15-lipoxygenase metabolite(s) of arachidonic acid mediates adrenocorticotropin action in bovine adrenal steroidogenesis.

@article{Yamazaki199615lipoxygenaseMO,
  title={15-lipoxygenase metabolite(s) of arachidonic acid mediates adrenocorticotropin action in bovine adrenal steroidogenesis.},
  author={Takeshi Yamazaki and Kiyoshi Higuchi and Shiro Kominami and Shigeki Takemori},
  journal={Endocrinology},
  year={1996},
  volume={137 7},
  pages={
          2670-5
        }
}
The acute activation of adrenal glucocorticoid synthesis by ACTH has long been believed to be mediated by cAMP as the major second messenger, although increases in cellular cAMP concentration have not been observed at low concentrations of ACTH. We found that steroidogenesis in bovine adrenal fasciculata-reticularis cells was activated by the addition of arachidonic acid or its 15-lipoxygenase metabolite, 15-hydroperoxyeicosatetraenoic acid. The cellular 15-lipoxygenase pathway was… 
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TLDR
The results suggested that epoxygenase metabolites may have a minor stimulatory effect on ACTH secretion and cyclooxygenases metabolites mayHave a minor inhibitory effect onACTH secretion, and the three major lipoxygen enzyme metabolites tested, 5(S), 12(S)-, and 15(S-hydroxyeicosatetraenoic acid (HETE), all stimulated sustained ACTH release in a dose-dependent manner.
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TLDR
The dominant role played by cAMP-dependentprotein kinase in these adrenal cells was demonstrated by experiments showing the regulation of ornithine decarboxylase gene expression by protein kinase C requires basal camp-dependent protein Kinase activity.
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