Protein secretion by Xenopus laevis oocytes and their surrounding follicular cells in vitro has been investigated using two-dimensional gel electrophoresis. Viable oocytes, devoid of follicle layers, were prepared by treatment with collagenase; they retain in full their capacity to synthesize, sequester and export secretory proteins following microinjection with heterologous messenger RNA. Both RNA-injected and normal cells export a large number of endogenous oocyte proteins and, as with heterologous secretory translation products, these proteins are found within the oocyte in a vesicle fraction. Electron microscopy indicates that secretion involves exocytotic release of cortical vesicle contents. The follicular cells themselves also seem to contribute a number of proteins to the incubation medium surrounding isolated oocytes, but the presence of follicle layers is not required for the export of endogenous oocyte proteins.

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