Lactacystin, a proteasome inhibitor, enhances BMP-induced osteoblastic differentiation by increasing active Smads

Biochemical and Biophysical Research Communications

Volumn 407, Issue 1, 2011, Pages 225-229

  Ito, Yuki ^a   Fukushima, Hidefumi ^a   Katagiri, Takenobu ^b   Seo, Yoshinori ^a   Hirata, Shizu ^a   Zhang, Min ^a   Hosokawa, Ryuji ^a   Jimi, Eijiro ^a  

^a KYUSHU DENTAL COLLEGE   (Japan)

^b SAITAMA MEDICAL UNIVERSITY   (Japan)

Author keywords

BMP; Lactacystin; Osteoblast differentiation; Proteasome inhibitor; Smad1

Indexed keywords

ALKALINE PHOSPHATASE; BONE MORPHOGENETIC PROTEIN; BONE MORPHOGENETIC PROTEIN 2; BONE MORPHOGENETIC PROTEIN 4; COLLAGEN TYPE 1; DNA; INHIBITOR OF DIFFERENTIATION 1; LACTACYSTIN; MESSENGER RNA; OSTEOCALCIN; OSTEOGENIC PROTEIN 1; OSTEONECTIN; PROTEASOME INHIBITOR; SMAD PROTEIN; SMAD1 PROTEIN; SMAD8 PROTEIN; TRANSCRIPTION FACTOR OSTERIX; TRANSCRIPTION FACTOR RUNX2;

ANIMAL CELL; ARTICLE; BONE DEVELOPMENT; CELL DIFFERENTIATION; CELL STIMULATION; CONTROLLED STUDY; ENZYME ACTIVITY; GENE TARGETING; MOUSE; NONHUMAN; OSTEOBLAST; OSTEOBLASTIC DIFFERENTIATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION;

ACETYLCYSTEINE; ALKALINE PHOSPHATASE; ANIMALS; BONE MORPHOGENETIC PROTEINS; CELL DIFFERENTIATION; CELL LINE; CYSTEINE PROTEINASE INHIBITORS; HUMANS; MICE; OSTEOBLASTS; OSTEOGENESIS; PROTEASOME ENDOPEPTIDASE COMPLEX; SMAD PROTEINS;

EID: 79953163437     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.03.003     Document Type: Article

References (21)

1. Massagué J., Seoane J., Wotton D. Smad transcription factors. Genes Dev. 2005, 19:2783-2810.
2. Katagiri T., Suda T., Miyazono K. The bone morphogenetic proteins. The TGF-β Family 2008, 121-149. Cold Spring Harbor Press, New York. K. Miyazono, R. Derynck (Eds.).
3. Styrkarsdottir U., Cazier J.B., Kong A., et al. Linkage of osteoporosis to chromosome 20p12 and association to BMP2. PLoS Biol. 2003, 1:E69.
4. Tsuji K., Bandyopadhyay A., Harfe B.D., et al. BMP2 activity, although dispensable for bone formation, is required for the initiation of fracture healing. Nat Genet. 2006, 38:1424-1429.
5. Weissman A.M. Themes and variations on ubiquitylation. Nat. Rev. Mol. Cell Biol. 2001, 2:169-178.
6. Hershko A. The ubiquitin system for protein degradation and some of its roles in the control of the cell division cycle. Cell Death Differ. 2005, 12:1191-1197.
7. Garrett I.R., Chen D., Gutierrez G., et al. Selective inhibitors of the osteoblast proteasome stimulate bone formation in vivo and in vitro. J. Clin. Invest. 2003, 111:1771-1782.
8. Nojima J., Kanomata K., Takada Y., et al. Dual roles of smad proteins in the conversion from myoblasts to osteoblastic cells by bone morphogenetic proteins. J. Biol. Chem. 2010, 285:15577-15586.
9. Yu P.B., Deng D.Y., Lai C.S., et al. BMP type I receptor inhibition reduces heterotopic ossification. Nat. Med. 2008, 14:1363-1369.
10. Gruendler C., Lin Y., Farley J., et al. Proteasomal degradation of Smad1 induced by bone morphogenetic proteins. J. Biol. Chem. 2001, 276:46533-46543.
11. Zhao M., Qiao M., Harris S.E., et al. Smurf1 inhibits osteoblast differentiation and bone formation in vitro and in vivo. J. Biol. Chem. 2004, 279:12854-12859.
12. Katagiri T., Yamaguchi A., Komaki M., et al. Bone morphogenetic protein-2 converts the differentiation pathway of C2C12 myoblasts into the osteoblast lineage. J. Cell Biol. 1994, 127:1755-1766.
13. Hirata S., Kitamura C., Fukushima H., et al. Low-level laser irradiation enhances BMP-induced osteoblast differentiation by stimulating the BMP/Smad signaling pathway. J. Cell. Biochem. 2010, 111:1445-1452.
14. Katagiri T., Imada M., Yanai T., et al. Identification of a BMP-responsive element in Id1, the gene for inhibition of myogenesis. Genes Cells 2002, 7:949-960.
15. Yamazaki M., Fukushima H., Shin M., et al. TNFA represses BMP signaling by interfering with the DNA binding of Smads through the activation of NF-κB. J. Biol. Chem. 2009, 284:35987-35995.
16. Aubin J.E. Regulation of osteoblast formation and function. Rev. Endocr. Metab. Disord. 2001, 2:81-94.
17. Richardson P.G., Mitsiades C., Hideshima T., et al. Bortezomib: proteasome inhibition as an effective anticancer therapy. Annu. Rev. Med. 2006, 57:33-47.
18. Maki C.G., Huibregtse J.M., Howley P.M. In vivo ubiquitination and proteasome-mediated degradation of p53(1). Cancer Res. 1996, 56:2649-2654.
19. Rodriguez M.S., Wright J., Thompson J., et al. Identification of lysine residues required for signal-induced ubiquitination and degradation of IκBα in vivo. Oncogene 1996, 12:2425-2435.
20. Chang S.F., Chang T.K., Peng H.H., et al. BMP-4 induction of arrest and differentiation of osteoblast-like cells via p21 CIP1 and p27 KIP1 regulation. Mol. Endocrinol. 2009, 23:1827-1838.
21. Alles N., Soysa N.S., Hayashi J., et al. Suppression of NF-κB increases bone formation and ameliorates osteopenia in ovariectomized mice. Endocrinology 2010, 151:4626-4634.