메뉴 건너뛰기




Volumn 58, Issue 1, 2008, Pages 209-220

Sphingomyelinase decreases type II collagen expression in bovine articular cartilage chondrocytes via the ERK signaling pathway

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; CERAMIDE; COLLAGEN TYPE 2; CYTOKINE; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEIN C FOS; RAF PROTEIN; SPHINGOMYELIN PHOSPHODIESTERASE; TRANSCRIPTION FACTOR SOX9;

EID: 38149114635     PISSN: 00043591     EISSN: None     Source Type: Journal    
DOI: 10.1002/art.23172     Document Type: Article
Times cited : (13)

References (50)
  • 1
    • 0032990777 scopus 로고    scopus 로고
    • The role of cytokines as inflammatory mediators in osteoarthritis: Lessons from animal models [review]
    • Goldring MB. The role of cytokines as inflammatory mediators in osteoarthritis: lessons from animal models [review]. Connect Tissue Res 1999;40:1-11.
    • (1999) Connect Tissue Res , vol.40 , pp. 1-11
    • Goldring, M.B.1
  • 2
    • 0034882639 scopus 로고    scopus 로고
    • Ceramide regulates cellular homeostasis via diverse stress signaling pathways [review]
    • Ruvolo PP. Ceramide regulates cellular homeostasis via diverse stress signaling pathways [review]. Leukemia 2001;15:1153-60.
    • (2001) Leukemia , vol.15 , pp. 1153-1160
    • Ruvolo, P.P.1
  • 3
    • 85182482269 scopus 로고    scopus 로고
    • Does protein kinase R mediate TNF-α- and ceramide-induced increases in expression and activation of matrix metalloproteinases in articular cartilage by a novel mechanism?
    • Gilbert SJ, Duance VC, Mason DJ. Does protein kinase R mediate TNF-α- and ceramide-induced increases in expression and activation of matrix metalloproteinases in articular cartilage by a novel mechanism? Arthritis Res Ther 2004;6:R46-55.
    • (2004) Arthritis Res Ther , vol.6
    • Gilbert, S.J.1    Duance, V.C.2    Mason, D.J.3
  • 4
    • 0034614352 scopus 로고    scopus 로고
    • Effects of ceramide on apoptosis, proteoglycan degradation, and matrix metalloproteinase expression in rabbit articular cartilage
    • Sabatini M, Rolland G, Leonce S, Thomas M, Lesur C, Perez V, et al. Effects of ceramide on apoptosis, proteoglycan degradation, and matrix metalloproteinase expression in rabbit articular cartilage. Biochem Biophys Res Commun 2000;267:438-44.
    • (2000) Biochem Biophys Res Commun , vol.267 , pp. 438-444
    • Sabatini, M.1    Rolland, G.2    Leonce, S.3    Thomas, M.4    Lesur, C.5    Perez, V.6
  • 6
    • 34247551025 scopus 로고    scopus 로고
    • Exogenous sphingomyelinase increases collagen and sulphated glycosaminoglycan production by primary articular chondrocytes: An in vitro study
    • Gilbert SJ, Blain EJ, Jones P, Duance VC, Mason D. Exogenous sphingomyelinase increases collagen and sulphated glycosaminoglycan production by primary articular chondrocytes: an in vitro study. Arthritis Res Ther 2006;8:R89-100.
    • (2006) Arthritis Res Ther , vol.8
    • Gilbert, S.J.1    Blain, E.J.2    Jones, P.3    Duance, V.C.4    Mason, D.5
  • 8
    • 33644880217 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate/sphingosine 1-phosphate receptor 1 signaling in rheumatoid synovium: Regulation of synovial proliferation and inflammatory gene expression
    • Kitano M, Hla T, Sekiguchi M, Kawahito Y, Yoshimura R, Miyazawa K, et al. Sphingosine 1-phosphate/sphingosine 1-phosphate receptor 1 signaling in rheumatoid synovium: regulation of synovial proliferation and inflammatory gene expression. Arthritis Rheum 2006;54:742-53.
