메뉴 건너뛰기




Volumn 67, Issue 8, 2015, Pages 2097-2107

Transthyretin deposition in articular cartilage: A novel mechanism in the pathogenesis of osteoarthritis

Author keywords

[No Author keywords available]

Indexed keywords

ADVANCED GLYCATION END PRODUCT RECEPTOR; AMYLOID; CONGO RED; MITOGEN ACTIVATED PROTEIN KINASE P38; PREALBUMIN; RECOMBINANT PROTEIN; RESVERATROL; TOLL LIKE RECEPTOR 4; AMYLOID PROTEIN; IMMUNOGLOBULIN RECEPTOR; MESSENGER RNA; TLR4 PROTEIN, HUMAN;

EID: 84938151998     PISSN: 23265191     EISSN: 23265205     Source Type: Journal    
DOI: 10.1002/art.39178     Document Type: Article
Times cited : (36)

References (69)
  • 1
    • 38149052992 scopus 로고    scopus 로고
    • The National Arthritis Data Workgroup. Estimates of the prevalence of arthritis and other rheumatic conditions in the United States: Part II
    • Lawrence RC, Felson DT, Helmick CG, Arnold LM, Choi H, Deyo RA, et al., for the National Arthritis Data Workgroup. Estimates of the prevalence of arthritis and other rheumatic conditions in the United States: part II. Arthritis Rheum 2008; 58: 26-35.
    • (2008) Arthritis Rheum , vol.58 , pp. 26-35
    • Lawrence, R.C.1    Felson, D.T.2    Helmick, C.G.3    Arnold, L.M.4    Choi, H.5    Deyo, R.A.6
  • 2
    • 0346786219 scopus 로고    scopus 로고
    • The systemic amyloidoses
    • Buxbaum JN., The systemic amyloidoses. Curr Opin Rheumatol 2004; 16: 67-75.
    • (2004) Curr Opin Rheumatol , vol.16 , pp. 67-75
    • Buxbaum, J.N.1
  • 4
    • 84861994775 scopus 로고    scopus 로고
    • Effects of aging on articular cartilage homeostasis
    • Lotz M, Loeser RF., Effects of aging on articular cartilage homeostasis. Bone 2012; 51: 241-8.
    • (2012) Bone , vol.51 , pp. 241-248
    • Lotz, M.1    Loeser, R.F.2
  • 8
    • 79955972936 scopus 로고    scopus 로고
    • Insight into amyloid structure using chemical probes
    • Reinke AA, Gestwicki JE., Insight into amyloid structure using chemical probes. Chem Biol Drug Des 2011; 77: 399-411.
    • (2011) Chem Biol Drug des , vol.77 , pp. 399-411
    • Reinke, A.A.1    Gestwicki, J.E.2
  • 9
    • 0014792730 scopus 로고
    • Amyloid deposits in articular cartilage
    • Bywaters EG, Dorling J., Amyloid deposits in articular cartilage. Ann Rheum Dis 1970; 29: 294-306.
    • (1970) Ann Rheum Dis , vol.29 , pp. 294-306
    • Bywaters, E.G.1    Dorling, J.2
  • 12
    • 0022510635 scopus 로고
    • Amyloid deposits in the knee joint at autopsy
    • Ladefoged C., Amyloid deposits in the knee joint at autopsy. Ann Rheum Dis 1986; 45: 668-72.
    • (1986) Ann Rheum Dis , vol.45 , pp. 668-672
    • Ladefoged, C.1
  • 13
    • 0026543957 scopus 로고
    • Localized deposition of amyloid in articular cartilage
    • Athanasou NA, Sallie B., Localized deposition of amyloid in articular cartilage. Histopathology 1992; 20: 41-6.
    • (1992) Histopathology , vol.20 , pp. 41-46
    • Athanasou, N.A.1    Sallie, B.2
  • 15
    • 84855429655 scopus 로고    scopus 로고
    • Plasma proteins present in osteoarthritic synovial fluid can stimulate cytokine production via Toll-like receptor 4
    • Sohn DH, Sokolove J, Sharpe O, Erhart JC, Chandra PE, Lahey LJ, et al., Plasma proteins present in osteoarthritic synovial fluid can stimulate cytokine production via Toll-like receptor 4. Arthritis Res Ther 2012; 14: R7.
