Parathyroid hormone stimulates protein kinase C but not adenylate cyclase in mouse epidermal keratinocytes
| Autor: | Hervé Jouishomme, R. H. Rixon, Balu Chakravarthy, Jon P. Durkin, James F. Whitfield, Ross E. Williams, R. J. Isaacs, Marianna Sikorska |
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| Rok vydání: | 1992 |
| Předmět: |
Keratinocytes
medicine.medical_specialty Growth-hormone-releasing hormone receptor Physiology Molecular Sequence Data Clinical Biochemistry Parathyroid hormone Adenylate kinase Biology Cyclase Mice Structure-Activity Relationship chemistry.chemical_compound Internal medicine Cyclic AMP medicine Animals Cyclic adenosine monophosphate Amino Acid Sequence Protein Kinase C Protein kinase C Mice Inbred BALB C Osteosarcoma Parathyroid hormone receptor Cell Biology Enzyme Activation Endocrinology Epidermal Cells chemistry Parathyroid Hormone Peptides Cyclase activity Adenylyl Cyclases |
| Zdroj: | Journal of Cellular Physiology. 150:299-303 |
| ISSN: | 1097-4652 0021-9541 |
| DOI: | 10.1002/jcp.1041500212 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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