    • (2006) Arthritis Rheum , vol.54 , pp. 742-753
    • Kitano, M.1    Hla, T.2    Sekiguchi, M.3    Kawahito, Y.4    Yoshimura, R.5    Miyazawa, K.6
  • 10
    • 0033985056 scopus 로고    scopus 로고
    • Involvement of caspase-3 and GD3 ganglioside in ceramide-induced apoptosis in Farber disease
    • Farina F, Cappello F, Todaro M, Bucchieri F, Peri G, Zummo G, et al. Involvement of caspase-3 and GD3 ganglioside in ceramide-induced apoptosis in Farber disease. J Histochem Cytochem 2000;48:57-62.
    • (2000) J Histochem Cytochem , vol.48 , pp. 57-62
    • Farina, F.1    Cappello, F.2    Todaro, M.3    Bucchieri, F.4    Peri, G.5    Zummo, G.6
  • 11
    • 0028108015 scopus 로고
    • Functional dichotomy of neutral and acidic sphingomyelinases in tumor necrosis factor signaling
    • Wiegmann K, Schutze S, Machleidt T, Witte D, Kronke M. Functional dichotomy of neutral and acidic sphingomyelinases in tumor necrosis factor signaling. Cell 1994;78:1005-15.
    • (1994) Cell , vol.78 , pp. 1005-1015
    • Wiegmann, K.1    Schutze, S.2    Machleidt, T.3    Witte, D.4    Kronke, M.5
  • 12
    • 0027488403 scopus 로고
    • Ceramide: A novel second messenger
    • Mathias S, Kolesnick R. Ceramide: a novel second messenger. Adv Lipid Res 1993;25:65-90.
    • (1993) Adv Lipid Res , vol.25 , pp. 65-90
    • Mathias, S.1    Kolesnick, R.2
  • 13
    • 0030595340 scopus 로고    scopus 로고
    • FAN, a novel WD-repeat protein, couples the p55 TNF-receptor to neutral sphingomyelinase
    • Adam-Klages S, Adam D, Wiegmann K, Struve S, Kolanus W, Schneider-Mergener J, et al. FAN, a novel WD-repeat protein, couples the p55 TNF-receptor to neutral sphingomyelinase. Cell 1996;86:937-47.
    • (1996) Cell , vol.86 , pp. 937-947
    • Adam-Klages, S.1    Adam, D.2    Wiegmann, K.3    Struve, S.4    Kolanus, W.5    Schneider-Mergener, J.6
  • 14
    • 0032568836 scopus 로고    scopus 로고
    • Involvement of de novo ceramide biosynthesis in tumor necrosis factor-α/cycloheximide- induced cerebral endothelial cell death
    • Xu J, Yeh CH, Chen S, He L, Sensi SL, Canzoniero LM, et al. Involvement of de novo ceramide biosynthesis in tumor necrosis factor-α/cycloheximide- induced cerebral endothelial cell death. J Biol Chem 1998;273:16521-6.
    • (1998) J Biol Chem , vol.273 , pp. 16521-16526
    • Xu, J.1    Yeh, C.H.2    Chen, S.3    He, L.4    Sensi, S.L.5    Canzoniero, L.M.6
  • 15
    • 0033974782 scopus 로고    scopus 로고
    • Ceramide in the eukaryotic stress response
    • Hannun YA, Luberto C. Ceramide in the eukaryotic stress response. Trends Cell Biol 2000;10:73-80.
    • (2000) Trends Cell Biol , vol.10 , pp. 73-80
    • Hannun, Y.A.1    Luberto, C.2
  • 16
    • 0037189940 scopus 로고    scopus 로고
    • Divergent role of ceramide generated by exogenous sphingomy-elinases on NF-κB activation and apoptosis in human colon HT-29 cells
    • Colell A, Coll O, Mari M, Fernandez-Checa JC, Garcia-Ruiz C. Divergent role of ceramide generated by exogenous sphingomy-elinases on NF-κB activation and apoptosis in human colon HT-29 cells. FEBS Lett 2002;526:15-20.
    • (2002) FEBS Lett , vol.526 , pp. 15-20
    • Colell, A.1    Coll, O.2    Mari, M.3    Fernandez-Checa, J.C.4    Garcia-Ruiz, C.5
  • 17
    • 0026458406 scopus 로고
    • TNF activates NF-κB by phosphatidylcholine-specific phospholipase C-induced "acidic" sphingomyelin breakdown
    • Schutze S, Potthoff K, Machleidt T, Berkovic D, Wiegmann K, Kronke M. TNF activates NF-κB by phosphatidylcholine-specific phospholipase C-induced "acidic" sphingomyelin breakdown. Cell 1992;71:765-76.