    • (2012) Arthritis Res Ther , vol.14 , pp. R7
    • Sohn, D.H.1    Sokolove, J.2    Sharpe, O.3    Erhart, J.C.4    Chandra, P.E.5    Lahey, L.J.6
  • 16
    • 0023696119 scopus 로고
    • Evidence that the amyloid fibril protein in senile systemic amyloidosis is derived from normal prealbumin
    • Cornwell GG III, Sletten K, Johansson B, Westermark P., Evidence that the amyloid fibril protein in senile systemic amyloidosis is derived from normal prealbumin. Biochem Biophys Res Commun 1988; 154: 648-53.
    • (1988) Biochem Biophys Res Commun , vol.154 , pp. 648-653
    • Cornwell, G.G.1    Sletten, K.2    Johansson, B.3    Westermark, P.4
  • 17
    • 41649088603 scopus 로고    scopus 로고
    • Senile systemic amyloidosis affects 25% of the very aged and associates with genetic variation in α2-macroglobulin and tau: A population-based autopsy study
    • Tanskanen M, Peuralinna T, Polvikoski T, Notkola IL, Sulkava R, Hardy J, et al., Senile systemic amyloidosis affects 25% of the very aged and associates with genetic variation in α2-macroglobulin and tau: a population-based autopsy study. Ann Med 2008; 40: 232-9.
    • (2008) Ann Med , vol.40 , pp. 232-239
    • Tanskanen, M.1    Peuralinna, T.2    Polvikoski, T.3    Notkola, I.L.4    Sulkava, R.5    Hardy, J.6
  • 18
    • 22844447647 scopus 로고    scopus 로고
    • Transthyretin-related familial amyloidotic polyneuropathy
    • Ando Y, Nakamura M, Araki S., Transthyretin-related familial amyloidotic polyneuropathy. Arch Neurol 2005; 62: 1057-62.
    • (2005) Arch Neurol , vol.62 , pp. 1057-1062
    • Ando, Y.1    Nakamura, M.2    Araki, S.3
  • 20
    • 2942593931 scopus 로고    scopus 로고
    • Transthyretin aggregation under partially denaturing conditions is a downhill polymerization
    • Hurshman AR, White JT, Powers ET, Kelly JW., Transthyretin aggregation under partially denaturing conditions is a downhill polymerization. Biochemistry 2004; 43: 7365-81.
    • (2004) Biochemistry , vol.43 , pp. 7365-7381
    • Hurshman, A.R.1    White, J.T.2    Powers, E.T.3    Kelly, J.W.4
  • 24
    • 84898077465 scopus 로고    scopus 로고
    • Quantification of transthyretin kinetic stability in human plasma using subunit exchange
    • Rappley I, Monteiro C, Novais M, Baranczak A, Solis G, Wiseman RL, et al., Quantification of transthyretin kinetic stability in human plasma using subunit exchange. Biochemistry 2014; 53: 1993-2006.
    • (2014) Biochemistry , vol.53 , pp. 1993-2006
    • Rappley, I.1    Monteiro, C.2    Novais, M.3    Baranczak, A.4    Solis, G.5    Wiseman, R.L.6
  • 26
    • 0033856957 scopus 로고    scopus 로고
    • Investigation of the Alamar Blue (resazurin) fluorescent dye for the assessment of mammalian cell cytotoxicity
    • O'Brien J, Wilson I, Orton T, Pognan F., Investigation of the Alamar Blue (resazurin) fluorescent dye for the assessment of mammalian cell cytotoxicity. Eur J Biochem 2000; 267: 5421-6.
