Reproduction   citetrack
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS  

Journal of Reproduction and Fertility (1994) 101 703-711
DOI: 10.1530/jrf.0.1010703
Copyright © 1994 Society for Reproduction and Fertility
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lassalle, B.
Right arrow Articles by Testart, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lassalle, B.
Right arrow Articles by Testart, J.

Human zona pellucida recognition associated with removal of sialic acid from human sperm surface

B. Lassalle and J. Testart

The ability of human spermatozoa recovered from highly motile sperm fractions to bind wheat germ agglutinin (WGA) after discontinuous Percoll gradient centrifugation was studied. WGA could bind to almost all motile spermatozoa, whereas fewer than 25% of spermatozoa could bind peanut (PNA) and concanavalin A (Con A) agglutinin, two lectins that specifically bind acrosomal membranes. After removal of the plasma membrane with 0.04% Triton X100, WGA, PNA and Con A bound more than 80% of spermatozoa, but binding sites for WGA on the anterior acrosomal region were markedly reduced. The expression of sialic acid on human sperm plasma membrane was demonstrated, since WGA, which specifically recognizes both sialic acid (NeuNAc) and N-acetylglucosamine (GlcNAc), bound almost all intact motile spermatozoa, whereas succinylated WGA, which recognizes only GlcNAc, bound less than 10% of intact motile spermatozoa. Moreover, binding of WGA was compared with that of three other lectins (Sambucus nigra, SNA; Maackia amurensis, MAL and Limulus polyphemus, LPA) with specificity for different NeuNAc linkages. Only SNA, which requires the presence of the disaccharide structure NeuNAc {alpha}(2,6) Gal/GalNAc, showed a positive correlation with sperm motility as observed with WGA. Moreover, there was a strong inhibition of WGA binding on spermatozoa preincubated with bovine submaxillary mucin containing (2,6)-linked NeuNAc. These results demonstrate the presence of NeuNAc {alpha}(2,6) Gal/GalNAc glycoconjugate sequences on the plasma membrane of the motile human spermatozoon. Treatment of spermatozoa with Arthrobacter ureafaciens neuraminidase to cleave NeuNAc residues led to a dose-dependent decrease of WGA binding at the sperm surface and to the enhancement of sperm attachment to the zona pellucida. We hypothesize that the release of sialic acid from the sperm plasma membrane could be one of the capacitation events necessary for unmasking certain sperm surface antigens implicated in zona pellucida recognition.




This article has been cited by other articles:


Home page
Hum ReprodHome page
T. L. Tollner, A. I. Yudin, C. A. Treece, J. W. Overstreet, and G. N. Cherr
Macaque sperm coating protein DEFB126 facilitates sperm penetration of cervical mucus
Hum. Reprod., November 1, 2008; 23(11): 2523 - 2534.
[Abstract] [Full Text] [PDF]


Home page
Mol Hum ReprodHome page
H.-W. Liu, Y.-C. Lin, C.-F. Chao, S.-Y. Chang, and G.-H. Sun
GP-83 and GP-39, two glycoproteins secreted by human epididymis are conjugated to spermatozoa during maturation
Mol. Hum. Reprod., May 1, 2000; 6(5): 422 - 428.
[Abstract] [Full Text] [PDF]


Home page
J. Pharmacol. Exp. Ther.Home page
V. Srikanth, T. Malini, J. Arunakaran, P. Govindarajulu, and K. Balasubramanian
Effects of Ethanol Treatment on Epididymal Secretory Products and Sperm Maturation in Albino Rats
J. Pharmacol. Exp. Ther., February 1, 1999; 288(2): 509 - 515.
[Abstract] [Full Text]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS  
Copyright © 1994 by the Society for Reproduction and Fertility.