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  • Title: H-89 inhibits collagenase induction by phorbol ester through a mechanism that does not involve protein kinase A.
    Author: Shoshan MC, Ljungdahl S, Linder S.
    Journal: Cell Signal; 1996 Mar; 8(3):191-5. PubMed ID: 8736703.
    Abstract:
    Cyclic adenosine monophosphate (cAMP)-dependent protein kinase A (PKA) regulates the activity of growth-factor-induced pathways at the level of cytoplasmic kinases and nuclear transcription factors. We observed that H-89, an inhibitor of PKA, induced mitogen-activated protein (MAP) kinase activity in a 12V-ras-transformed fibroblast cell line. In contrast, H-89 inhibited phorbol-ester-mediated induction of MAP kinase, junB messenger ribonucleic acid (mRNA), and collagenase mRNA in these cells. Phorbol-ester stimulation of a collagenase-promoter reporter construct was also inhibited by H-89. However, stimulation of the collagenase promoter was not inhibited by overexpression of the PKA-inhibitory protein PKI. These data suggest that H-89 inhibits the activity of an enzyme required for phorbol-ester induction of collagenase mRNA, but that this inhibition does not occur at the level of PKA.
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