    • (2000) Eur J Biochem , vol.267 , pp. 5421-5426
    • O'Brien, J.1    Wilson, I.2    Orton, T.3    Pognan, F.4
  • 27
    • 0020485070 scopus 로고
    • Cellular origin of prealbumin in the rat
    • Felding P, Fex G., Cellular origin of prealbumin in the rat. Biochim Biophys Acta 1982; 716: 446-9.
    • (1982) Biochim Biophys Acta , vol.716 , pp. 446-449
    • Felding, P.1    Fex, G.2
  • 28
    • 0021996005 scopus 로고
    • Rat transthyretin (prealbumin): Molecular cloning, nucleotide sequence, and gene expression in liver and brain
    • Dickson PW, Howlett GJ, Schreiber G., Rat transthyretin (prealbumin): molecular cloning, nucleotide sequence, and gene expression in liver and brain. J Biol Chem 1985; 260: 8214-9.
    • (1985) J Biol Chem , vol.260 , pp. 8214-8219
    • Dickson, P.W.1    Howlett, G.J.2    Schreiber, G.3
  • 29
    • 0035079799 scopus 로고    scopus 로고
    • Amyloid and nonfibrillar deposits in mice transgenic for wild-type human transthyretin: A possible model for senile systemic amyloidosis
    • Teng MH, Yin JY, Vidal R, Ghiso J, Kumar A, Rabenou R, et al., Amyloid and nonfibrillar deposits in mice transgenic for wild-type human transthyretin: a possible model for senile systemic amyloidosis. Lab Invest 2001; 81: 385-96.
    • (2001) Lab Invest , vol.81 , pp. 385-396
    • Teng, M.H.1    Yin, J.Y.2    Vidal, R.3    Ghiso, J.4    Kumar, A.5    Rabenou, R.6
  • 30
    • 79953681364 scopus 로고    scopus 로고
    • The value of routine histopathology during hip arthroplasty in patients with degenerative and inflammatory arthritis
    • Niggemeyer O, Steinhagen J, Zustin J, Ruther W., The value of routine histopathology during hip arthroplasty in patients with degenerative and inflammatory arthritis. Hip Int 2011; 21: 98-106.
    • (2011) Hip Int , vol.21 , pp. 98-106
    • Niggemeyer, O.1    Steinhagen, J.2    Zustin, J.3    Ruther, W.4
  • 31
    • 84893138276 scopus 로고    scopus 로고
    • Clinical and laboratory characteristics of patients having amyloidogenic transthyretin deposition in osteoarthritic knee joints
    • Gu YJ, Ge P, Mu Y, Lu JH, Zheng F, Sun XG., Clinical and laboratory characteristics of patients having amyloidogenic transthyretin deposition in osteoarthritic knee joints. J Zhejiang Univ Sci B 2014; 15: 92-9.
    • (2014) J Zhejiang Univ Sci B , vol.15 , pp. 92-99
    • Gu, Y.J.1    Ge, P.2    Mu, Y.3    Lu, J.H.4    Zheng, F.5    Sun, X.G.6
  • 32
    • 84883001300 scopus 로고    scopus 로고
    • Synovial deposition of wild-type transthyretin-derived amyloid in knee joint osteoarthritis patients
    • Takanashi T, Matsuda M, Yazaki M, Yamazaki H, Nawata M, Katagiri Y, et al., Synovial deposition of wild-type transthyretin-derived amyloid in knee joint osteoarthritis patients. Amyloid 2013; 20: 151-5.
    • (2013) Amyloid , vol.20 , pp. 151-155
    • Takanashi, T.1    Matsuda, M.2    Yazaki, M.3    Yamazaki, H.4    Nawata, M.5    Katagiri, Y.6
  • 33
    • 84856378249 scopus 로고    scopus 로고
    • High prevalence of wild-type transthyretin deposition in patients with idiopathic carpal tunnel syndrome: A common cause of carpal tunnel syndrome in the elderly
    • Sekijima Y, Uchiyama S, Tojo K, Sano K, Shimizu Y, Imaeda T, et al., High prevalence of wild-type transthyretin deposition in patients with idiopathic carpal tunnel syndrome: a common cause of carpal tunnel syndrome in the elderly. Hum Pathol 2011; 42: 1785-91.
