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  • Title: Parathyroid hormone stimulates protein kinase C but not adenylate cyclase in mouse epidermal keratinocytes.
    Author: Whitfield JF, Chakravarthy BR, Durkin JP, Isaacs RJ, Jouishomme H, Sikorska M, Williams RE, Rixon RH.
    Journal: J Cell Physiol; 1992 Feb; 150(2):299-303. PubMed ID: 1310323.
    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 beta-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.
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