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 subpopu- lation 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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|Titolo:||Protein profile of capacitated versus ejaculated human sperm.|
|Citazione:||Secciani, F., Bianchi, L., Ermini, L., Cianti, R., Armini, A., LA SALA, G.b., et al. (2009). Protein profile of capacitated versus ejaculated human sperm. JOURNAL OF PROTEOME RESEARCH, 8, 3377-3789.|
|Appare nelle tipologie:||1.1 Articolo in rivista|