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- W2022306021 abstract "Intact human parathyroid hormone, hPTH [1–84], and the hPTH [1–34] fragment stimulated membrane-associated protein kinase C (PKC) activity in immortalized (but still differentiation-competent) murine BALB/MK-2 skin keratinocytes. Unexpectedly, the hormone and its fragment did not stimulate adenylate cyclase. The failure of PTH to stimulate adenylate cyclase activity was not due to the lack of a functioning receptor-cyclase coupling mechanism because the cells were stimulated to synthesize cyclic adenosine monophosphate (cyclic AMP) by the β-adrenergic drug isoproterenol. Thus, skin keratinocytes seem to have an unconventional PTH receptor that is coupled to a PKC-activating mechanism but not to adenylate cyclase. These observations suggest that normal and neoplastic skin keratinocytes respond to the PTH-related peptide that they make and secrete." @default.
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- W2022306021 date "1992-02-01" @default.
- W2022306021 modified "2023-10-15" @default.
- W2022306021 title "Parathyroid hormone stimulates protein kinase C but not adenylate cyclase in mouse epidermal keratinocytes" @default.
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- W2022306021 doi "https://doi.org/10.1002/jcp.1041500212" @default.
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