    • (2011) Hum Pathol , vol.42 , pp. 1785-1791
    • Sekijima, Y.1    Uchiyama, S.2    Tojo, K.3    Sano, K.4    Shimizu, Y.5    Imaeda, T.6
  • 34
    • 0036965815 scopus 로고    scopus 로고
    • Senile systemic amyloidosis presenting as bilateral carpal tunnel syndrome
    • Takei Y, Hattori T, Gono T, Tokuda T, Saitoh S, Hoshii Y, et al., Senile systemic amyloidosis presenting as bilateral carpal tunnel syndrome. Amyloid 2002; 9: 252-5.
    • (2002) Amyloid , vol.9 , pp. 252-255
    • Takei, Y.1    Hattori, T.2    Gono, T.3    Tokuda, T.4    Saitoh, S.5    Hoshii, Y.6
  • 35
    • 0242606487 scopus 로고    scopus 로고
    • Senile systemic amyloidosis starting as bilateral carpal and left ulnar tunnel syndrome
    • Takei Y, Hattori T, Tokuda T, Matsuda M, Saitoh S, Hoshii Y, et al., Senile systemic amyloidosis starting as bilateral carpal and left ulnar tunnel syndrome. Intern Med 2003; 42: 1050-1.
    • (2003) Intern Med , vol.42 , pp. 1050-1051
    • Takei, Y.1    Hattori, T.2    Tokuda, T.3    Matsuda, M.4    Saitoh, S.5    Hoshii, Y.6
  • 36
    • 0028839263 scopus 로고
    • Damage to type II collagen in aging and osteoarthritis starts at the articular surface, originates around chondrocytes, and extends into the cartilage with progressive degeneration
    • Hollander AP, Pidoux I, Reiner A, Rorabeck C, Bourne R, Poole AR., Damage to type II collagen in aging and osteoarthritis starts at the articular surface, originates around chondrocytes, and extends into the cartilage with progressive degeneration. J Clin Invest 1995; 96: 2859-69.
    • (1995) J Clin Invest , vol.96 , pp. 2859-2869
    • Hollander, A.P.1    Pidoux, I.2    Reiner, A.3    Rorabeck, C.4    Bourne, R.5    Poole, A.R.6
  • 37
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly JW., The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr Opin Struct Biol 1998; 8: 101-6.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 38
    • 0035920156 scopus 로고    scopus 로고
    • Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants
    • Quintas A, Vaz DC, Cardoso I, Saraiva MJ, Brito RM., Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants. J Biol Chem 2001; 276: 27207-13.
    • (2001) J Biol Chem , vol.276 , pp. 27207-27213
    • Quintas, A.1    Vaz, D.C.2    Cardoso, I.3    Saraiva, M.J.4    Brito, R.M.5
  • 39
    • 84875426278 scopus 로고    scopus 로고
    • Age-related oxidative modifications of transthyretin modulate its amyloidogenicity
    • Zhao L, Buxbaum JN, Reixach N., Age-related oxidative modifications of transthyretin modulate its amyloidogenicity. Biochemistry 2013; 52: 1913-26.
    • (2013) Biochemistry , vol.52 , pp. 1913-1926
    • Zhao, L.1    Buxbaum, J.N.2    Reixach, N.3
  • 40
    • 23944483446 scopus 로고    scopus 로고
    • Effect of nitric oxide in amyloid fibril formation on transthyretin-related amyloidosis
    • Saito S, Ando Y, Nakamura M, Ueda M, Kim J, Ishima Y, et al., Effect of nitric oxide in amyloid fibril formation on transthyretin-related amyloidosis. Biochemistry 2005; 44: 11122-9.
