Linked Life Data

11730909

Source:http://linkedlifedata.com/resource/pubmed/id/11730909

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2001-12-3
pubmed:abstractText
Bovine seminal vesicles secrete a family of similar proteins designated BSP-A1, BSP-A2, BSP-A3 and BSP-30-kDa (collectively called bovine seminal plasma (BSP) proteins). The biochemical properties of these proteins are well documented and considerable progress has been made concerning their biological role. At ejaculation these BSP proteins bind to the sperm surface. The binding sites on the sperm surface have been identified as choline phospholipids (specifically phosphatidylcholine (PC), phophatidylcholine plasmalogen (PC plasm) and sphingomyelin (SPM)) composed of sperm plasma membrane. Our previous studies have shown that the BSP proteins interact specifically with heparin and high-density lipoproteins (HDL), the capacitation factors in bovine. In addition, we have shown that the BSP proteins potentiate epididymal sperm capacitation induced by heparin and HDL. Recently, we showed that the BSP proteins stimulated cholesterol and phospholipid efflux from the sperm membrane. Furthermore, the lipid efflux from sperm is dependent on BSP protein concentration and duration of incubation. The loss of membrane cholesterol is an important step in the capacitation process. These results together indicate that BSP proteins play an important role in sperm membrane lipid modification events that occur during sperm capacitation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0165-0378
pubmed:author
pubmed:issnType
Print
pubmed:volume
53
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
109-19
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Role of seminal plasma phospholipid-binding proteins in sperm membrane lipid modification that occurs during capacitation.
pubmed:affiliation
Department of Medicine, University of Montreal and Guy-Bernier Research Center, Maisonneuve-Rosemont Hospital, 5415 Blvd. de L'Assomption, Montreal, Québec, Canada H1T 2M4. manjunap@medclin.umontreal.ca
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't