Document Detail


Label-free quantitation of phosphopeptide changes during rat sperm capacitation.
MedLine Citation:
PMID:  19947656     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Before fertilization can occur, ejaculated mammalian spermatozoa must undergo a maturation process known as capacitation, which is dominated by post-translational modifications, particularly phosphorylation. Despite its biological importance, characterization of those proteins targeted for phosphorylation during capacitation remains ill-defined. Here, we report the isolation and purification of 288 phosphorylated peptides from rat spermatozoa using titanium dioxide columns in combination with nanoflow mass spectrometry. This equated to 120 identified phosphorylated proteins present in pure populations of spermatozoa. The MS survey scans of replicate titanium dioxide eluates, derived from both noncapacitated and capacitated sperm lysates, were then compared in silico using a virtual 2D PAGE format and DeCyderMS software. This analysis found 15 differentially phosphorylated proteins during capacitation. Included in this list were sperm qualifiers such as Izumo, a known sperm-oocyte fusion protein. To demonstrate that this label-free quantitative approach to phosphoprotein analysis was viable, we measured the enzymatic activity of 5'-nucleotidase, the phosphorylation status of which changed during capacitation. The results revealed, for the first time, that 5'-nucleotidase activity is up-regulated as sperm capacitate. This change, together with the other protein identifications reported in this study, constitute important new leads in elucidating the biochemical mechanisms by which spermatozoa attain a capacitated state.
Authors:
Mark A Baker; Nathan D Smith; Louise Hetherington; Kristy Taubman; Mark E Graham; Phillip J Robinson; R John Aitken
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of proteome research     Volume:  9     ISSN:  1535-3907     ISO Abbreviation:  J. Proteome Res.     Publication Date:  2010 Feb 
Date Detail:
Created Date:  2010-02-05     Completed Date:  2010-04-29     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101128775     Medline TA:  J Proteome Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  718-29     Citation Subset:  IM    
Affiliation:
The ARC Centre of Excellence in Biotechnology and Development, Priority Research Centre in Reproductive Science, School of Environmental and Life Sciences, University of Newcastle, Callaghan, NSW, 2308, Australia. Mark.Baker@newcastle.edu.au
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Electrophoresis, Polyacrylamide Gel
Male
Molecular Sequence Data
Phosphopeptides / chemistry,  metabolism*
Rats
Sperm Capacitation*
Chemical
Reg. No./Substance:
0/Phosphopeptides
Comments/Corrections
Comment In:
J Proteome Res. 2010 Feb 5;9(2):639   [PMID:  20039706 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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