    • (2005) Biochemistry , vol.44 , pp. 11122-11129
    • Saito, S.1    Ando, Y.2    Nakamura, M.3    Ueda, M.4    Kim, J.5    Ishima, Y.6
  • 41
    • 79954990699 scopus 로고    scopus 로고
    • Heparan sulfate/heparin promotes transthyretin fibrillization through selective binding to a basic motif in the protein
    • Noborn F, O'Callaghan P, Hermansson E, Zhang X, Ancsin JB, Damas AM, et al., Heparan sulfate/heparin promotes transthyretin fibrillization through selective binding to a basic motif in the protein. Proc Natl Acad Sci U S A 2011; 108: 5584-9.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 5584-5589
    • Noborn, F.1    O'Callaghan, P.2    Hermansson, E.3    Zhang, X.4    Ancsin, J.B.5    Damas, A.M.6
  • 42
    • 79851492876 scopus 로고    scopus 로고
    • Sulfated glycosaminoglycans accelerate transthyretin amyloidogenesis by quaternary structural conversion
    • Bourgault S, Solomon JP, Reixach N, Kelly JW., Sulfated glycosaminoglycans accelerate transthyretin amyloidogenesis by quaternary structural conversion. Biochemistry 2011; 50: 1001-15.
    • (2011) Biochemistry , vol.50 , pp. 1001-1015
    • Bourgault, S.1    Solomon, J.P.2    Reixach, N.3    Kelly, J.W.4
  • 43
    • 0033025739 scopus 로고    scopus 로고
    • Sulfation of chondroitin sulfate in human articular cartilage: The effect of age, topographical position, and zone of cartilage on tissue composition
    • Bayliss MT, Osborne D, Woodhouse S, Davidson C., Sulfation of chondroitin sulfate in human articular cartilage: the effect of age, topographical position, and zone of cartilage on tissue composition. J Biol Chem 1999; 274: 15892-900.
    • (1999) J Biol Chem , vol.274 , pp. 15892-15900
    • Bayliss, M.T.1    Osborne, D.2    Woodhouse, S.3    Davidson, C.4
  • 44
    • 0028931127 scopus 로고
    • Comparison of chondroitin sulphate composition of femoral head articular cartilage from patients with femoral neck fractures and osteoarthritis and controls
    • Burkhardt D, Michel BA, Baici A, Kissling R, Theiler R., Comparison of chondroitin sulphate composition of femoral head articular cartilage from patients with femoral neck fractures and osteoarthritis and controls. Rheumatol Int 1995; 14: 235-41.
    • (1995) Rheumatol Int , vol.14 , pp. 235-241
    • Burkhardt, D.1    Michel, B.A.2    Baici, A.3    Kissling, R.4    Theiler, R.5
  • 45
    • 0032519990 scopus 로고    scopus 로고
    • Ageing and zonal variation in post-translational modification of collagen in normal human articular cartilage: The age-related increase in non-enzymatic glycation affects biomechanical properties of cartilage
    • Bank RA, Bayliss MT, Lafeber FP, Maroudas A, Tekoppele JM., Ageing and zonal variation in post-translational modification of collagen in normal human articular cartilage: the age-related increase in non-enzymatic glycation affects biomechanical properties of cartilage. Biochem J 1998; 330: 345-51.
    • (1998) Biochem J , vol.330 , pp. 345-351
    • Bank, R.A.1    Bayliss, M.T.2    Lafeber, F.P.3    Maroudas, A.4    Tekoppele, J.M.5
  • 46
    • 84871502515 scopus 로고    scopus 로고
    • Protein homeostasis: Live long, won't prosper
    • Toyama BH, Hetzer MW., Protein homeostasis: live long, won't prosper. Nat Rev Mol Cell Biol 2013; 14: 55-61.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 55-61
    • Toyama, B.H.1    Hetzer, M.W.2
  • 50
    • 1542357685 scopus 로고    scopus 로고
    • Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture
    • Reixach N, Deechongkit S, Jiang X, Kelly JW, Buxbaum JN., Tissue damage in the amyloidoses: transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture. Proc Natl Acad Sci U S A 2004; 101: 2817-22.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 2817-2822
    • Reixach, N.1    Deechongkit, S.2    Jiang, X.3    Kelly, J.W.4    Buxbaum, J.N.5
  • 51
    • 56349095198 scopus 로고    scopus 로고
    • Hammarstrom P. Prefibrillar transthyretin oligomers and cold stored native tetrameric transthyretin are cytotoxic in cell culture
    • Sorgjerd K, Klingstedt T, Lindgren M, Kagedal K, Hammarstrom P. Prefibrillar transthyretin oligomers and cold stored native tetrameric transthyretin are cytotoxic in cell culture. Biochem Biophys Res Commun 2008; 377: 1072-8.
