Glucose-regulated protein 78 (Grp78/BiP) is secreted by human oviduct epithelial cells and modulates sperm-zona pellucida binding.

MARÍN-BRIGGILER, C.I.; GONZÁLEZ-ECHEVERRÍA, M.F.; MUNUCE, M.J.; GHERSEVICH, S.; CAILLE, A.M.; HELLMAN, U.; CORRIGALL, V.M.; VAZQUEZ LEVIN, M.H.

FERTILITY AND STERILITY

Elsevier

Lugar: Nueva York. NY. EEUU; Año: 2010 vol. 93 p. 1574 - 1584

0015-0282

Fertil Steril. 2010 Mar 15;93(5):1574-84. Epub 2009 Mar 17 Objective: To determine the secretion of Grp78 by human oviduct epithelial cells, its association to spermatozoa, and its involvement in gamete interaction. Design: Prospective study. Setting: Basic research laboratory. Subject(s): Semen samples obtained from normozoospermic volunteers. Tubal tissue provided by patients undergoing hysterectomies. Oocytes collected from women undergoing IVF-ET. Intervention(s): Analysis of Grp78 expression and secretion by oviductal tissue. Gamete incubation with recombinant Grp78 (rec-Grp78). Main outcome measure(s): Assessment of protein expression and secretion by immunohistochemistry and Western immunoblotting, respectively. Evaluation of rec-Grp78 binding to human spermatozoa by immunocytochemistry, and analysis of its effect upon gamete interaction using the hemizona assay. Result(s): Grp78 was found in the surface of oviduct epithelial cells. Soluble Grp78 was detected in oviductal fluids from women in the periovulatory period and in oviductal tissue conditioned medium. Rec-Grp78 was able to bind to the sperm acrosomal cap, and its presence during gamete interaction led to a decrease in the number of spermatozoa bound to the zona pellucida (ZP). When calcium ions from the incubation medium were replaced by strontium, rec-Grp78 enhanced sperm-ZP interaction. Conclusion(s): Grp78 is expressed and secreted by oviduct epithelial cells. The protein would bind to the gametes and may modulate their interaction in a calcium-dependent manner.