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Volumn 187, Issue 5, 2009, Pages 669-683

The glycosaminoglycan-binding domain of PRELP acts as a cell type-specific NF-κB inhibitor that impairs osteoclastogenesis

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; BINDING PROTEIN; CHONDROITIN SULFATE; GLYCOSAMINOGLYCAN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LIPOCORTIN 2; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN PRELP; UNCLASSIFIED DRUG; GLYCOPROTEIN; MEMBRANE PROTEIN; PRELP PROTEIN, MOUSE; PROTEOGLYCAN; SCLEROPROTEIN;

EID: 74049094448     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200906014     Document Type: Article
Times cited : (67)

References (41)
  • 1
    • 0033231406 scopus 로고    scopus 로고
    • Internalization of the hyaluronan receptor CD44 by chondrocytes
    • doi:10.1006/excr.1999.4641
    • Aguiar, D.J., W. Knudson, and C.B. Knudson. 1999. Internalization of the hyaluronan receptor CD44 by chondrocytes. Exp. Cell Res. 252:292-302. doi:10.1006/excr.1999.4641
    • (1999) Exp. Cell Res , vol.252 , pp. 292-302
    • Aguiar, D.J.1    Knudson, W.2    Knudson, C.B.3
  • 3
    • 76149099342 scopus 로고    scopus 로고
    • Bengtsson, E. 1999. Structure and interactions of the extracellular matrix protein PRELP. PhD thesis. Lund University, S-221 00 Lund, Sweden. 163 pp.
    • Bengtsson, E. 1999. Structure and interactions of the extracellular matrix protein PRELP. PhD thesis. Lund University, S-221 00 Lund, Sweden. 163 pp.
  • 4
    • 0028892460 scopus 로고
    • The primary structure of a basic leucine-rich repeat protein, PRELP, found in connective tissues
    • doi:10.1074/jbc .270.43.25639
    • Bengtsson, E., P.J. Neame, D. Heinegård, and Y. Sommarin. 1995. The primary structure of a basic leucine-rich repeat protein, PRELP, found in connective tissues. J. Biol. Chem. 270:25639-25644. doi:10.1074/jbc .270.43.25639
    • (1995) J. Biol. Chem , vol.270 , pp. 25639-25644
    • Bengtsson, E.1    Neame, P.J.2    Heinegård, D.3    Sommarin, Y.4
  • 5
    • 0034731438 scopus 로고    scopus 로고
    • The amino-terminal part of PRELP binds to heparin and heparan sulfate
    • doi:10.1074/jbc.M007917200
    • Bengtsson, E., A. Aspberg, D. Heinegård, Y. Sommarin, and D. Spillmann. 2000. The amino-terminal part of PRELP binds to heparin and heparan sulfate. J. Biol. Chem. 275:40695-40702. doi:10.1074/jbc.M007917200
    • (2000) J. Biol. Chem , vol.275 , pp. 40695-40702
    • Bengtsson, E.1    Aspberg, A.2    Heinegård, D.3    Sommarin, Y.4    Spillmann, D.5
  • 6
    • 0037177893 scopus 로고    scopus 로고
    • The leucine-rich repeat protein PRELP binds perlecan and collagens and may function as a basement membrane anchor
    • doi:10.1074/jbc.M108285200
    • Bengtsson, E., M. Mörgelin, T. Sasaki, R. Timpl, D. Heinegård, and A. Aspberg. 2002. The leucine-rich repeat protein PRELP binds perlecan and collagens and may function as a basement membrane anchor. J. Biol. Chem. 277:15061-15068. doi:10.1074/jbc.M108285200
    • (2002) J. Biol. Chem , vol.277 , pp. 15061-15068
    • Bengtsson, E.1    Mörgelin, M.2    Sasaki, T.3    Timpl, R.4    Heinegård, D.5    Aspberg, A.6
  • 7
    • 0032759871 scopus 로고    scopus 로고