    • (1992) Cell , vol.71 , pp. 765-776
    • Schutze, S.1    Potthoff, K.2    Machleidt, T.3    Berkovic, D.4    Wiegmann, K.5    Kronke, M.6
  • 18
    • 0040885889 scopus 로고    scopus 로고
    • Regulation of Raf-1 kinase by TNF via its second messenger ceramide and cross-talk with mitogenic signalling
    • Muller G, Storz P, Bourteele S, Doppler H, Pfizenmaier K, Mischak H, et al. Regulation of Raf-1 kinase by TNF via its second messenger ceramide and cross-talk with mitogenic signalling. EMBO J 1998;17:732-42.
    • (1998) EMBO J , vol.17 , pp. 732-742
    • Muller, G.1    Storz, P.2    Bourteele, S.3    Doppler, H.4    Pfizenmaier, K.5    Mischak, H.6
  • 20
    • 2942696322 scopus 로고    scopus 로고
    • Differential binding of ceramide to MEKK1 in glomerular endothelial and mesangial cells
    • Huwiler A, Xin C, Brust AK, Briner VA, Pfeilschifter J. Differential binding of ceramide to MEKK1 in glomerular endothelial and mesangial cells. Biochim Biophys Acta 2004;1636:159-68.
    • (2004) Biochim Biophys Acta , vol.1636 , pp. 159-168
    • Huwiler, A.1    Xin, C.2    Brust, A.K.3    Briner, V.A.4    Pfeilschifter, J.5
  • 21
    • 0034948731 scopus 로고    scopus 로고
    • Ceramide-induced apoptosis in cortical neurons is mediated by an increase in p38 phosphorylation and not by the decrease in ERK phosphorylation
    • Willaime S, Vanhoutte P, Caboche J, Lemaigre-Dubreuil Y, Mariani J, Brugg B. Ceramide-induced apoptosis in cortical neurons is mediated by an increase in p38 phosphorylation and not by the decrease in ERK phosphorylation. Eur J Neurosci 2001;13: 2037-46.
    • (2001) Eur J Neurosci , vol.13 , pp. 2037-2046
    • Willaime, S.1    Vanhoutte, P.2    Caboche, J.3    Lemaigre-Dubreuil, Y.4    Mariani, J.5    Brugg, B.6
  • 22
    • 33751539325 scopus 로고    scopus 로고
    • Ceramide inhibition of chondrocyte proliferation and bone growth is IGF-I independent
    • MacRae VE, Burdon T, Ahmed SF, Farquharson C. Ceramide inhibition of chondrocyte proliferation and bone growth is IGF-I independent. J Endocrinol 2006;191:369-77.
    • (2006) J Endocrinol , vol.191 , pp. 369-377
    • MacRae, V.E.1    Burdon, T.2    Ahmed, S.F.3    Farquharson, C.4
  • 24
    • 27444433461 scopus 로고    scopus 로고
    • Ceramide- and ERK-dependent pathway for the activation of CCAAT/enhancer binding protein by interleukin-1β in hepatocytes
    • Giltiay NV, Karakashian AA, Alimov AP, Ligthlc S, Nikolova-Karakashian MN. Ceramide- and ERK-dependent pathway for the activation of CCAAT/enhancer binding protein by interleukin-1β in hepatocytes. J Lipid Res 2005;46:2497-505.
    • (2005) J Lipid Res , vol.46 , pp. 2497-2505
    • Giltiay, N.V.1    Karakashian, A.A.2    Alimov, A.P.3    Ligthlc, S.4    Nikolova-Karakashian, M.N.5
  • 25
    • 0035965998 scopus 로고    scopus 로고
    • Tumor necrosis factor-α supports the survival of osteoclasts through the activation of Akt and ERK
    • Lee SE, Chung WJ, Kwak HB, Chung CH, Kwack KB, Lee ZH, et al. Tumor necrosis factor-α supports the survival of osteoclasts through the activation of Akt and ERK. J Biol Chem 2001;276: 49343-9.
    • (2001) J Biol Chem , vol.276 , pp. 49343-49349
    • Lee, S.E.1    Chung, W.J.2    Kwak, H.B.3    Chung, C.H.4    Kwack, K.B.5    Lee, Z.H.6
  • 26
    • 1942536250 scopus 로고    scopus 로고
    • Signaling mechanisms in tumor necrosis factor α-induced death of microvascular endothelial cells of the corpus luteum
    • Pru JK, Lynch MP, Davis JS, Rueda BR. Signaling mechanisms in tumor necrosis factor α-induced death of microvascular endothelial cells of the corpus luteum. Reprod Biol Endocrinol 2003;1:17.
