Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2002-5-21
pubmed:abstractText
We have shown previously that male germ cell-specific sulfoglycolipid, sulfogalactosylglycerolipid (SGG), is involved in sperm-zona pellucida binding, and that SGG and its desulfating enzyme, arylsulfatase A (AS-A), coexist in the same sperm head area. However, AS-A exists at a markedly low level in sperm as compared to SGG (i.e., 1/400 of SGG molar concentration). In the present study, we investigated whether perturbation of this molar ratio would interfere with sperm-egg interaction. We demonstrated that purified AS-A bound to the mouse sperm surface through its high affinity with SGG. When capacitated, Percoll gradient-centrifuged mouse sperm were treated for 1 h with various concentrations of AS-A, their binding to zona-intact eggs was inhibited in a dose-dependent manner and reached the background level with 63 nM AS-A. This inhibition could be partially explained by an increase in premature acrosome reaction. The acrosome-reacted sperm population of the 63 nM AS-A-treated sperm sample was twice that of the control sample (treated with 63 nM ovalbumin) at 1 h (i.e., 32% vs. 15%) and rose to 53% at 2 h. This induction was presumably due to SGG aggregation attributed to AS-A, existing as a dimer at neutral pH, and could be mimicked by anti-SGG immunoglobulin (Ig) G/IgM + secondary IgG antibody. Drastic inhibition (75%) of in vivo fertilization was also observed in females inseminated with sperm suspension containing 630 nM AS-A as compared to the rate in females inseminated with sperm suspension included with 630 nM ovalbumin. Our results demonstrate a promising potential for AS-A as a nonhormonal, vaginal contraceptive.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-3363
pubmed:author
pubmed:issnType
Print
pubmed:volume
66
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1820-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12021068-Acrosome Reaction, pubmed-meshheading:12021068-Animals, pubmed-meshheading:12021068-Cerebroside-Sulfatase, pubmed-meshheading:12021068-Contraceptive Agents, Female, pubmed-meshheading:12021068-Dimerization, pubmed-meshheading:12021068-Galactolipids, pubmed-meshheading:12021068-Humans, pubmed-meshheading:12021068-Hydrogen-Ion Concentration, pubmed-meshheading:12021068-Immunoglobulin G, pubmed-meshheading:12021068-Immunoglobulin M, pubmed-meshheading:12021068-Insemination, Artificial, pubmed-meshheading:12021068-Liver, pubmed-meshheading:12021068-Male, pubmed-meshheading:12021068-Mice, pubmed-meshheading:12021068-Sperm Capacitation, pubmed-meshheading:12021068-Sperm-Ovum Interactions, pubmed-meshheading:12021068-Spermatozoa, pubmed-meshheading:12021068-Zona Pellucida
pubmed:year
2002
pubmed:articleTitle
Binding of arylsulfatase A to mouse sperm inhibits gamete interaction and induces the acrosome reaction.
pubmed:affiliation
Hormones/Growth/Development Group, Ottawa Health Research Institute, Ottawa, Ontario, Canada K1Y 4E9.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't