, 2 INSERM U 131, Cytokines et immunorégulation, Institut Paris-sud sur les Cytokines, 32 rue des Carnets, 92104 Clamart, France, 3 INSERM U 418, Communications Cellulaires et Différenciation, Hôpital Debrousse, 29 rue Soeur Bouvier, 69322 Lyon, France

Abstract

We have previously characterized an 18–19 kDa cationic protein, SOB3, that was detected in the epididymis and localized within the acrosome and on the neck region of human spermatozoa. We suggested that it is involved in secondary sperm binding to the zona pellucida. The present study describes its purification to homogeneity by preparative electrophoresis and non-equilibrium pH gradient electrophoresis. Degenerate primers deduced from microsequencing were used to amplify a specific fragment from human epididymal RNA by reverse transcription-polymerase chain reaction (RT-PCR). This 164 bp fragment was extended by 5' and 3'-RACE to obtain the 548 bp full length cDNA. The open reading frame encodes a 170 amino acid protein. SOB3 is a single copy gene. It is 98% identical to prepro-FALL39 and 100% identical to CAP18, two human genes which were initially identified by screening a human bone marrow {lambda}gt11 library, and which encode an antimicrobial protein. Northern blots of human tissues revealed a 1 kb transcript in corpus and cauda epididymis only, while RT-PCR showed presence of the mRNA in the three epididymal regions and also in round spermatids. The above results suggest that SOB3 has two roles in sperm protection and fertilization, depending on its dual origin and final sperm localization.

antimicrobial peptide/CAP18/fertilization/prepro-FALL-39/sperm protein

Notes

4 To whom correspondence should be addressed at: INSERM U 355, 32 rue des Carnets, 92140 Clamart. E-mail: catherine.finaz{at}inserm.ipsc.u-psud.fr


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Biol. Reprod.Home page
M.A. Palladino, T.A. Johnson, R. Gupta, J.L. Chapman, and P. Ojha
Members of the Toll-Like Receptor Family of Innate Immunity Pattern-Recognition Receptors Are Abundant in the Male Rat Reproductive Tract
Biol Reprod, June 1, 2007; 76(6): 958 - 964.
[Abstract] [Full Text] [PDF]


Home page
FASEB J.Home page
A. F. Gombart, N. Borregaard, and H. P. Koeffler
Human cathelicidin antimicrobial peptide (CAMP) gene is a direct target of the vitamin D receptor and is strongly up-regulated in myeloid cells by 1,25-dihydroxyvitamin D3
FASEB J, July 1, 2005; 19(9): 1067 - 1077.
[Abstract] [Full Text] [PDF]


Home page
J. Leukoc. Biol.Home page
M. Zanetti
Cathelicidins, multifunctional peptides of the innate immunity
J. Leukoc. Biol., January 1, 2004; 75(1): 39 - 48.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
O. E. Sorensen, L. Gram, A. H. Johnsen, E. Andersson, S. Bangsboll, G. S. Tjabringa, P. S. Hiemstra, J. Malm, A. Egesten, and N. Borregaard
Processing of Seminal Plasma hCAP-18 to ALL-38 by Gastricsin: A NOVEL MECHANISM OF GENERATING ANTIMICROBIAL PEPTIDES IN VAGINA
J. Biol. Chem., August 1, 2003; 278(31): 28540 - 28546.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Respir. Cell Mol. Bio.Home page
C. Y. Kao, Y. Chen, Y. H. Zhao, and R. Wu
ORFeome-Based Search of Airway Epithelial Cell-Specific Novel Human {beta}-Defensin Genes
Am. J. Respir. Cell Mol. Biol., July 1, 2003; 29(1): 71 - 80.
[Abstract] [Full Text] [PDF]


Home page
Biol. Reprod.Home page
M.A. Palladino, T.A. Mallonga, and M.S. Mishra
Messenger RNA (mRNA) Expression for the Antimicrobial Peptides {beta}-Defensin-1 and {beta}-Defensin-2 in the Male Rat Reproductive Tract: {beta}-Defensin-1 mRNA in Initial Segment and Caput Epididymidis Is Regulated by Androgens and Not Bacterial Lipopolysaccharides
Biol Reprod, February 1, 2003; 68(2): 509 - 515.
[Abstract] [Full Text] [PDF]


Home page
Hum ReprodHome page
E. Andersson, O.E. Sorensen, B. Frohm, N. Borregaard, A. Egesten, and J. Malm
Isolation of human cationic antimicrobial protein-18 from seminal plasma and its association with prostasomes
Hum. Reprod., October 1, 2002; 17(10): 2529 - 2534.
[Abstract] [Full Text] [PDF]



Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.