PMID:
     19408963
Authors:
     Secciani F, Bianchi L, Ermini L, Cianti R, Armini A, La Sala GB,
     Focarelli R, Bini L, Rosati F.
Title:
     Protein profile of capacitated versus ejaculated human sperm.
Journal:
     J Proteome Res. 2009 Jul;8(7):3377-89. doi: 10.1021/pr900031r.
Abstract:
     Freshly ejaculated sperm acquire the fertilizing potential by a continuing 
     process that occurs during sperm transport through the female genital tract, and 
     it is physiologically not complete until the spermatozoon reaches the oocyte. The 
     process termed capacitation can be mimicked in vitro by using appropriate 
     capacitation media. Despite its importance, the molecular mechanisms underlying 
     capacitation are poorly understood. This work deals with a proteomic approach to 
     the analysis of protein profile variations in human normospermic samples as a 
     consequence of three hours in vitro capacitation. 2DE gels were produced per 
     freshly ejaculated sperm and per capacitated sperm and several quantitative and 
     qualitative significant variations were found. Among the MS obtained 
     identifications, proteins with a significant decrease after capacitation were 
     found to be involved in protein fate, metabolism, and flagellar organization; on 
     the contrary, increasing proteins were found to be related to cellular stress. 
     Interestingly, the detected flagellar organization proteins decreased during 
     capacitation whereas their corresponding fragments increased. A swim-up selected 
     and three-hour capacitated sperm subpopulation has also been resolved by 2DE, and 
     its synthetic gel has been analyzed for the variations observed in the entire 
     sperm population. An immunofluorescence analysis of this sperm typology was 
     carried out with antiactin and antitubulin antibodies.

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