    • (2008) Biochem Biophys Res Commun , vol.377 , pp. 1072-1078
    • Sorgjerd, K.1    Klingstedt, T.2    Lindgren, M.3    Kagedal, K.4
  • 52
    • 84898419785 scopus 로고    scopus 로고
    • Resveratrol protects chondrocytes from apoptosis via altering the ultrastructural and biomechanical properties: An AFM study
    • Jin H, Liang Q, Chen T, Wang X., Resveratrol protects chondrocytes from apoptosis via altering the ultrastructural and biomechanical properties: an AFM study. PLoS One 2014; 9: e91611.
    • (2014) PLoS One , vol.9 , pp. e91611
    • Jin, H.1    Liang, Q.2    Chen, T.3    Wang, X.4
  • 54
    • 0035180285 scopus 로고    scopus 로고
    • Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: Evidence for toxicity of nonfibrillar aggregates
    • Sousa MM, Cardoso I, Fernandes R, Guimaraes A, Saraiva MJ., Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates. Am J Pathol 2001; 159: 1993-2000.
    • (2001) Am J Pathol , vol.159 , pp. 1993-2000
    • Sousa, M.M.1    Cardoso, I.2    Fernandes, R.3    Guimaraes, A.4    Saraiva, M.J.5
  • 55
    • 0036841818 scopus 로고    scopus 로고
    • Evidence for early cytotoxic aggregates in transgenic mice for human transthyretin Leu55Pro
    • Sousa MM, Fernandes R, Palha JA, Taboada A, Vieira P, Saraiva MJ., Evidence for early cytotoxic aggregates in transgenic mice for human transthyretin Leu55Pro. Am J Pathol 2002; 161: 1935-48.
    • (2002) Am J Pathol , vol.161 , pp. 1935-1948
    • Sousa, M.M.1    Fernandes, R.2    Palha, J.A.3    Taboada, A.4    Vieira, P.5    Saraiva, M.J.6
  • 56
    • 84861772766 scopus 로고    scopus 로고
    • Why are some amyloidoses systemic? Does hepatic "chaperoning at a distance" prevent cardiac deposition in a transgenic model of human senile systemic (transthyretin) amyloidosis?
    • Buxbaum JN, Tagoe C, Gallo G, Walker JR, Kurian S, Salomon DR., Why are some amyloidoses systemic? Does hepatic "chaperoning at a distance" prevent cardiac deposition in a transgenic model of human senile systemic (transthyretin) amyloidosis? FASEB J 2012; 26: 2283-93.
    • (2012) FASEB J , vol.26 , pp. 2283-2293
    • Buxbaum, J.N.1    Tagoe, C.2    Gallo, G.3    Walker, J.R.4    Kurian, S.5    Salomon, D.R.6
  • 57
    • 23644436200 scopus 로고    scopus 로고
    • Articular chondrocytes express the receptor for advanced glycation end products: Potential role in osteoarthritis
    • Loeser RF, Yammani RR, Carlson CS, Chen H, Cole A, Im HJ, et al., Articular chondrocytes express the receptor for advanced glycation end products: potential role in osteoarthritis. Arthritis Rheum 2005; 52: 2376-85.
    • (2005) Arthritis Rheum , vol.52 , pp. 2376-2385
    • Loeser, R.F.1    Yammani, R.R.2    Carlson, C.S.3    Chen, H.4    Cole, A.5    Im, H.J.6
  • 58
    • 33749331604 scopus 로고    scopus 로고
    • Increase in production of matrix metalloproteinase 13 by human articular chondrocytes due to stimulation with S100A4: Role of the receptor for advanced glycation end products
    • Yammani RR, Carlson CS, Bresnick AR, Loeser RF., Increase in production of matrix metalloproteinase 13 by human articular chondrocytes due to stimulation with S100A4: role of the receptor for advanced glycation end products. Arthritis Rheum 2006; 54: 2901-11.