    • Stromelysin (MMP-3) synthesis is up-regulated in estrogen-deficient mouse osteoblasts in vivo and in vitro
    • doi:10.1359/jbmr.1999.14.11.1880
    • Breckon, J.J., S. Papaioannou, L.W. Kon, A. Tumber, R.M. Hembry, G. Murphy, J.J. Reynolds, and M.C. Meikle. 1999. Stromelysin (MMP-3) synthesis is up-regulated in estrogen-deficient mouse osteoblasts in vivo and in vitro. J. Bone Miner. Res. 14:1880-1890. doi:10.1359/jbmr.1999.14.11.1880
    • (1999) J. Bone Miner. Res , vol.14 , pp. 1880-1890
    • Breckon, J.J.1    Papaioannou, S.2    Kon, L.W.3    Tumber, A.4    Hembry, R.M.5    Murphy, G.6    Reynolds, J.J.7    Meikle, M.C.8
  • 9
    • 4444347398 scopus 로고    scopus 로고
    • Chondroitin sulfate chains on syndecan-1 and syndecan-4 from normal murine mammary gland epithelial cells are structurally and functionally distinct and cooperate with heparan sulfate chains to bind growth factors. A novel function to control binding of midkine, pleiotrophin, and basic fibroblast growth factor
    • doi:10.1074/ jbc.M403031200
    • Deepa, S.S., S. Yamada, M. Zako, O. Goldberger, and K. Sugahara. 2004. Chondroitin sulfate chains on syndecan-1 and syndecan-4 from normal murine mammary gland epithelial cells are structurally and functionally distinct and cooperate with heparan sulfate chains to bind growth factors. A novel function to control binding of midkine, pleiotrophin, and basic fibroblast growth factor. J. Biol. Chem. 279:37368-37376. doi:10.1074/ jbc.M403031200
    • (2004) J. Biol. Chem , vol.279 , pp. 37368-37376
    • Deepa, S.S.1    Yamada, S.2    Zako, M.3    Goldberger, O.4    Sugahara, K.5
  • 10
    • 65549133368 scopus 로고    scopus 로고
    • Delivery of macromolecules using arginine-rich cell-penetrating peptides: Ways to overcome endosomal entrapment
    • doi:10.1208/s12248-008-9071-2
    • El-Sayed, A., S. Futaki, and H. Harashima. 2009. Delivery of macromolecules using arginine-rich cell-penetrating peptides: ways to overcome endosomal entrapment. AAPS J. 11:13-22. doi:10.1208/s12248-008-9071-2
    • (2009) AAPS J , vol.11 , pp. 13-22
    • El-Sayed, A.1    Futaki, S.2    Harashima, H.3
  • 12
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery
    • doi:10.1074/jbc.M007540200
    • Futaki, S., T. Suzuki, W. Ohashi, T. Yagami, S. Tanaka, K. Ueda, and Y. Sugiura. 2001. Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J. Biol. Chem. 276:5836-5840. doi:10.1074/jbc.M007540200
    • (2001) J. Biol. Chem , vol.276 , pp. 5836-5840
    • Futaki, S.1    Suzuki, T.2    Ohashi, W.3    Yagami, T.4    Tanaka, S.5    Ueda, K.6    Sugiura, Y.7
  • 13
    • 0037172801 scopus 로고    scopus 로고
    • Translocation of branched-chain arginine peptides through cell membranes: Flexibility in the spatial disposition of positive charges in membrane-permeable peptides
    • doi:10.1021/bi0256173
    • Futaki, S., I. Nakase, T. Suzuki, Z. Youjun, and Y. Sugiura. 2002. Translocation of branched-chain arginine peptides through cell membranes: flexibility in the spatial disposition of positive charges in membrane-permeable peptides. Biochemistry. 41:7925-7930. doi:10.1021/bi0256173
    • (2002) Biochemistry , vol.41 , pp. 7925-7930
