Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2010-8-30
pubmed:abstractText
Binder-of-sperm (BSP) proteins interact with sperm membranes and are proposed to extract selectively phosphatidylcholine and cholesterol from these. This change in lipid composition is a key step in sperm capacitation. The present work demonstrates that the interactions between the protein BSP1 and model membranes composed with phosphatidylcholine lead to drastic changes in the morphology of the lipidic self-assemblies. Using cryo-electron microscopy and fluorescence microscopy, we show that, in the presence of the protein, the lipid vesicles elongate, and form bead necklace-like structures that evolve toward small vesicles or thread-like structures. In the presence of multilamellar vesicles, where a large reservoir of lipid is available, the presence of BSP proteins lead to the formation of long nanotubes. Long spiral-like threads, associated with lipid/protein complexes, are also observed. The local curvature of lipid membranes induced by the BSP proteins may be involved in lipid domain formation and the extraction of some lipids during the sperm maturation process.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1090-2104
pubmed:author
pubmed:copyrightInfo
Copyright 2010 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
27
pubmed:volume
399
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
406-11
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Bovine binder-of-sperm protein BSP1 promotes protrusion and nanotube formation from liposomes.
pubmed:affiliation
Department of Chemistry, Center for Self-Assembled Chemical Systems, Université de Montréal, C.P. 6128, Succ. Centre Ville, Montréal, Québec, Canada H3C 3J7. michel.lafleur@umontreal.ca
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't