    • (2006) Arthritis Rheum , vol.54 , pp. 2901-2911
    • Yammani, R.R.1    Carlson, C.S.2    Bresnick, A.R.3    Loeser, R.F.4
  • 59
    • 31044444377 scopus 로고    scopus 로고
    • Activation of receptor for advanced glycation end products in osteoarthritis leads to increased stimulation of chondrocytes and synoviocytes
    • Steenvoorden MM, Huizinga TW, Verzijl N, Bank RA, Ronday HK, Luning HA, et al., Activation of receptor for advanced glycation end products in osteoarthritis leads to increased stimulation of chondrocytes and synoviocytes. Arthritis Rheum 2006; 54: 253-63.
    • (2006) Arthritis Rheum , vol.54 , pp. 253-263
    • Steenvoorden, M.M.1    Huizinga, T.W.2    Verzijl, N.3    Bank, R.A.4    Ronday, H.K.5    Luning, H.A.6
  • 60
    • 29144510038 scopus 로고    scopus 로고
    • Inflammation-induced chondrocyte hypertrophy is driven by receptor for advanced glycation end products
    • Cecil DL, Johnson K, Rediske J, Lotz M, Schmidt AM, Terkeltaub R., Inflammation-induced chondrocyte hypertrophy is driven by receptor for advanced glycation end products. J Immunol 2005; 175: 8296-302.
    • (2005) J Immunol , vol.175 , pp. 8296-8302
    • Cecil, D.L.1    Johnson, K.2    Rediske, J.3    Lotz, M.4    Schmidt, A.M.5    Terkeltaub, R.6
  • 61
    • 0035478665 scopus 로고    scopus 로고
    • Familial amyloid polyneuropathy: Receptor for advanced glycation end products-dependent triggering of neuronal inflammatory and apoptotic pathways
    • Sousa MM, Du Yan S, Fernandes R, Guimaraes A, Stern D, Saraiva MJ., Familial amyloid polyneuropathy: receptor for advanced glycation end products-dependent triggering of neuronal inflammatory and apoptotic pathways. J Neurosci 2001; 21: 7576-86.
    • (2001) J Neurosci , vol.21 , pp. 7576-7586
    • Sousa, M.M.1    Du Yan, S.2    Fernandes, R.3    Guimaraes, A.4    Stern, D.5    Saraiva, M.J.6
  • 62
    • 33646925693 scopus 로고    scopus 로고
    • In vitro inhibition of transthyretin aggregate-induced cytotoxicity by full and peptide derived forms of the soluble receptor for advanced glycation end products (RAGE)
    • Monteiro FA, Cardoso I, Sousa MM, Saraiva MJ., In vitro inhibition of transthyretin aggregate-induced cytotoxicity by full and peptide derived forms of the soluble receptor for advanced glycation end products (RAGE). FEBS Lett 2006; 580: 3451-6.
    • (2006) FEBS Lett , vol.580 , pp. 3451-3456
    • Monteiro, F.A.1    Cardoso, I.2    Sousa, M.M.3    Saraiva, M.J.4
  • 63
    • 84878947383 scopus 로고    scopus 로고
    • Advanced glycation end products induce peroxisome proliferator-activated receptor γ down-regulation-related inflammatory signals in human chondrocytes via Toll-like receptor-4 and receptor for advanced glycation end products
    • Chen YJ, Sheu ML, Tsai KS, Yang RS, Liu SH., Advanced glycation end products induce peroxisome proliferator-activated receptor γ down-regulation-related inflammatory signals in human chondrocytes via Toll-like receptor-4 and receptor for advanced glycation end products. PLoS One 2013; 8: e66611.
