Abstract
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.
MeSH Terms
Animals
Antibodies, Monoclonal/isolation & purification
Antigen-Antibody Complex
Female
Growth Substances/isolation & purification,pharmacology
HeLa Cells/cytology
Humans
Kinetics
Maturation-Promoting Factor
Mitosis
Oocytes/cytology,drug effects,physiology
Xenopus laevis
Chemicals
Antibodies, Monoclonal
Antigen-Antibody Complex
Growth Substances
Maturation-Promoting Factor
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Kuang J
Department of Medical Oncology, University of Texas M. D. Anderson Cancer Center, Houston 77030.
Zhao J
Wright D A
Saunders G F
Rao P N
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