    • (2003) Reprod Biol Endocrinol , vol.1 , pp. 17
    • Pru, J.K.1    Lynch, M.P.2    Davis, J.S.3    Rueda, B.R.4
  • 27
    • 33745487524 scopus 로고    scopus 로고
    • Role of mitogen-activated protein kinases and NFκB on IL-1β-induced effects on collagen type II, MMP-1 and 13 mRNA expression in normal articular human chondrocytes
    • Fan Z, Yang H, Bau B, Soder S, Aigner T. Role of mitogen-activated protein kinases and NFκB on IL-1β-induced effects on collagen type II, MMP-1 and 13 mRNA expression in normal articular human chondrocytes. Rheumatol Int 2006;26:900-3.
    • (2006) Rheumatol Int , vol.26 , pp. 900-903
    • Fan, Z.1    Yang, H.2    Bau, B.3    Soder, S.4    Aigner, T.5
  • 28
    • 0344374450 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase signaling in bovine articular chondrocytes in response to fluid flow does not require calcium mobilization
    • Hung CT, Henshaw DR, Wang CC, Mauck RL, Raia F, Palmer G, et al. Mitogen-activated protein kinase signaling in bovine articular chondrocytes in response to fluid flow does not require calcium mobilization. J Biomech 2000;33:73-80.
    • (2000) J Biomech , vol.33 , pp. 73-80
    • Hung, C.T.1    Henshaw, D.R.2    Wang, C.C.3    Mauck, R.L.4    Raia, F.5    Palmer, G.6
  • 29
    • 33750322263 scopus 로고    scopus 로고
    • The MAPK scaffold kinase suppressor of Ras is involved in ERK activation by stress and proinflammatory cytokines and induction of arthritis
    • Fusello AM, Mandik-Nayak L, Shih F, Lewis RE, Allen PM, Shaw AS. The MAPK scaffold kinase suppressor of Ras is involved in ERK activation by stress and proinflammatory cytokines and induction of arthritis. J Immunol 2006;177:6152-8.
    • (2006) J Immunol , vol.177 , pp. 6152-6158
    • Fusello, A.M.1    Mandik-Nayak, L.2    Shih, F.3    Lewis, R.E.4    Allen, P.M.5    Shaw, A.S.6
  • 30
    • 25144518584 scopus 로고    scopus 로고
    • Tumour necrosis factor activates the mitogen-activated protein kinases p38a and ERK in the synovial membrane in vivo
    • Gortz B, Hayer S, Tuerck B, Zwerina J, Smolen JS, Schett G. Tumour necrosis factor activates the mitogen-activated protein kinases p38a and ERK in the synovial membrane in vivo. Arthritis Res Ther 2005;7:R1140-7.
    • (2005) Arthritis Res Ther , vol.7
    • Gortz, B.1    Hayer, S.2    Tuerck, B.3    Zwerina, J.4    Smolen, J.S.5    Schett, G.6
  • 31
    • 0036051342 scopus 로고    scopus 로고
    • Molecular interpretation of ERK signal duration by immediate early gene products
    • Murphy LO, Smith S, Chen RH, Fingar DC, Blenis J. Molecular interpretation of ERK signal duration by immediate early gene products. Nat Cell Biol 2002;4:556-64.
    • (2002) Nat Cell Biol , vol.4 , pp. 556-564
    • Murphy, L.O.1    Smith, S.2    Chen, R.H.3    Fingar, D.C.4    Blenis, J.5
  • 32
    • 0029925577 scopus 로고    scopus 로고
    • Expression of c-fos gene inhibits proteoglycan synthesis in transfected chondrocyte
    • Tsuji M, Funahashi S, Takigawa M, Seiki M, Fujii K, Yoshida T. Expression of c-fos gene inhibits proteoglycan synthesis in transfected chondrocyte. FEBS Lett 1996;381:222-6.
