메뉴 건너뛰기




Volumn 5, Issue 1, 2003, Pages 33-40

Advanced glycation endproducts and osteoarthritis

Author keywords

Articular Cartilage; Human Articular Cartilage; Pentosidine; Proteoglycan Synthesis; Synovial Fluid

Indexed keywords

ADVANCED GLYCATION END PRODUCT; ADVANCED GLYCOSYLATION END PRODUCT RECEPTOR; ADVANCED GLYCOSYLATION END-PRODUCT RECEPTOR; IMMUNOGLOBULIN RECEPTOR;

EID: 0038622976     PISSN: 15233774     EISSN: 15346307     Source Type: Journal    
DOI: 10.1007/s11926-003-0081-x     Document Type: Article
Times cited : (60)

References (60)
  • 1
    • 0028783940 scopus 로고
    • The incidence and natural history of knee osteoarthritis in the elderly. The Framingham Osteoarthritis Study
    • PID: 7575700, COI: 1:STN:280:DyaK28%2FhslCnug%3D%3D
    • Felson DT, Zhang Y, Hannan MT, et al.: The incidence and natural history of knee osteoarthritis in the elderly. The Framingham Osteoarthritis Study. Arthritis Rheum 1995, 38:1500–1555. DOI: 10.1002/art.1780381017
    • (1995) Arthritis Rheum , vol.38 , pp. 1500-1555
    • Felson, D.T.1    Zhang, Y.2    Hannan, M.T.3
  • 2
    • 0025773098 scopus 로고
    • Obesity and osteoarthritis of the knee: evidence from the National Health and Nutrition Examination Survey (NHANES I)
    • PID: 2287947, COI: 1:STN:280:DyaK3M7kt1Oqtg%3D%3D
    • Davis MA, Ettinger WH, Neuhaus JM: Obesity and osteoarthritis of the knee: evidence from the National Health and Nutrition Examination Survey (NHANES I). Semin Arthritis Rheum 1990, 20(suppl):34–41. DOI: 10.1016/0049-0172(90)90045-H
    • (1990) Semin Arthritis Rheum , vol.20 , pp. 34-41
    • Davis, M.A.1    Ettinger, W.H.2    Neuhaus, J.M.3
  • 3
    • 0028265929 scopus 로고
    • Quantitative analysis of crosslinks pyridinoline and pentosidine in articular cartilage of patients with bone and joint disorders
    • PID: 8185700, COI: 1:STN:280:DyaK2c3kt1WhtA%3D%3D
    • Takahashi M, Kushida K, Ohishi T, et al.: Quantitative analysis of crosslinks pyridinoline and pentosidine in articular cartilage of patients with bone and joint disorders. Arthritis Rheum 1994, 37:724–728. DOI: 10.1002/art.1780370517
    • (1994) Arthritis Rheum , vol.37 , pp. 724-728
    • Takahashi, M.1    Kushida, K.2    Ohishi, T.3
  • 4
    • 0036164004 scopus 로고    scopus 로고
    • Crosslinking by advanced glycation end products increases the stiffness of the collagen network in human articular cartilage: a possible mechanism through which age is a risk factor for osteoarthritis
    • PID: 11822407, COI: 1:CAS:528:DC%2BD38Xht1Wlu70%3D, vitro incubation of articular cartilage with ribose or threose increases its AGE content and stiffness
    • Verzijl N, DeGroot J, Ben ZC, et al.: Crosslinking by advanced glycation end products increases the stiffness of the collagen network in human articular cartilage: a possible mechanism through which age is a risk factor for osteoarthritis. Arthritis Rheum 2002, 46:114–123. In vitro incubation of articular cartilage with ribose or threose increases its AGE content and stiffness. DOI: 10.1002/1529-0131(200201)46:1<114::AID-ART10025>3.0.CO;2-P
    • (2002) Arthritis Rheum , vol.46 , pp. 114-123
    • Verzijl, N.1    DeGroot, J.2    Ben, Z.C.3
  • 5
    • 0001430544 scopus 로고
    • Accelerated age-related browning of human collagen in diabetes mellitus
    • PID: 6582514, COI: 1:CAS:528:DyaL2cXhtFyrurs%3D
    • Monnier VM, Kohn RR, Cerami A: Accelerated age-related browning of human collagen in diabetes mellitus. Proc Natl Acad Sci U S A 1984, 81:583–587. DOI: 10.1073/pnas.81.2.583
    • (1984) Proc Natl Acad Sci U S A , vol.81 , pp. 583-587
    • Monnier, V.M.1    Kohn, R.R.2    Cerami, A.3
  • 6
    • 0028272883 scopus 로고
    • Pathogenic effects of advanced glycosylation: biochemical, biologic, and clinical implications for diabetes and aging
    • PID: 8139257, COI: 1:CAS:528:DyaK2cXksFCksLg%3D
    • Vlassara H, Bucala R, Striker L: Pathogenic effects of advanced glycosylation: biochemical, biologic, and clinical implications for diabetes and aging. Lab Invest 1994, 70:138–151.
    • (1994) Lab Invest , vol.70 , pp. 138-151
    • Vlassara, H.1    Bucala, R.2    Striker, L.3
  • 7
    • 0025930287 scopus 로고
