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MPM-2, a monoclonal antibody specific for cells in mitosis, recognizes a family of proteins that share a common phosphorylated epitope. In this study we have shown that during the maturation of Xenopus laevis oocytes induced by progesterone, phosphorylation of MPM-2 antigens coincided with the appearance of MPF activity. When MPM-2 (0.7-1.4 micrograms per oocyte) was injected into oocytes prior to progesterone stimulation, MPF activity failed to appear and induction of maturation was inhibited as judged by both germinal-vesicle breakdown and white-spot formation. Further, MPM-2 was able to neutralize as well as immunodeplete MPF activity from mitotic HeLa cell and mature oocyte extracts. These results suggest that MPM-2 recognizes either MPF itself or a protein(s) that regulates MPF activity and that the kinase that phosphorylates MPM-2 antigens may be a key component in the regulation of M-phase induction.
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