Protein kinase C-activating domains of parathyroid hormone-related protein.
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| Abstract |
N-terminal fragments of PTH-related protein (PTHrP), PTHrP-(1-34), and PTHrP-(1-40) stimulated both adenylyl cyclase and a mechanism that increases membrane-associated protein kinase C (PKC) activity in ROS 17/2 rat osteosarcoma cells. There were two peaks in the PKC response to the N-terminal PTHrP fragments: one peak was obtained with picomolar and the other with nanomolar PTHrP concentrations. The PKC-stimulating picomolar concentrations of the PTHrP fragments did not detectably stimulate adenylyl cyclase, but the nanomolar concentrations did. Since a similar two-peak response of PKC activity was obtained with PTHrP-(28-34), the single, N-terminal PKC activation domain of the PTHrP is in the same 28-34 region of the molecule as that of PTH despite this region having different primary amino acid sequences in the two hormones. Unlike PTH, PTHrP has a second PKC activation domain, as indicated by the ability of picomolar concentrations of the PTHrP-(107-111) fragment to stimulate maximally membrane-associated PKC activity in the osteosarcoma cells.
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| Authors | L Gagnon, H Jouishomme, J F Whitfield, J P Durkin, S MacLean, W Neugebauer, G Willick, R H Rixon, B Chakravarthy |
| Journal | Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research (J Bone Miner Res) Vol. 8 Issue 4 Pg. 497-503 (Apr 1993) ISSN: 0884-0431 [Print] United States |
| PMID | 8475799 (Publication Type: Journal Article) |
| Chemical References |
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