Parathyroid hormone fragment [3-34] stimulates protein kinase C (PKC) activity in rat osteosarcoma and murine T-lymphoma cells.
The parathyroid hormone (PTH) fragment [1-34] strongly stimulated both adenylate cyclase and membrane-associated PKC activities in rat 17/2 osteosarcoma cells. By contrast, the PTH [3-34] fragment, which was unable to stimulate adenylate cyclase, remained a potent stimulator of membrane-associated PKC activity in these cells. Both PTH fragments also strongly stimulated membrane-PKC activity in cyc-S49T-lymphoma cells possessing a defective adenylate cyclase system. This ability of PTH [3-34] to stimulate membrane-associated PKC activity could explain the residual bioactivity of this fragment.
Chakravarthy
B R
BR
Division of Biological Sciences, National Research Council of Canada, Ottawa, Ontario.
Durkin
J P
JP
Rixon
R H
RH
Whitfield
J F
JF
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000201:enzymology; D000242:Cyclic AMP / Q000378:metabolism; D007700:Kinetics; D008223:Lymphoma; D051379:Mice; D012516:Osteosarcoma; D010281:Parathyroid Hormone / Q000494:pharmacology*; D010446:Peptide Fragments / Q000494:pharmacology*; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats
D010281:Parathyroid Hormone; D010446:Peptide Fragments; C031617:parathyroid hormone (3-34); D000255:Adenosine Triphosphate; D000242:Cyclic AMP; D011493:Protein Kinase C