    • (2013) PLoS One , vol.8 , pp. e66611
    • Chen, Y.J.1    Sheu, M.L.2    Tsai, K.S.3    Yang, R.S.4    Liu, S.H.5
  • 64
    • 84858962775 scopus 로고    scopus 로고
    • Alarmins S100A8 and S100A9 elicit a catabolic effect in human osteoarthritic chondrocytes that is dependent on Toll-like receptor 4
    • Schelbergen RF, Blom AB, van den Bosch MH, Sloetjes A, Abdollahi-Roodsaz S, Schreurs BW, et al., Alarmins S100A8 and S100A9 elicit a catabolic effect in human osteoarthritic chondrocytes that is dependent on Toll-like receptor 4. Arthritis Rheum 2012; 64: 1477-87.
    • (2012) Arthritis Rheum , vol.64 , pp. 1477-1487
    • Schelbergen, R.F.1    Blom, A.B.2    Van Den Bosch, M.H.3    Sloetjes, A.4    Abdollahi-Roodsaz, S.5    Schreurs, B.W.6
  • 65
    • 77953914908 scopus 로고    scopus 로고
    • Small hyaluronan oligosaccharides induce inflammation by engaging both Toll-like-4 and CD44 receptors in human chondrocytes
    • Campo GM, Avenoso A, Campo S, D'Ascola A, Nastasi G, Calatroni A., Small hyaluronan oligosaccharides induce inflammation by engaging both Toll-like-4 and CD44 receptors in human chondrocytes. Biochem Pharmacol 2010; 80: 480-90.
    • (2010) Biochem Pharmacol , vol.80 , pp. 480-490
    • Campo, G.M.1    Avenoso, A.2    Campo, S.3    D'Ascola, A.4    Nastasi, G.5    Calatroni, A.6
  • 66
    • 0026377044 scopus 로고
    • Doppler echocardiographic assessments of left ventricular diastolic filling in patients with amyloid heart disease
    • Hongo M, Kono J, Yamada H, Misawa T, Tanaka M, Nakatsuka T, et al., Doppler echocardiographic assessments of left ventricular diastolic filling in patients with amyloid heart disease. J Cardiol 1991; 21: 391-401.
    • (1991) J Cardiol , vol.21 , pp. 391-401
    • Hongo, M.1    Kono, J.2    Yamada, H.3    Misawa, T.4    Tanaka, M.5    Nakatsuka, T.6
  • 67
    • 84878956207 scopus 로고    scopus 로고
    • AG10 inhibits amyloidogenesis and cellular toxicity of the familial amyloid cardiomyopathy-associated V122I transthyretin
    • Penchala SC, Connelly S, Wang Y, Park MS, Zhao L, Baranczak A, et al., AG10 inhibits amyloidogenesis and cellular toxicity of the familial amyloid cardiomyopathy-associated V122I transthyretin. Proc Natl Acad Sci U S A 2013; 110: 9992-7.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 9992-9997
    • Penchala, S.C.1    Connelly, S.2    Wang, Y.3    Park, M.S.4    Zhao, L.5    Baranczak, A.6
  • 68
    • 84861421529 scopus 로고    scopus 로고
    • The transthyretin amyloidoses: From delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug
    • Johnson SM, Connelly S, Fearns C, Powers ET, Kelly JW., The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug. J Mol Biol 2012; 421: 185-203.
    • (2012) J Mol Biol , vol.421 , pp. 185-203
    • Johnson, S.M.1    Connelly, S.2    Fearns, C.3    Powers, E.T.4    Kelly, J.W.5
  • 69
    • 84890954073 scopus 로고    scopus 로고
    • Repurposing diflunisal for familial amyloid polyneuropathy: A randomized clinical trial
    • Berk JL, Suhr OB, Obici L, Sekijima Y, Zeldenrust SR, Yamashita T, et al., Repurposing diflunisal for familial amyloid polyneuropathy: a randomized clinical trial. JAMA 2013; 310: 2658-67.
    • (2013) JAMA , vol.310 , pp. 2658-2667
    • Berk, J.L.1    Suhr, O.B.2    Obici, L.3    Sekijima, Y.4    Zeldenrust, S.R.5    Yamashita, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.