Overproduction of a Ca(2+)-independent protein kinase C isozyme, nPKC epsilon, increases the secretion of prolactin from thyrotropin-releasing hormone-stimulated rat pituitary GH4C1 cells.

@article{Akita1994OverproductionOA,
  title={Overproduction of a Ca(2+)-independent protein kinase C isozyme, nPKC epsilon, increases the secretion of prolactin from thyrotropin-releasing hormone-stimulated rat pituitary GH4C1 cells.},
  author={Yoshiko Akita and Shigeo Ohno and Yukiko Yajima and Yusuke Konno and Takaomi C Saido and Kouichi Mizuno and Kazuhiro Chida and S. Osada and Toshio Kuroki and Seinosuke Kawashima},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 6},
  pages={4653-60}
}
Rat pituitary GH4C1 cells express protein kinase C (PKC) transcripts for cPKC alpha, cPKC beta II, nPKC delta, nPKC epsilon, nPKC eta, and aPKC zeta, but not for cPKC gamma or nPKC theta. Of the transcripts produced, the nPKC epsilon isoform is the most abundant. Transfection of GH4C1 cells with an expression plasmid containing nPKC epsilon cDNA leads to the transient overexpression of cellular nPKC epsilon and confers enhanced phorbol ester binding activity. Transient expression of an inactive… CONTINUE READING
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