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A DUB, Ubiquitin C‐terminal Hydrolase‐L3 Affects Osteoblast Formation
Author(s) -
KIM JI YOUNG,
Ahn Sang-Ho,
Wada Keiji,
Cho Je-Yoel
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.lb481
Subject(s) - osteoblast , ubiquitin , deubiquitinating enzyme , bone remodeling , microbiology and biotechnology , chemistry , bone morphogenetic protein 2 , biology , endocrinology , biochemistry , gene , in vitro
Deubiquitination, the reversal of ubiquitination, is the action of deubiquitinating enzymes (DUBs). Its mechanism is essential in various biological processes and diseases. Mutations in genes expressing DUBs have been implicated in a number of diseases including cancer, neurodegeneration, and osteoporosis. Our recent study showed that ubiquitin C‐terminal hydrolase L3 (Uch‐L3), a DUB, regulates Smad1 ubiquitination and bone morphogenetic protein 2‐induced osteoblast differentiation. In this study, for the first time, we observed the specific function of Uch‐L3 in bone metabolism in vivo. Uch‐L3 knock‐out mice have the osteoporotic phenotype, such as less bone mass than that of control group. The decreased activity of osteoblast was also observed in Uch‐L3 knock‐out mice by the analysis of calcein double labeling. In primary osteoblast cells, the deficiency of Uch‐L3 gave the delayed mineralization. An amazing observation, furthermore, was the increased expression of Uch‐L3 during the osteoblastogenesis. Therefore, these results suggest Uch‐L3 might be an important modulator of osteoblast formation in the maintenance of bone homeostasis. [This research was supported by a grant from the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology (No. 2010‐0011231).]