    • Futaki, S.1    Nakase, I.2    Suzuki, T.3    Youjun, Z.4    Sugiura, Y.5
  • 14
    • 34548183102 scopus 로고    scopus 로고
    • Argininerich peptides and their internalization mechanisms
    • doi:10.1042/BST0350784
    • Futaki, S., I. Nakase, A. Tadokoro, T. Takeuchi, and A.T. Jones. 2007. Argininerich peptides and their internalization mechanisms. Biochem. Soc. Trans. 35:784-787. doi:10.1042/BST0350784
    • (2007) Biochem. Soc. Trans , vol.35 , pp. 784-787
    • Futaki, S.1    Nakase, I.2    Tadokoro, A.3    Takeuchi, T.4    Jones, A.T.5
  • 15
    • 20344369564 scopus 로고    scopus 로고
    • Annexins: Linking Ca2+ signalling to membrane dynamics
    • doi:10.1038/ nrm1661
    • Gerke, V., C.E. Creutz, and S.E. Moss. 2005. Annexins: linking Ca2+ signalling to membrane dynamics. Nat. Rev. Mol. Cell Biol. 6:449-461. doi:10.1038/ nrm1661
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 449-461
    • Gerke, V.1    Creutz, C.E.2    Moss, S.E.3
  • 16
    • 33846612392 scopus 로고    scopus 로고
    • The consequence of PRELP overexpression on skin
    • doi:10.1016/j.matbio.2006.10.005
    • Grover, J., E.R. Lee, L.C. Mounkes, C.L. Stewart, and P.J. Roughley. 2007. The consequence of PRELP overexpression on skin. Matrix Biol. 26:140-143. doi:10.1016/j.matbio.2006.10.005
    • (2007) Matrix Biol , vol.26 , pp. 140-143
    • Grover, J.1    Lee, E.R.2    Mounkes, L.C.3    Stewart, C.L.4    Roughley, P.J.5
  • 17
    • 0030899412 scopus 로고    scopus 로고
    • Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol
    • Harder, T., R. Kellner, R.G. Parton, and J. Gruenberg. 1997. Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol. Mol. Biol. Cell. 8:533-545.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 533-545
    • Harder, T.1    Kellner, R.2    Parton, R.G.3    Gruenberg, J.4
  • 19
    • 33845269544 scopus 로고    scopus 로고
    • Hutchinson-Gilford progeria syndrome: Review of the phenotype
    • Hennekam, R.C. 2006. Hutchinson-Gilford progeria syndrome: review of the phenotype. Am. J. Med. Genet. A. 140:2603-2624.
    • (2006) Am. J. Med. Genet. A , vol.140 , pp. 2603-2624
    • Hennekam, R.C.1
  • 20
    • 54349124546 scopus 로고    scopus 로고
    • Regulation of bone mass, osteoclast function, and ovariectomy-induced bone loss by the type 2 cannabinoid receptor
    • doi:10.1210/en.2008-0150
    • Idris, A.I., A. Sophocleous, E. Landao-Bassonga, R.J. van't Hof, and S.H. Ralston. 2008. Regulation of bone mass, osteoclast function, and ovariectomy-induced bone loss by the type 2 cannabinoid receptor. Endocrinology. 149:5619-5626. doi:10.1210/en.2008-0150
    • (2008) Endocrinology , vol.149 , pp. 5619-5626
    • Idris, A.I.1    Sophocleous, A.2    Landao-Bassonga, E.3    van't Hof, R.J.4    Ralston, S.H.5
  • 21
    • 0030010512 scopus 로고    scopus 로고
    • Proteoglycans of the extracellular environment: Clues from the gene and protein side offer novel perspectives in molecular diversity and function
    • Iozzo, R.V., and A.D. Murdoch. 1996. Proteoglycans of the extracellular environment: clues from the gene and protein side offer novel perspectives in molecular diversity and function. FASEB J. 10:598-614.
