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) All Versions of this Article: 69/4/1183    most recent biolreprod.102.010231v1 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 Weerachatyanukul, W. Articles by Tanphaichitr, N. Search for Related Content PubMed PubMed Citation Articles by Weerachatyanukul, W. Articles by Tanphaichitr, N. Agricola Articles by Weerachatyanukul, W. Articles by Tanphaichitr, N.

Acquisition of Arylsulfatase A onto the Mouse Sperm Surface During Epididymal Transit¹

Hormones/Growth/Development Research Group,³ Ottawa Health Research Institute, Ottawa, Ontario K1Y 4E9, Canada Departments of Obstetrics and Gynecology,⁴ and Biochemistry/Microbiology/Immunology,⁵ University of Ottawa, Ottawa, Ontario K1Y 4E9, Canada Environmental and Occupational Toxicology Division,⁶ Health Canada, Ottawa, Ontario K1A 0L2, Canada Department of Anatomy and Cell Biology,⁷ McGill University, Montreal, Quebec H3A 2B2, Canada Department of Anatomy, Faculty of Science,⁸ Mahidol University, Bangkok, Thailand Laboratory Medicine,⁹ Anatomical Pathology, Ottawa Hospital, Civic Campus, Ottawa, Ontario K1Y 4E9, Canada

Arylsulfatase A (AS-A) is localized to the sperm surface and participates in sperm-zona pellucida binding. We investigated how AS-A, usually known as an acrosomal enzyme, trafficked to the sperm surface. Immunocytochemistry of the mouse testis confirmed the existence of AS-A in the acrosomal region of round and elongating spermatids. However, immunofluorescence and flow cytometry indicated the absence of AS-A on the surface of live testicular sperm. In contrast, positive AS-A staining was observed in the heads of live caudal epididymal and vas deferens sperm. The results suggested that acquisition of AS-A on the sperm surface occurred during epididymal transit. Immunocytochemistry of the epididymis revealed AS-A in narrow and apical cells in the initial segment and in clear cells in all epididymal regions. However, these epithelial cells are in the minority and are not involved in secretory activity. In the caudal epididymis and vas deferens, AS-A was also localized to principal cells, the major epithelial cells. Because principal cells have secretory activity, they may secrete AS-A into the epididymal fluid. This hypothesis was supported by our results revealing the presence of AS-A in the epididymal and vas deferens fluid (determined by immunoblotting and ELISA) and an AS-A transcript in the epididymis (by reverse transcription polymerase chain reaction). Alexa-430 AS-A bound to epididymal sperm with high affinity (K_d = 46 nM). This binding was inhibited by treatment of sperm with an antibody against sperm surface sulfogalactosylglycerolipid. This finding suggests that AS-A in the epididymal fluid may deposit onto sperm via its affinity to sulfogalactosylglycerolipid.

¹ This work was funded by CIHR (grant no. 10366 to N.T.). W.W. and A.A. are awardees of a scholarship from the National Science and Technology Development Agency of Thailand and the Thailand Research Fund, respectively. W.W., H.X., and A.A. contributed equally to this work.

² Correspondence: Nongnuj Tanphaichitr, Ottawa Health Research Institute, 725 Parkdale Ave., Ottawa, ON K1Y 4E9, Canada. FAX: 613 761-5365; ntanphaichitr{at}ohri.ca

This article has been cited by other articles:

				J. Lefebvre, J. Fan, S. Chevalier, R. Sullivan, E. Carmona, and P. Manjunath Genomic structure and tissue-specific expression of human and mouse genes encoding homologues of the major bovine seminal plasma proteins Mol. Hum. Reprod., January 1, 2007; 13(1): 45 - 53. [Abstract] [Full Text] [PDF]

				Y. S. Cho, N. Iguchi, J. Yang, M. A. Handel, and N. B. Hecht Meiotic Messenger RNA and Noncoding RNA Targets of the RNA-Binding Protein Translin (TSN) in Mouse Testis Biol Reprod, October 1, 2005; 73(4): 840 - 847. [Abstract] [Full Text] [PDF]

				Y. Zhang, Y. Hayashi, X. Cheng, T. Watanabe, X. Wang, N. Taniguchi, and K. Honke Testis-specific sulfoglycolipid, seminolipid, is essential for germ cell function in spermatogenesis Glycobiology, June 1, 2005; 15(6): 649 - 654. [Abstract] [Full Text] [PDF]