    • (1996) FEBS Lett , vol.381 , pp. 222-226
    • Tsuji, M.1    Funahashi, S.2    Takigawa, M.3    Seiki, M.4    Fujii, K.5    Yoshida, T.6
  • 33
    • 0033940149 scopus 로고    scopus 로고
    • The possible role of c-fos expression in rheumatoid cartilage destruction
    • Tsuji M, Hirakawa K, Kato A, Fujii K. The possible role of c-fos expression in rheumatoid cartilage destruction. J Rheumatol 2000; 27:1606-21.
    • (2000) J Rheumatol , vol.27 , pp. 1606-1621
    • Tsuji, M.1    Hirakawa, K.2    Kato, A.3    Fujii, K.4
  • 34
    • 33846380636 scopus 로고    scopus 로고
    • HC-gp39 contributes to chondrocyte differentiation by inducing SOX9 and type II collagen expressions
    • Jacques C, Recklies AD, Levy A, Berenbaum F. HC-gp39 contributes to chondrocyte differentiation by inducing SOX9 and type II collagen expressions. Osteoarthritis Cartilage 2007;15:138-46.
    • (2007) Osteoarthritis Cartilage , vol.15 , pp. 138-146
    • Jacques, C.1    Recklies, A.D.2    Levy, A.3    Berenbaum, F.4
  • 35
    • 0030899814 scopus 로고    scopus 로고
    • SOX9 is a potent activator of the chondrocyte-specific enhancer of the pro α1(II) collagen gene
    • Lefebvre V, Huang W, Harley VR, Goodfellow PN, de Crombrugghe B. SOX9 is a potent activator of the chondrocyte-specific enhancer of the pro α1(II) collagen gene. Mol Cell Biol 1997;17: 2336-46.
    • (1997) Mol Cell Biol , vol.17 , pp. 2336-2346
    • Lefebvre, V.1    Huang, W.2    Harley, V.R.3    Goodfellow, P.N.4    de Crombrugghe, B.5
  • 36
    • 33750530166 scopus 로고    scopus 로고
    • Igf-I extends the chondrogenic potential of human articular chondrocytes in vitro: Molecular association between Sox9 and Erk1/2
    • Shakibaei M, Seifarth C, John T, Rahmanzadeh M, Mobasheri A. Igf-I extends the chondrogenic potential of human articular chondrocytes in vitro: molecular association between Sox9 and Erk1/2. Biochem Pharmacol 2006;72:1382-95.
    • (2006) Biochem Pharmacol , vol.72 , pp. 1382-1395
    • Shakibaei, M.1    Seifarth, C.2    John, T.3    Rahmanzadeh, M.4    Mobasheri, A.5
  • 37
    • 33749459324 scopus 로고    scopus 로고
    • Disassembly of the vimentin cytoskeleton disrupts articular cartilage chondrocyte homeostasis
    • Blain EJ, Gilbert SJ, Duance VC. Disassembly of the vimentin cytoskeleton disrupts articular cartilage chondrocyte homeostasis. Matrix Biology 2006;25:398-408.
    • (2006) Matrix Biology , vol.25 , pp. 398-408
    • Blain, E.J.1    Gilbert, S.J.2    Duance, V.C.3
  • 38
    • 0034531395 scopus 로고    scopus 로고
    • Patel CV, Handy I, Goldsmith T, Patel RC. PACT, a stress-modulated cellular activator of interferon-induced double-stranded RNA-activated protein kinase, PKR. J Biol Chem 2000; 275:37993-8.
    • Patel CV, Handy I, Goldsmith T, Patel RC. PACT, a stress-modulated cellular activator of interferon-induced double-stranded RNA-activated protein kinase, PKR. J Biol Chem 2000; 275:37993-8.
  • 39
    • 85176676735 scopus 로고    scopus 로고
    • Alessi DR, Cuenda A, Cohen P, Dudley DT, Saltiel AR. PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo. J Biol Chem 1995;270: 27489-94.
    • Alessi DR, Cuenda A, Cohen P, Dudley DT, Saltiel AR. PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo. J Biol Chem 1995;270: 27489-94.
  • 42
    • 0037334522 scopus 로고    scopus 로고
    • Microenvironment regulation of extracellular signal-regulated kinase activity in chondrocytes: Effects of culture configuration, interleukin-1, and compressive stress
    • Li KW, Wang AS, Sah RL. Microenvironment regulation of extracellular signal-regulated kinase activity in chondrocytes: effects of culture configuration, interleukin-1, and compressive stress. Arthritis Rheum 2003;48:689-99.
