Parathyroid hormone stimulates protein kinase C but not adenylate cyclase in mouse epidermal keratinocytes

✍ Scribed by James F. Whitfield; Balu R. Chakravarthy; Jon P. Durkin; Richard J. Isaacs; Hervé Jouishomme; Marianna Sikorska; Ross E. Williams; Raymond H. Rixon

• Book ID: 102887272
• Publisher: John Wiley and Sons
• Year: 1992
• Tongue: English
• Weight: 534 KB
• Volume: 150
• Category: Article
• ISSN: 0021-9541
• DOI: 10.1002/jcp.1041500212

✦ Synopsis

Intact human parathyroid hormone, hPTH 11-84], and the hPTH 11-34] fragment stimulated membrane-associated protein kinase C (PKC) activity in immortalized (but still differentiation-competent) murine BALBIMK-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-cyclasc coupling mechanism because the cells were stimulated to synthesize cyclic adenosine monophosphate (cyclic AMP) by the P-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.