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Presence, processing and localization of mouse ADAM15 during sperm maturation and the role of its disintegrin domain during sperm-egg binding

K Pasten-Hidalgo, Biologia Celular, CINVESTAV-IPN, Mexico City, Mexico
R Hernandez-Rivas, Biomedicina Molecular, CINVESTAV-IPN, Mexico City, Mexico
A Roa-Espitia, Biologia Celular, CINVESTAV-IPN, Mexico City, Mexico
M Sanchez-Gutierrez, Instituto de Ciencias de la Salud, Universidad de Pachuca, Pachuca, Mexico
F Martinez-Perez, Facultad de Ciencias, UNAM, Mexico City, Mexico
A O-Monroy, Biologia Celular, CINVESTAV-IPN, Mexico City, Mexico
E Hernandez-Gonzalez, Biologia Celular, CINVESTAV-IPN, Mexico City, Mexico
A Mujica, Biología Celular, Cinvestav, México, 07000, Mexico

Correspondence: Adela Mujica, Email: adelam{at}cell.cinvestav.mx

Abstract

Successful fertilization requires gametes to complete several stages, beginning with maturation and transport along the male and female reproductive tracts and ending with the interaction between the sperm and the egg. This last step involves sperm-egg adhesion and membrane fusion. Metalloprotease-disintegrin (ADAMs) consists of a family of membrane-anchored glycoproteins thought to play diverse roles in cell-cell adhesion through their interaction with integrins. This study analyses the presence, location, processing and possible role of ADAM15 in mouse sperm. The presence of ADAM15 in mouse spermatozoa was detected by Western blotting, which revealed that ADAM15 is post-translationally processed, during epididymal sperm maturation and the acrosome reaction. The 35 kDa antigen present in the acrosome-reacted sperm is the last proteolytic product of the 110/75 kDa ADAM15 found in non-capacitated sperm. This 35 kDa protein contains the disintegrin domain. By indirect immuno-fluorescence, ADAM15 was identified in the acrosomal region and along the flagellum of mouse spermatozoa. In acrosome-reacted sperm, ADAM15 was lost from the acrosomal region, but remained diffusely distributed throughout the head and flagellum. Furthermore, the ADAM15 disintegrin domain (RPPTDDCDLPEF), partially inhibited fusion and almost completely inhibited sperm-oolemma adhesion. In conclusion, our data indicate that ADAM15 is present in the testis and in spermatozoa from the caput, corpus and cauda epididymal, as well as in non-capacitated and acrosome-reacted gametes. Results also indicate that ADAM15 is processed during epididymal maturation and acrosome reaction and that it may play a role during sperm-egg binding.