Biol Reprod
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

BOR - Papers in Press, published online ahead of print September 29, 2004.
Biol Reprod 2004, 10.1095/biolreprod.104.034470
This Article
Right arrow Full Text (Rapid PDF)
Right arrow All Versions of this Article:
72/2/328    most recent
biolreprod.104.034470v1
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 PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Asquith, K. L.
Right arrow Articles by Aitken, R. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Asquith, K. L.
Right arrow Articles by Aitken, R. J.
Agricola
Right arrow Articles by Asquith, K. L.
Right arrow Articles by Aitken, R. J.
Submitted July 19, 2004
Returned for revision August 7, 2004
Accepted September 16, 2004

Male Reproductive Tract


Localisation and Significance of Molecular Chaperones, Heat Shock Protein 1 (Hspd1) and Tumor Rejection Antigen gp96 (Tra1), in the Male Reproductive Tract and During Capacitation and Acrosome Reaction

Kelly L. Asquith , Amanda J. Harman , Eileen A. McLaughlin , Brett Nixon , and R. John Aitken *

* To whom correspondence should be addressed. E-mail: jaitken{at}mail.newcastle.edu.au.

Abstract
Although the molecular basis of sperm-oocyte interaction is unclear, recent studies have implicated two chaperone proteins, heat shock protein 1 (Hspd1; previously known as heat shock protein 60) and tumor rejection antigen gp96 (Tra1; previously known as endoplasmin), in the formation of a functional zona-receptor complex on the surface of mammalian spermatozoa. The current study was undertaken to investigate the expression of these chaperones during the ontogeny of male germ cells through spermatogenesis, epididymal sperm maturation, capacitation and acrosomal exocytosis. In testicular sections, both Hspd1 and Tra1 were closely associated with the mitochondria of spermatogonia and primary spermatocytes. However this labeling pattern disappeared from the male germ line during spermiogenesis to become undetectable in testicular spermatozoa. Subsequently, these chaperones could be detected in epididymal spermatozoa and in previously unreported 'dense bodies' in the epididymal lumen. The latter appeared in the precise region of the epididymis (proximal corpus) where spermatozoa acquire the capacity to recognise and bind to the zona pellucida, implicating these structures in the functional remodelling of the sperm surface during epididymal maturation. Both Hspd1 and Tra1 were subsequently found to become co-expressed on the surface of live mouse spermatozoa following capacitation in vitro and were lost once these cells had undergone the acrosome reaction, as would be expected of cell surface molecules involved in sperm-egg interaction. These data reinforce the notion that these chaperones are intimately involved in the mechanisms by which mammalian spermatozoa both acquire and express their ability to recognise the zona pellucida.

Key words: Gamete Biology • Testis • Acrosome reaction • Epididymis • Signal transduction


This article has been cited by other articles:


Home page
 Biol. Reprod.Home page
A. Walsh, D. Whelan, A. Bielanowicz, B. Skinner, R. J. Aitken, M. K. O'Bryan, and B. Nixon
Identification of the Molecular Chaperone, Heat Shock Protein 1 (Chaperonin 10), in the Reproductive Tract and in Capacitating Spermatozoa in the Male Mouse
Biol Reprod, June 1, 2008; 78(6): 983 - 993.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Zhang, Z.-H. Li, M. Q. Zhang, M. S. Katz, and B.-X. Zhang
Heat Shock Protein 90{beta}1 Is Essential for Polyunsaturated Fatty Acid-induced Mitochondrial Ca2+ Efflux
J. Biol. Chem., March 21, 2008; 283(12): 7580 - 7589.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. H. von Horsten, S. S. Johnson, S. K. SanFrancisco, M. C. Hastert, S. M. Whelly, and G. A. Cornwall
Oligomerization and Transglutaminase Cross-linking of the Cystatin CRES in the Mouse Epididymal Lumen: POTENTIAL MECHANISM OF EXTRACELLULAR QUALITY CONTROL
J. Biol. Chem., November 9, 2007; 282(45): 32912 - 32923.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
T. Dottorini, L. Nicolaides, H. Ranson, D. W. Rogers, A. Crisanti, and F. Catteruccia
A genome-wide analysis in Anopheles gambiae mosquitoes reveals 46 male accessory gland genes, possible modulators of female behavior
PNAS, October 9, 2007; 104(41): 16215 - 16220.
[Abstract] [Full Text] [PDF]

Home page
 Mol Hum ReprodHome page
L.A. Mitchell, B. Nixon, and R.J. Aitken
Analysis of chaperone proteins associated with human spermatozoa during capacitation
Mol. Hum. Reprod., September 1, 2007; 13(9): 605 - 613.
[Abstract] [Full Text] [PDF]

Home page
 Mol Hum ReprodHome page
J. Zhang, J. Wu, R. Huo, Y. Mao, Y. Lu, X. Guo, J. Liu, Z. Zhou, X. Huang, and J. Sha
ERp57 is a potential biomarker for human fertilization capability
Mol. Hum. Reprod., September 1, 2007; 13(9): 633 - 639.
[Abstract] [Full Text] [PDF]

Home page
 Biol. Reprod.Home page
G. Frenette, J. Girouard, and R. Sullivan
Comparison Between Epididymosomes Collected in the Intraluminal Compartment of the Bovine Caput and Cauda Epididymidis
Biol Reprod, December 1, 2006; 75(6): 885 - 890.
[Abstract] [Full Text] [PDF]

Home page
 Biol. Reprod.Home page
H. Rejraji, B. Sion, G. Prensier, M. Carreras, C. Motta, J.-M. Frenoux, E. Vericel, G. Grizard, P. Vernet, and J. R. Drevet
Lipid Remodeling of Murine Epididymosomes and Spermatozoa During Epididymal Maturation
Biol Reprod, June 1, 2006; 74(6): 1104 - 1113.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Copyright © 2004 by the Society for the Study of Reproduction.