Proteomic studies in spermatogenesis

    In closed connection with functional genomic studies, proteomic analysis during testis development, associated to germ cell differentiation, have been carried out. By means of the 2D-PAGE maps and analysis by MALDI-TOF we have identified the pattern of accumulation of 44 soluble proteins or isoforms in the testis development. Proteins with redox or antioxidant activity were identified in high proportion, some of those not previously characterised in testis. Similar experimental approach has been carried out in the proteomic analysis of testis from animals exposed in vivo to endocrine disruptors considered environmental pollutants (see Reprotoxicity, gene deregulation and male infertility).

Concerning defined proteins, in this period we are focussed in three interacting proteins, associated to cytoplasm membrane, involved in cell adhesion and cytoskeletal reorganization : vinexin, vinculin and flotillin 1. We have previously demonstrated that flotillin1, associated to "lipid rafts" participates in cell-cell interactions and is present in Sertoli cells (somatic component of the seminiferous epithelium). As significant results we have demonstrated (article in press) a new isoform of vinexin (vinexin t) in germ cells. As well as, we detected that in mice exposed in vivo to 17-beta estradiol, a total depletion of this new germ cell-vinexin form. These results seems to be in agreement with some effects found in developmental pathologies in testis associated to alterations of cell interactions in the seminiferous epithelium caused by exposure to estrogenic compounds (xenoestrogens).