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J. Biol. Chem., Vol. 261, Issue 15, 6637-6639, May, 1986
T Jahnsen, L Hedin, SM Lohmann, U Walter and JS Richards
In this study purified isoforms of rat ovarian regulatory subunit of type
II cAMP-dependent protein kinase (R-II) were compared with R-II purified
from rat brain. A special neural form of R-II has been previously described
in bovine brain. Analysis by one-dimensional sodium dodecyl
sulfate-polyacrylamide gel electrophoresis resolved three isoforms of rat
ovarian R-II (R-II54, Mr = 54,000; R-II52, Mr = 52,000; and R-II51, Mr =
51,000) compared to two R-II isoforms in rat brain (R-II54 and R-II52).
Polychromatic silver-stained peptide maps of purified R-II subunits
indicated that peptides generated from both rat ovarian R-II52 and R-II51
were similar (if not identical) to the peptides of the neural form, R-II52,
purified from rat brain. These peptides differed markedly from those
generated from R-II54 of either rat ovary, brain, or heart. Ovarian
R-II52/51 photoaffinity labeled with 8-N3-[32P]cAMP and analyzed by
two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis
was shown to consist of three (rather than two) isoelectric variants, which
were similar to three variants resolved from rat brain R-II and clearly
distinct from that of rat heart R-II54. An antibody which recognized both
the R-II54 and R-II52/51 isoforms of rat ovarian extracts also recognized
both forms of rat brain R-II (R-II54 and R-II52) and similar forms in
extracts of rat adrenal and parotid glands. These results strongly suggest
that the R-II52 isoform previously designated as a neural specific form of
R-II is present in high concentrations in a nonneural tissue, the rat
ovary.
The neural type II regulatory subunit of cAMP-dependent protein kinase is present and regulated by hormones in the rat ovary
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