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Activation of c‐Jun NH2‐terminal kinases by interleukin‐1β in normal human osteoblastic and rat UMR‐106 cells
Author(s) -
Chaudhary Lala R.,
Avioli Louis V.
Publication year - 1998
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(19980401)69:1<87::aid-jcb10>3.0.co;2-c
Subject(s) - kinase , mapk/erk pathway , microbiology and biotechnology , mitogen activated protein kinase , c jun , signal transduction , protein kinase a , chemistry , biology , biochemistry , transcription factor , gene
We recently demonstrated the activation of extracellular signal‐ regulated protein kinase 1 and 2 (ERK1 and ERK2) by IGF‐1, FGF‐2, and PDGF‐BB in normal human osteoblastic (HOB) cells as well as in rat and mouse osteoblastic cells. In this report, we have examined whether c‐Jun NH2‐Terminal Kinase (JNK) pathway is activated by growth factors and interleukin‐1β (IL‐1β) in normal HOB and rat UMR‐106 cells using immune‐complex kinase assay and anti‐active JNK antibody, which recognizes activated forms of both JNK1 and JNK2. Results have demonstrated the presence of JNK1 and JNK2 proteins in normal HOB and UMR‐106 cells. Both JNK1 and JNK2 were activated by IL‐1β. IL‐1β preferentially activated JNK pathway in a dose‐ and time‐dependent manner and had little effect on ERK pathway. On the other hand, FGF‐2 did not activate JNK but most strongly activated ERK pathway. The activation of JNK was maximal at 20 min whereas maximal activation of ERK1 and ERK2 was observed within 10 min. Results have clearly demonstrated that IL‐1β preferentially activates JNK pathway whereas FGF‐2 activates ERK pathway in normal human and rat UMR‐106 osteoblastic cells. J. Cell. Biochem. 69:87–93, 1998. © 1998 Wiley‐Liss, Inc.