MAMMALIAN OOCYTES EXHIBIT SPECIFIC RECOGNITION OF THE RGD (ARG-GLY-ASP) TRIPEPTIDE AND EXPRESS OOLEMMAL INTEGRINS

Integrins are a family of cell adhesion receptors involved in many cel l-cell and cell-matrix interactions. Some of these heterodimeric recep tors, such as alpha5beta1 and alphavbeta1, specifically recognize the amino acid sequence Arg-Gly-Asp (RGD) within their ligands. The RGD se quence is found in fibronectin, vitronectin, and other extracellular m atrix proteins. Our results demonstrate that the oolemmas of eggs from human and several other mammalian species contain receptors capable o f binding to RGD ligands, and that integrin subunits are expressed by oocytes. Four distinct techniques were utilized to identify the presen ce of functional integrins on mammalian eggs. RGD-binding receptors we re detected on the surfaces of zona-free eggs from all species tested. Covaspheres coated with PepTide-2000, which contains RGD, bound to th e eggs and formed rosettes. Rosetting was competitively inhibited by P eptide-2000 and by GRGDTP, a soluble RGD peptide, but not by RGES. An ELISA using polyclonal antibodies directed against the cytoplasmic tai ls of the integrin subunits identified the integrin subunits alpha5, b eta1, and alphav, but not beta3, in detergent extracts of Syrian hamst er eggs. A dot blot confirmed the presence of alphav in hamster egg ly sates. Finally, the integrin subunits alpha2, alpha5, alpha6, but not alpha4, were detected on the surfaces of zona-free eggs from human and Syrian hamster. Immunobeads coated with monoclonal antibodies specifi c for alpha2, alpha5, and alpha6 bound to the eggs and formed rosettes . A similar rosetting was obtained from beads coated with polyclonal a ntibody against the vitronectin receptor (alphavbeta3/beta5). These ob servations suggest that the integrins alpha2beta1, alpha5beta1, alpha6 beta1, and one or more integrins containing alphav are expressed by oo cytes. We propose that these integrins may play important roles in fer tilization and implantation. (C) 1993 Wiley-Liss, Inc.