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J. Biol. Chem., Vol. 276, Issue 10, 7586-7592, March 9, 2001
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From the Parathyroid hormone (PTH) is known to have both
catabolic and anabolic effects on bone. The dual functionality of PTH
may stem from its ability to activate two signal transduction
mechanisms: adenylate cyclase and phospholipase C. Here, we demonstrate
that continuous treatment of UMR 106-01 and primary osteoblasts with PTH peptides, which selectively activate protein kinase C, results in
significant increases in DNA synthesis. Given that ERKs are involved in
cellular proliferation, we examined the regulation of ERKs in UMR
106-01 and primary rat osteoblasts following PTH treatment. We
demonstrate that treatment of osteoblastic cells with very low
concentrations of PTH (10
Stimulation of Extracellular Signal-regulated
Kinases and Proliferation in Rat Osteoblastic Cells by Parathyroid
Hormone Is Protein Kinase C-dependent*
,
**
Cell and Molecular Biology Program and the
Departments of § Pharmacological and Physiological Science
and ¶ Orthopedic Surgery, Saint Louis University School of
Medicine, St. Louis, Missouri 63104 and the ** Department
of Physiology and Biophysics, UMDNJ-Robert Wood Johnson Medical School,
Piscataway, New Jersey 08854.
12 to
1011 M) is sufficient for
substantial increases in ERK activity. Treatment with PTH-(1-34)
(108 M), PTH-(1-31), or
8-bromo-cAMP failed to stimulate ERKs, whereas treatment with phorbol
12-myristate 13-acetate, serum, or PTH peptides lacking the N-terminal
amino acids stimulated activity. Furthermore, the activation of ERKs
was prevented by pretreatment of osteoblastic cells with inhibitors of
protein kinase C (GF 109203X) and MEK (PD 98059). Treatment of UMR
cells with epidermal growth factor (EGF), but not PTH, promoted
tyrosine phosphorylation of the EGF receptor. Transient transfection of
UMR cells with p21N17Ras did not block activation of ERKs
following treatment with low concentrations of PTH. Thus, activation of
ERKs and proliferation by PTH is protein kinase
C-dependent, but stimulation occurs independently of the
EGF receptor and Ras activation.
*
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: Dept. of
Physiology and Biophysics, UMDNJ-Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854. Tel.: 732-235-4552; Fax: 732-235-5038; E-mail: partrinc@umdnj.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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