Protein profile of capacitated versus ejaculated human sperm

Federica Secciani, Laura Bianchi, Leonardo Ermini, Riccardo Cianti, Alessandro Armini, Giovan Battista La Sala, Riccardo Focarelli, Luca Bini, Floriana Rosati

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)3377-3389
Number of pages13
JournalJournal of Proteome Research
Volume8
Issue number7
DOIs
Publication statusPublished - Jul 6 2009

Keywords

  • 2DE
  • Capacitation
  • Human sperm
  • Mass spectrometry

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)

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