    • (1996) FASEB J , vol.10 , pp. 598-614
    • Iozzo, R.V.1    Murdoch, A.D.2
  • 22
    • 0037155805 scopus 로고    scopus 로고
    • A requirement for the CD44 cytoplasmic domain for hyaluronan binding, pericellular matrix assembly, and receptor-mediated endocytosis in COS-7 cells
    • doi:10.1074/jbc .M108654200
    • Jiang, H., R.S. Peterson, W. Wang, E. Bartnik, C.B. Knudson, and W. Knudson. 2002. A requirement for the CD44 cytoplasmic domain for hyaluronan binding, pericellular matrix assembly, and receptor-mediated endocytosis in COS-7 cells. J. Biol. Chem. 277:10531-10538. doi:10.1074/jbc .M108654200
    • (2002) J. Biol. Chem , vol.277 , pp. 10531-10538
    • Jiang, H.1    Peterson, R.S.2    Wang, W.3    Bartnik, E.4    Knudson, C.B.5    Knudson, W.6
  • 23
    • 0030737922 scopus 로고    scopus 로고
    • CD44 antibodies inhibit osteoclast formation
    • doi:10.1359/ jbmr.1997.12.8.1155
    • Kania, J.R., T. Kehat-Stadler, and S.R. Kupfer. 1997. CD44 antibodies inhibit osteoclast formation. J. Bone Miner. Res. 12:1155-1164. doi:10.1359/ jbmr.1997.12.8.1155
    • (1997) J. Bone Miner. Res , vol.12 , pp. 1155-1164
    • Kania, J.R.1    Kehat-Stadler, T.2    Kupfer, S.R.3
  • 24
    • 41149156893 scopus 로고    scopus 로고
    • Cellular internalization and distribution of arginine-rich peptides as a function of extracellular peptide concentration, serum, and plasma membrane associated proteoglycans
    • doi:10.1021/bc700289w
    • Kosuge, M., T. Takeuchi, I. Nakase, A.T. Jones, and S. Futaki. 2008. Cellular internalization and distribution of arginine-rich peptides as a function of extracellular peptide concentration, serum, and plasma membrane associated proteoglycans. Bioconjug. Chem. 19:656-664. doi:10.1021/bc700289w
    • (2008) Bioconjug. Chem , vol.19 , pp. 656-664
    • Kosuge, M.1    Takeuchi, T.2    Nakase, I.3    Jones, A.T.4    Futaki, S.5
  • 25
    • 0345689603 scopus 로고    scopus 로고
    • PRELP, collagen, and a theory of Hutchinson-Gilford progeria
    • doi:10.1016/S1568-1637(02)00044-2
    • Lewis, M. 2003. PRELP, collagen, and a theory of Hutchinson-Gilford progeria. Ageing Res. Rev. 2:95-105. doi:10.1016/S1568-1637(02)00044-2
    • (2003) Ageing Res. Rev , vol.2 , pp. 95-105
    • Lewis, M.1
  • 26
    • 0037047275 scopus 로고    scopus 로고
    • Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate
    • doi:10.1074/jbc .M204004200
    • Li, Z., W.S. Hou, C.R. Escalante-Torres, B.D. Gelb, and D. Bromme. 2002. Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate. J. Biol. Chem. 277:28669-28676. doi:10.1074/jbc .M204004200
    • (2002) J. Biol. Chem , vol.277 , pp. 28669-28676
    • Li, Z.1    Hou, W.S.2    Escalante-Torres, C.R.3    Gelb, B.D.4    Bromme, D.5
  • 27
    • 16644370637 scopus 로고    scopus 로고
    • Effects of 17 beta-estradiol on the expression of interstitial collagenases-8 and -13 (MMP-8 and MMP-13) and tissue inhibitor of metalloproteinase-1 (TIMP-1) in ovariectomized rat osteoblastic cells
    • doi:10.1007/s10735-004-6206-3
    • Li, J., E.Y. Liao, R.C. Dai, Q.Y. Wei, and X.H. Luo. 2004. Effects of 17 beta-estradiol on the expression of interstitial collagenases-8 and -13 (MMP-8 and MMP-13) and tissue inhibitor of metalloproteinase-1 (TIMP-1) in ovariectomized rat osteoblastic cells. J. Mol. Histol. 35:723-731. doi:10.1007/s10735-004-6206-3
    • (2004) J. Mol. Histol , vol.35 , pp. 723-731
    • Li, J.1    Liao, E.Y.2    Dai, R.C.3    Wei, Q.Y.4    Luo, X.H.5
  • 29
    • 39149123550 scopus 로고    scopus 로고
    • Immortalized mouse articular cartilage cell lines retain chondrocyte phenotype and respond to both anabolic factor BMP-2 and pro-inflammatory factor IL-1
    • doi:10.1002/jcp.21282
    • Majumdar, M.K., P.S. Chockalingam, R.A. Bhat, R. Sheldon, C. Keohan, T. Blanchet, S. Glasson, and E.A. Morris. 2008. Immortalized mouse articular cartilage cell lines retain chondrocyte phenotype and respond to both anabolic factor BMP-2 and pro-inflammatory factor IL-1. J. Cell. Physiol. 215:68-76. doi:10.1002/jcp.21282
