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Parathyroid hormone stimulates protein kinase C but not adenylate cyclase in mouse epidermal keratinocytes
Author(s) -
Whitfield James F.,
Chakravarthy Balu R.,
Durkin Jon P.,
Isaacs Richard J.,
Jouishomme Hervé,
Sikorska Marianna,
Williams Ross E.,
Rixon Raymond H.
Publication year - 1992
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041500212
Subject(s) - cyclase , adenylate kinase , parathyroid hormone , endocrinology , medicine , growth hormone releasing hormone receptor , cyclic adenosine monophosphate , adenosine , protein kinase c , protein kinase a , parathyroid hormone receptor , receptor , chemistry , hormone , keratinocyte , biology , hormone receptor , signal transduction , kinase , biochemistry , calcium , cancer , breast cancer , in vitro
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.