Linked Life Data

10837118

Source:http://linkedlifedata.com/resource/pubmed/id/10837118

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2000-7-24
pubmed:abstractText
The sperm surface protein fertilin functions in sperm-egg interaction. On guinea pig and bovine sperm, fertilin is a heterodimer of alpha and beta subunits. Both subunits are initially synthesized as precursors and then proteolytically processed by removing N-terminal domains. Since the mouse is currently the main mammalian species in which fertilization is studied, in the present report, we analyzed the structure, processing, and expression of fertilin in mouse. We found that the processing of mouse fertilin beta occurs during epididymal maturation and involves changes in the cytoplasmic tail domain as well as the N-terminal domains. Although we (R. Yuan et al., 1997, J. Cell Biol. 137, 105-112) and others (M. S. Chen et al., 1999, J. Cell Biol. 144, 549-561) have previously reported that mature fertilin beta is 55-57 kDa, here we show that 55 kDa is an unrelated protein in the sperm extract which cross-reacts with an antibody that recognizes precursor, but not mature, fertilin beta. Comparison of Western blots of wild-type and fertilin beta knockout sperm revealed that authentic, mature fertilin beta is 45 kDa. We also obtained direct evidence that mouse fertilin alpha and beta exist as a heterodimer. In addition, we found that in mice lacking the fertilin beta subunit, fertilin alpha is absent from mature sperm. A widely proposed model for sperm-egg fusion suggests that fertilin alpha is the sperm component that promotes membrane fusion by undergoing a conformational change that exposes a virus-like, hydrophobic fusion peptide. Because sperm lacking fertilin alpha and fertilin beta can fuse with eggs at 50% the wild-type rate, this model is called into question. The results suggest instead that other gamete surface molecules act to promote membrane fusion and that fertilin's role in gamete fusion is in sperm-egg plasma membrane adhesion.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0012-1606
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
222
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
289-95
pubmed:dateRevised
2009-9-2
pubmed:meshHeading
pubmed-meshheading:10837118-ADAM Proteins, pubmed-meshheading:10837118-Amino Acid Sequence, pubmed-meshheading:10837118-Animals, pubmed-meshheading:10837118-Cattle, pubmed-meshheading:10837118-Dimerization, pubmed-meshheading:10837118-Epididymis, pubmed-meshheading:10837118-Female, pubmed-meshheading:10837118-Genotype, pubmed-meshheading:10837118-Guinea Pigs, pubmed-meshheading:10837118-Macromolecular Substances, pubmed-meshheading:10837118-Male, pubmed-meshheading:10837118-Membrane Glycoproteins, pubmed-meshheading:10837118-Metalloendopeptidases, pubmed-meshheading:10837118-Mice, pubmed-meshheading:10837118-Mice, Inbred ICR, pubmed-meshheading:10837118-Mice, Knockout, pubmed-meshheading:10837118-Molecular Sequence Data, pubmed-meshheading:10837118-Sperm-Ovum Interactions, pubmed-meshheading:10837118-Spermatozoa
pubmed:year
2000
pubmed:articleTitle
Analysis of mouse fertilin in wild-type and fertilin beta(-/-) sperm: evidence for C-terminal modification, alpha/beta dimerization, and lack of essential role of fertilin alpha in sperm-egg fusion.
pubmed:affiliation
Section of Molecular and Cellular Biology, University of California at Davis, Davis, California, 95616, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.