    • (2008) J. Cell. Physiol , vol.215 , pp. 68-76
    • Majumdar, M.K.1    Chockalingam, P.S.2    Bhat, R.A.3    Sheldon, R.4    Keohan, C.5    Blanchet, T.6    Glasson, S.7    Morris, E.A.8
  • 31
    • 0032746024 scopus 로고    scopus 로고
    • Annexin II increases osteoclast formation by stimulating the proliferation of osteoclast precursors in human marrow cultures
    • doi:10.1172/JCI6374
    • Menaa, C., R.D. Devlin, S.V. Reddy, Y. Gazitt, S.J. Choi, and G.D. Roodman. 1999. Annexin II increases osteoclast formation by stimulating the proliferation of osteoclast precursors in human marrow cultures. J. Clin. Invest. 103:1605-1613. doi:10.1172/JCI6374
    • (1999) J. Clin. Invest , vol.103 , pp. 1605-1613
    • Menaa, C.1    Devlin, R.D.2    Reddy, S.V.3    Gazitt, Y.4    Choi, S.J.5    Roodman, G.D.6
  • 32
    • 0942278947 scopus 로고    scopus 로고
    • Immunolocalization of matrix metalloproteinase-13 on bone surface under osteoclasts in rat tibia
    • doi:10.1016/j.bone.2003.09.001
    • Nakamura, H., G. Sato, A. Hirata, and T. Yamamoto. 2004. Immunolocalization of matrix metalloproteinase-13 on bone surface under osteoclasts in rat tibia. Bone. 34:48-56. doi:10.1016/j.bone.2003.09.001
    • (2004) Bone , vol.34 , pp. 48-56
    • Nakamura, H.1    Sato, G.2    Hirata, A.3    Yamamoto, T.4
  • 33
    • 4043110719 scopus 로고    scopus 로고
    • Induction of RANKL expression and osteoclast maturation by the binding of fibroblast growth factor 2 to heparan sulfate proteoglycan on rheumatoid synovial fibroblasts
    • doi:10.1002/art.20367
    • Nakano, K., Y. Okada, K. Saito, and Y. Tanaka. 2004. Induction of RANKL expression and osteoclast maturation by the binding of fibroblast growth factor 2 to heparan sulfate proteoglycan on rheumatoid synovial fibroblasts. Arthritis Rheum. 50:2450-2458. doi:10.1002/art.20367
    • (2004) Arthritis Rheum , vol.50 , pp. 2450-2458
    • Nakano, K.1    Okada, Y.2    Saito, K.3    Tanaka, Y.4
  • 34
    • 33846223900 scopus 로고    scopus 로고
    • Interaction of arginine-rich peptides with membrane-associated proteoglycans is crucial for induction of actin organization and macropinocytosis
    • doi:10.1021/bi0612824
    • Nakase, I., A. Tadokoro, N. Kawabata, T. Takeuchi, H. Katoh, K. Hiramoto, M. Negishi, M. Nomizu, Y. Sugiura, and S. Futaki. 2007. Interaction of arginine-rich peptides with membrane-associated proteoglycans is crucial for induction of actin organization and macropinocytosis. Biochemistry. 46:492-501. doi:10.1021/bi0612824
    • (2007) Biochemistry , vol.46 , pp. 492-501
    • Nakase, I.1    Tadokoro, A.2    Kawabata, N.3    Takeuchi, T.4    Katoh, H.5    Hiramoto, K.6    Negishi, M.7    Nomizu, M.8    Sugiura, Y.9    Futaki, S.10
  • 35
    • 38949188925 scopus 로고    scopus 로고
    • Methodological and cellular aspects that govern the internalization mechanisms of arginine-rich cell-penetrating peptides
    • doi:10.1016/ j.addr.2007.10.006
    • Nakase, I., T. Takeuchi, G. Tanaka, and S. Futaki. 2008. Methodological and cellular aspects that govern the internalization mechanisms of arginine-rich cell-penetrating peptides. Adv. Drug Deliv. Rev. 60:598-607. doi:10.1016/ j.addr.2007.10.006
    • (2008) Adv. Drug Deliv. Rev , vol.60 , pp. 598-607
    • Nakase, I.1    Takeuchi, T.2    Tanaka, G.3    Futaki, S.4
  • 36
    • 0023488581 scopus 로고
    • Bone histomorphometry: Standardization of nomenclature, symbols, and units. Report of the ASBMR Histomorphometry Nomenclature Committee
    • Parfitt, A.M., M.K. Drezner, F.H. Glorieux, J.A. Kanis, H. Malluche, P.J. Meunier, S.M. Ott, and R.R. Recker. 1987. Bone histomorphometry: standardization of nomenclature, symbols, and units. Report of the ASBMR Histomorphometry Nomenclature Committee. J. Bone Miner. Res. 2:595-610.
