| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
Regular Article |
a The Sperm Physiology Laboratory,
b Department of Obstetrics and Gynecology, W.M. Keck Foundation Biotechnology Resource Laboratory, Yale University School of Medicine, New Haven, Connecticut 06510
c Reproductive Toxicology Division, National Health and Environmental Effects Research Laboratory, U.S. Environmental Protection Agency, Research Triangle Park, North Carolina 27711
ABSTRACT
We previously described a putative creatine kinase M isoform in human sperm that is developmentally regulated and expressed during late spermiogenesis, simultaneous with cytoplasmic extrusion. We have now identified this protein as the testis-expressed 70-kDa heat shock protein chaperone known as HspA2 (the human homologue of mouse Hsp70-2). We have isolated and characterized HspA2 (formerly CK-M) by amino acid sequencing and have localized it by immunocytochemistry to spermatocytes at low levels, to spermatids, and in the tail of mature sperm. The specificity of the CK-M/HspA2 antiserum to HspA2 was demonstrated on immunoblots of one- and two-dimensional SDS-PAGE. In agreement with our earlier biochemical data, immunocytochemistry of testicular tissue indicated that HspA2 is selectively expressed in mature spermatids and in sperm about to be released in the seminiferous tubuli. The identity of HspA2 has been further confirmed by cross-absorption of the mouse HSP70-2 antibody by the HspA2/CK-M fraction, and by identical immunostaining patterns of human testicular tissue using either the anti-CK-M/HspA2 or an anti-mouse Hsp70-2 antisera. During spermiogenesis, both cytoplasmic extrusion and plasma membrane remodeling, which facilitate the formation of the zona pellucida binding site, involve major intrasperm protein transport, which may be chaperoned by HspA2. Accordingly, in immature human sperm, which fail to express HspA2, there is cytoplasmic retention and lack of zona pellucida binding. The present findings provide the biological rationale for the role of the human HspA2 as an objective biochemical marker of sperm function and male fertility, which we have established in earlier clinical studies.
1 Supported by NIH grant HD-32902, and by the CONRAD program. Part of this research was presented at the 1999 annual meeting of the European Society of Human Reproduction, Tours, France.
2 Correspondence: FAX: 203 737 1200; gabor.huszar{at}yale.edu
This article has been cited by other articles:
|
|
 |
|
  A.P. Cedenho, S.B. Lima, M.A. Cenedeze, D.M. Spaine, V. Ortiz, and S. Oehninger Oligozoospermia and heat-shock protein expression in ejaculated spermatozoa Hum. Reprod., July 1, 2006; 21(7): 1791 - 1794. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 W.C.L. Ford Glycolysis and sperm motility: does a spoonful of sugar help the flagellum go round? Hum. Reprod. Update, May 1, 2006; 12(3): 269 - 274. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. Celik-Ozenci, A. Jakab, T. Kovacs, J. Catalanotti, R. Demir, P. Bray-Ward, D. Ward, and G. Huszar Sperm selection for ICSI: shape properties do notpredict the absence or presence of numericalchromosomal aberrations Hum. Reprod., September 1, 2004; 19(9): 2052 - 2059. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 G. Huszar, C. Celik-Ozenci, S. Cayli, T. Kovacs, L. Vigue, and E. Kovanci Semen Characteristics After Overnight Shipping: Preservation of Sperm Concentrations, HspA2 Ratios, CK Activity, Cytoplasmic Retention, Chromatin Maturity, DNA Integrity, and Sperm Shape J Androl, July 1, 2004; 25(4): 593 - 604. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. E. Kuster, R. A. Hess, and G. C. Althouse Immunofluorescence Reveals Ubiquitination of Retained Distal Cytoplasmic Droplets on Ejaculated Porcine Spermatozoa J Androl, May 1, 2004; 25(3): 340 - 347. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Cayli, D. Sakkas, L. Vigue, R. Demir, and G. Huszar Cellular maturity and apoptosis in human sperm: creatine kinase, caspase-3 and Bcl-XL levels in mature and diminished maturity sperm Mol. Hum. Reprod., May 1, 2004; 10(5): 365 - 372. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. Celik-Ozenci, J. Catalanotti, A. Jakab, C. Aksu, D. Ward, P. Bray-Ward, R. Demir, and G. Huszar Human Sperm Maintain Their Shape Following Decondensation and Denaturation for Fluorescent In Situ Hybridization: Shape Analysis and Objective Morphometry Biol Reprod, October 1, 2003; 69(4): 1347 - 1355. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Jakab, T. Kovacs, Z. Zavaczki, A. Borsos, P. Bray-Ward, D. Ward, and G. Huszar Efficacy of the swim-up method in eliminating sperm with diminished maturity and aneuploidy Hum. Reprod., July 1, 2003; 18(7): 1481 - 1488. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. Sakkas, O. Moffatt, G. C. Manicardi, E. Mariethoz, N. Tarozzi, and D. Bizzaro Nature of DNA Damage in Ejaculated Human Spermatozoa and the Possible Involvement of Apoptosis Biol Reprod, April 1, 2002; 66(4): 1061 - 1067. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. Kovanci, T. Kovacs, E. Moretti, L. Vigue, P. Bray-Ward, D. C. Ward, and G. Huszar FISH assessment of aneuploidy frequencies in mature and immature human spermatozoa classified by the absence or presence of cytoplasmic retention Hum. Reprod., June 1, 2001; 16(6): 1209 - 1217. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
