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J. Biol. Chem., Vol. 276, Issue 34, 32204-32213, August 24, 2001
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From the Calcium Research Laboratory, We investigated the mechanisms of parathyroid
hormone-related peptide (PTHrP)-mediated effects on osteogenic cells in
primary rat bone marrow cell (BMC) cultures. We first demonstrated by reverse transcriptase-polymerase chain reaction and immunocytochemistry that BMCs express the type I parathyroid hormone/PTHrP receptor. Treatment with PTHrP increased osteogenic cell proliferation as determined by [3H]thymidine and bromodeoxyuridine
incorporation and augmented osteogenic colonies. Immunocytochemistry
and Western blotting revealed no direct effect on expression of the
osteoblast markers, type I collagen, bone sialoprotein, and
osteocalcin, indicating that PTHrP did not directly stimulate
differentiation in this system. PTHrP increased mitogen-activated
protein kinase (MAPK) activity in BMC and MAPK activity, and
PTHrP-induced osteogenic cell proliferation could be blocked by the MEK
inhibitor PD-098059. PTHrP also increased Ras activity in BMC. Although
wortmannin and H8, inhibitors of phosphoinositol 3-kinase and protein
kinase A, respectively, did not block PTHrP-stimulated Ras or MAPK
activity, chelerythrin chloride, a known protein kinase C inhibitor,
did block these PTHrP actions as well as PTHrP-induced osteogenic cell
proliferation. These results demonstrate that PTHrP stimulates osteogenic cell proliferation in rat marrow mesenchymal progenitor cells through protein kinase C-dependent activation of the
Ras and MAPK signaling pathway.
Parathyroid Hormone-related Peptide Stimulates
Osteogenic Cell Proliferation through Protein Kinase C Activation of
the Ras/Mitogen-activated Protein Kinase Signaling Pathway*
§,,,
Department of
Medicine and ¶ Department of Neurology and Neurosurgery, McGill
University Health Centre and McGill University, Montreal,
Quebec H3A 1A1, Canada
*
This work was supported in part by Grant MT-5775 (to D. G.)
from the Canadian Institutes for Health Research of Canada, by Grant
00731 (to D. G.) from the National Cancer Institute of Canada, and by
a research contract (to P. S. M.) from Biochem Pharma (Laval, Quebec,
Canada).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Calcium Research
Laboratory, Dept. of Medicine, Royal Victoria Hospital, H4.67, 687 Pine
Ave. West, Montreal, Quebec H3A 1A1, Canada. Tel.: 514-843-1632; Fax:
514-843-1712; E-mail: david.goltzman@muhc.mcgill.ca.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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