    • (1987) J. Bone Miner. Res , vol.2 , pp. 595-610
    • Parfitt, A.M.1    Drezner, M.K.2    Glorieux, F.H.3    Kanis, J.A.4    Malluche, H.5    Meunier, P.J.6    Ott, S.M.7    Recker, R.R.8
  • 37
    • 0034695439 scopus 로고    scopus 로고
    • Identification in vitreous and molecular cloning of opticin, a novel member of the family of leucine-rich repeat proteins of the extracellular matrix
    • doi:10.1074/jbc.275.3.2123
    • Reardon, A.J., M. Le Goff, M.D. Briggs, D. McLeod, J.K. Sheehan, D.J. Thornton, and P.N. Bishop. 2000. Identification in vitreous and molecular cloning of opticin, a novel member of the family of leucine-rich repeat proteins of the extracellular matrix. J. Biol. Chem. 275:2123-2129. doi:10.1074/jbc.275.3.2123
    • (2000) J. Biol. Chem , vol.275 , pp. 2123-2129
    • Reardon, A.J.1    Le Goff, M.2    Briggs, M.D.3    McLeod, D.4    Sheehan, J.K.5    Thornton, D.J.6    Bishop, P.N.7
  • 38
    • 0032476653 scopus 로고    scopus 로고
    • CD44 occupancy prevents macrophage multinucleation
    • doi:10.1083/ jcb.143.3.837
    • Sterling, H., C. Saginario, and A. Vignery. 1998. CD44 occupancy prevents macrophage multinucleation. J. Cell Biol. 143:837-847. doi:10.1083/ jcb.143.3.837
    • (1998) J. Cell Biol , vol.143 , pp. 837-847
    • Sterling, H.1    Saginario, C.2    Vignery, A.3
  • 39
    • 0035992868 scopus 로고    scopus 로고
    • Colocalization of intracellular osteopontin with CD44 is associated with migration, cell fusion, and resorption in osteoclasts
    • doi:10.1359/jbmr.2002.17.8.1486
    • Suzuki, K., B. Zhu, S.R. Rittling, D.T. Denhardt, H.A. Goldberg, C.A. McCulloch, and J. Sodek. 2002. Colocalization of intracellular osteopontin with CD44 is associated with migration, cell fusion, and resorption in osteoclasts. J. Bone Miner. Res. 17:1486-1497. doi:10.1359/jbmr.2002.17.8.1486
    • (2002) J. Bone Miner. Res , vol.17 , pp. 1486-1497
    • Suzuki, K.1    Zhu, B.2    Rittling, S.R.3    Denhardt, D.T.4    Goldberg, H.A.5    McCulloch, C.A.6    Sodek, J.7
  • 40
    • 0043267732 scopus 로고    scopus 로고
    • Genetic regulation of osteoclast development and function
    • doi:10.1038/nrg1122
    • Teitelbaum, S.L., and F.P. Ross. 2003. Genetic regulation of osteoclast development and function. Nat. Rev. Genet. 4:638-649. doi:10.1038/nrg1122
    • (2003) Nat. Rev. Genet , vol.4 , pp. 638-649
    • Teitelbaum, S.L.1    Ross, F.P.2
  • 41
    • 21644471962 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors modulate metalloproteinase gene expression in chondrocytes and block cartilage resorption
    • doi:10.1186/ar1702
    • Young, D.A., R.L. Lakey, C.J. Pennington, D. Jones, L. Kevorkian, D.R. Edwards, T.E. Cawston, and I.M. Clark. 2005. Histone deacetylase inhibitors modulate metalloproteinase gene expression in chondrocytes and block cartilage resorption. Arthritis Res. Ther. 7:R503-R512. doi:10.1186/ar1702
    • (2005) Arthritis Res. Ther , vol.7
    • Young, D.A.1    Lakey, R.L.2    Pennington, C.J.3    Jones, D.4    Kevorkian, L.5    Edwards, D.R.6    Cawston, T.E.7    Clark, I.M.8


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