Artículos de revistas
Participation of cysteine-rich secretory proteins (CRISP) in mammalian sperm-egg interaction
Fecha
2008Registro en:
Cohen, Debora Juana; Busso, Dolores; Da Ros, Vanina Gabriela; Ellerman, Diego Andrés; Maldera, Julieta Antonella; et al.; Participation of cysteine-rich secretory proteins (CRISP) in mammalian sperm-egg interaction; Universidad del País Vasco; International Journal Of Developmental Biology; 52; -1-2008; 737-742
0214-6282
1696-3547
CONICET Digital
CONICET
Autor
Cohen, Debora Juana
Busso, Dolores
Da Ros, Vanina Gabriela
Ellerman, Diego Andrés
Maldera, Julieta Antonella
Goldweic, Nadia Micaela
Cuasnicu, Patricia Sara
Resumen
Mammalian fertilization is a complex multi-step process mediated by different molecules present on both gametes. CRISP1 (cysteine-rich secretory protein 1) is an epididymal protein thought to participate in gamete fusion through its binding to egg-complementary sites. Structure-function studies using recombinant fragments of CRISP1 as well as synthetic peptides reveal that its egg-binding ability resides in a 12 amino acid region corresponding to an evolutionary conserved motif of the CRISP family, named Signature 2 (S2). Further experiments analyzing both the ability of other CRISP proteins to bind to the rat egg and the amino acid sequence of their S2 regions show that the amino acid sequence of the S2 is needed for CRISP1 to interact with the egg. CRISP1 appears to be involved in the first step of sperm binding to the zona pellucida, identifying a novel role for this protein in fertilization. The observation that sperm testicular CRISP2 is also able to bind to the egg surface suggests a role for this protein in gamete fusion. Subsequent experiments confirmed the participation of CRISP2 in this step of fertilization and revealed that CRISP1 and CRISP2 interact with common egg surface binding sites. Together, these results suggest a functional cooperation between CRISP1 and CRISP2 to ensure the success of fertilization. These observations contribute to a better understanding of the molecular mechanisms underlying mammalian fertilization.