    • (2003) Arthritis Rheum , vol.48 , pp. 689-699
    • Li, K.W.1    Wang, A.S.2    Sah, R.L.3
  • 43
    • 0026007737 scopus 로고
    • Identification of sphingomyelin turnover as an effector mechanism for the action of tumor necrosis factor α and γ-interferon: Specific role in cell differentiation
    • Kim MY, Linardic C, Obeid L, Hannun Y. Identification of sphingomyelin turnover as an effector mechanism for the action of tumor necrosis factor α and γ-interferon: specific role in cell differentiation. J Biol Chem 1991;266:484-9.
    • (1991) J Biol Chem , vol.266 , pp. 484-489
    • Kim, M.Y.1    Linardic, C.2    Obeid, L.3    Hannun, Y.4
  • 44
    • 0027327212 scopus 로고
    • Tumor necrosis factor-α (TNF-α) signal transduction through ceramide: Dissociation of growth inhibitory effects of TNF-α from activation of nuclear factor-κB
    • Dbaibo GS, Obeid LM, Hannun YA. Tumor necrosis factor-α (TNF-α) signal transduction through ceramide: dissociation of growth inhibitory effects of TNF-α from activation of nuclear factor-κB. J Biol Chem 1993;268:17762-6.
    • (1993) J Biol Chem , vol.268 , pp. 17762-17766
    • Dbaibo, G.S.1    Obeid, L.M.2    Hannun, Y.A.3
  • 45
    • 33845886924 scopus 로고    scopus 로고
    • Dynamic regulation of ERK2 nuclear translocation and mobility in living cells
    • Costa M, Marchi M, Cardarelli F, Roy A, Beltram F, Maffei L, et al. Dynamic regulation of ERK2 nuclear translocation and mobility in living cells. J Cell Sci 2006;119:4952-63.
    • (2006) J Cell Sci , vol.119 , pp. 4952-4963
    • Costa, M.1    Marchi, M.2    Cardarelli, F.3    Roy, A.4    Beltram, F.5    Maffei, L.6
  • 47
    • 0028787249 scopus 로고
    • The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells
    • Okazaki K, Sagata N. The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells. EMBO J 1995;14:5048-59.
    • (1995) EMBO J , vol.14 , pp. 5048-5059
    • Okazaki, K.1    Sagata, N.2
  • 48
    • 0034603036 scopus 로고    scopus 로고
    • Potent inhibition of the master chondrogenic factor Sox9 gene by interleukin-1 and tumor necrosis factor-α
    • Murakami S, Lefebvre V, de Crombrugghe B. Potent inhibition of the master chondrogenic factor Sox9 gene by interleukin-1 and tumor necrosis factor-α. J Biol Chem 2000;275:3687-92.
    • (2000) J Biol Chem , vol.275 , pp. 3687-3692
    • Murakami, S.1    Lefebvre, V.2    de Crombrugghe, B.3
  • 49
    • 0037305315 scopus 로고    scopus 로고
    • SOX9 exerts a bifunctional effect on type II collagen gene (COL2A1) expression in chondrocytes depending on the differentiation state
    • Kypriotou M, Fossard-Demoor M, Chadjichristos C, Ghayor C, de Crombrugghe B, Pujol JP, et al. SOX9 exerts a bifunctional effect on type II collagen gene (COL2A1) expression in chondrocytes depending on the differentiation state. DNA Cell Biol 2003;22: 119-29.
    • (2003) DNA Cell Biol , vol.22 , pp. 119-129
    • Kypriotou, M.1    Fossard-Demoor, M.2    Chadjichristos, C.3    Ghayor, C.4    de Crombrugghe, B.5    Pujol, J.P.6
  • 50
    • 0037143766 scopus 로고    scopus 로고
    • A nuclear export signal within the high mobility group domain regulates the nucleocytoplasmic translocation of SOX9 during sexual determination
    • Gasca S, Canizares J, De Santa Barbara P, Mejean C, Poulat F, Berta P, et al. A nuclear export signal within the high mobility group domain regulates the nucleocytoplasmic translocation of SOX9 during sexual determination. Proc Natl Acad Sci U S A 2002;99:11199-204.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 11199-11204
    • Gasca, S.1    Canizares, J.2    De Santa Barbara, P.3    Mejean, C.4    Poulat, F.5    Berta, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.