RELATION BETWEEN THE THIOL STATUS OF ODF1 AND THE SPERM MOTILITY. COMPARISON BETWEEN NORMO AND ASTHENOZOOSPERMIC SAMPLES

CABRILLANA M E; MARTINEZ MV; RUIZ ESTRABÓN M ; GUERRI MB ; MONCLUS M; VINCENTI A; FORNÉS MW

Mendoza

Congreso; XXXI Reunión Anual de la Sociedad de Biología de Cuyo; 2013

Sociedad de Biología de Cuyo

A correct assembling of the sperm tail in the testis and efficient maturation during epididymal transit is necessary for good motility. In the epididymal transit the thiols of flagellar proteins like ODF1 are oxidized and the sperm became motile. The aim of this work is to determine the importance of proteins thiol status in human sperm motility. Monobromobimane (mBBr) was used as specific thiol marker. Our previus results indicate that the interaction between mBBr and thiols interferes the rat sperm motility. Several proteins were labeled by mBBr including ODF1. Recordings of human sperms incubated with monobromobimane showed a decrease of the progressive motility. Other experiment was developing to compare normozoospermics (31) with asthenozoospermics (15) samples checking their thiol status. The mBBr fluorescent signal of the sperm tail in normal samples was lower, comparing with those from asthenozoospermics, suggesting an incomplete thiol oxidation. ODF1 was de most fluorescent protein detected by sds-page and western blot analysis. This work demonstrate that blocking thiol groups with mBBr change the progressive motility in human sperm to curvilinear movement and the role of these proteins, including ODF1, in the mechanisms that regulate progressive motility.