Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-2-28
pubmed:abstractText
Studies suggest that carbohydrates are important in different stages of fertilization. Plasma membrane changes accompanying in vitro capacitation and acrosome reaction (AR), such as removal or appearance of specific glycoproteins, have been studied using lectins that bind specifically to carbohydrate residues. In specialized artificial insemination farms and semen production centers, identification of boars with decreased fertilization ability (subfertility) is a newborn necessity. This investigation is a sequential study to determine the kinetics of surface carbohydrates turnover during in vitro capacitation and AR in fertile and subfertile boar sperm. Flow cytometry determinations of the binding of three FITC-labeled lectins were assessed. WGA binding was significantly lower in fresh, capacitated, and acrosome-reacted sperm of subfertile boars than in fertile boars. Con-A binding was not significantly different in fresh sperm of fertile and subfertile boars. However. Con-A labeling in capacitated, and acrosome-reacted sperm differed significantly in both groups. UEA binding increased only in capacitated sperm of subfertile boars. These findings could be used as indicators of capacitation and AR and may also be a good indicator of sperm fertilizing ability in boars.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0148-5016
pubmed:author
pubmed:issnType
Print
pubmed:volume
48
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
159-66
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Expression of lectin receptors on the membrane surface of sperm of fertile and subfertile boars by flow cytometry.
pubmed:affiliation
Depto Ciencias de la Salud, Universidad Autónoma Metropolitana-lztapalapa, México, DF.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't