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Activation of p38 mitogen‐activated protein kinase is crucial in osteoclastogenesis induced by tumor necrosis factor
Author(s) -
Matsumoto Masahito,
Sudo Tatsuhiko,
Maruyama Masumi,
Osada Hiroyuki,
Tsujimoto Masafumi
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02231-6
Subject(s) - osteoclast , tumor necrosis factor alpha , protein kinase a , multinucleate , microbiology and biotechnology , macrophage colony stimulating factor , p38 mitogen activated protein kinases , cancer research , activator (genetics) , bone marrow , biology , kinase , macrophage , immunology , receptor , biochemistry , in vitro
Tumor necrosis factor (TNF) induces osteoclast differentiation from bone marrow cells in the presence of macrophage colony‐stimulating factor. Treatment of bone marrow cells with SB203580 but not PD98059 inhibited TNF‐induced osteoclast differentiation. In RAW264 cells which differentiate into osteoclast‐like multinucleated cells by TNF treatment alone, activation of p38 mitogen‐activated protein (MAP) kinase induced by murine TNF was comparable to and independent of the receptor activator of necrosis factor‐κB ligand. Moreover, the number of multinucleated osteoclasts induced by TNF in bone marrow cell cultures derived from p38 MAP kinase gene deficient mice was significantly less than that from control mice. These results indicate that the p38 MAP kinase pathway plays a crucial role in TNF‐mediated osteoclast differentiation.