Abstract
Western blot analysis was used to investigate protein kinase C (PKC) profile of rat eggs. The presence of eight PKC isozymes was demonstrated: conventional PKC α, β and γ; novel PKC δ, ϵ and μ; atypical PKC ζ and λ. PKC α was detected by RT-PCR as well. PKC translocation from the cytosol to the plasma membrane served as a marker for enzyme activation. Immunofluorescence confocal microscopy demonstrated a relatively uniform distribution of PKC α, βI, and βII throughout the cytosol of metaphase II arrested eggs. PKC accumulation at the plasma membrane was detected 5 min after exposure to 12- O-tetradecanoyl phorbol-13-acetate and increased with time, thus demonstrating activation of these PKCs.
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