    • Oxidative glycation and free radical production: a causal mechanism of diabetic complications
    • PID: 1649079
    • Hunt JV, Wolff SP: Oxidative glycation and free radical production: a causal mechanism of diabetic complications. Free Radic Res Commun 1991, 12:115–123.
    • (1991) Free Radic Res Commun , vol.12 , pp. 115-123
    • Hunt, J.V.1    Wolff, S.P.2
  • 8
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • PID: 11742414, COI: 1:CAS:528:DC%2BD38Xhtlyltg%3D%3D
    • Brownlee M: Biochemistry and molecular cell biology of diabetic complications. Nature 2001, 414:813–820. DOI: 10.1038/414813a
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 9
    • 0030581630 scopus 로고    scopus 로고
    • Rapid formation of advanced glycation end products by intermediate metabolites of glycolytic pathway and polyol pathway
    • Hamada Y, Araki N, Koh N, et al.: Rapid formation of advanced glycation end products by intermediate metabolites of glycolytic pathway and polyol pathway. Biochem Biophys Res Commun 2003, 228:539–543. DOI: 10.1006/bbrc.1996.1695
    • (2003) Biochem Biophys Res Commun , vol.228 , pp. 539-543
    • Hamada, Y.1    Araki, N.2    Koh, N.3
  • 11
    • 0034893715 scopus 로고    scopus 로고
    • The role of AGEs in aging: causation or correlation
    • PID: 11525875, COI: 1:CAS:528:DC%2BD3MXmt1Kktr0%3D
    • Baynes JW: The role of AGEs in aging: causation or correlation. Exp Gerontol 2001, 36:1527–1537. DOI: 10.1016/S0531-5565(01)00138-3
    • (2001) Exp Gerontol , vol.36 , pp. 1527-1537
    • Baynes, J.W.1
  • 12
    • 0019870473 scopus 로고
    • Kinetic analysis of the nonenzymatic glycosylation of hemoglobin
    • PID: 7228877, COI: 1:CAS:528:DyaL3MXktVahsrc%3D
    • Higgins PJ, Bunn HF: Kinetic analysis of the nonenzymatic glycosylation of hemoglobin. J Biol Chem 1981, 256:5204–5208.
    • (1981) J Biol Chem , vol.256 , pp. 5204-5208
    • Higgins, P.J.1    Bunn, H.F.2
  • 13
    • 0027160460 scopus 로고
    • Accumulation of Maillard reaction products in skin collagen in diabetes and aging
    • PID: 8514858, COI: 1:CAS:528:DyaK3sXltlKkt7g%3D
    • Dyer DG, Dunn JA, Thorpe SR, et al.: Accumulation of Maillard reaction products in skin collagen in diabetes and aging. J Clin Invest 1993, 91:2463–2469.
    • (1993) J Clin Invest , vol.91 , pp. 2463-2469
    • Dyer, D.G.1    Dunn, J.A.2    Thorpe, S.R.3
  • 14
    • 0028286374 scopus 로고
    • Reactive glycosylation endproducts in diabetic uraemia and treatment of renal failure
    • PID: 7911868, COI: 1:STN:280:DyaK2c3ns1KktA%3D%3D
    • Makita Z, Bucala R, Rayfield EJ, et al.: Reactive glycosylation endproducts in diabetic uraemia and treatment of renal failure. Lancet 1994, 343:1519–1522. DOI: 10.1016/S0140-6736(94)92935-1
    • (1994) Lancet , vol.343 , pp. 1519-1522
    • Makita, Z.1    Bucala, R.2    Rayfield, E.J.3
  • 15
    • 0034671714 scopus 로고    scopus 로고
    • Effect of collagen turnover on the accumulation of advanced glycation end products
    • PID: 10976109, COI: 1:CAS:528:DC%2BD3cXptFSkurY%3D
    • Verzijl N, DeGroot J, Thorpe SR, et al.: Effect of collagen turnover on the accumulation of advanced glycation end products. J Biol Chem 2000, 275:39027–39031. DOI: 10.1074/jbc.M006700200
    • (2000) J Biol Chem , vol.275 , pp. 39027-39031
    • Verzijl, N.1    DeGroot, J.2    Thorpe, S.R.3
  • 16
    • 0029882670 scopus 로고    scopus 로고
    • The mechanism of collagen cross-linking in diabetes: a puzzle nearing resolution
    • Monnier VM, Glomb M, Elgawish A, Sell DR: The mechanism of collagen cross-linking in diabetes: a puzzle nearing resolution. Diabetes 2003, 45(suppl):S67-S72.
    • (2003) Diabetes , vol.45 , pp. S67-S72
    • Monnier, V.M.1    Glomb, M.2    Elgawish, A.3    Sell, D.R.4
  • 17
    • 0031766932 scopus 로고    scopus 로고
    • Glycation changes the charge distribution of type I collagen fibrils
    • PID: 9870360, COI: 1:CAS:528:DyaK1MXitFKn
    • Hadley JC, Meek KM, Malik NS: Glycation changes the charge distribution of type I collagen fibrils. Glycoconj J 1998, 15:835–840. DOI: 10.1023/A:1006928403140
    • (1998) Glycoconj J , vol.15 , pp. 835-840
    • Hadley, J.C.1    Meek, K.M.2    Malik, N.S.3
  • 18
    • 0030964857 scopus 로고    scopus 로고
    • Interaction between beta 2- microglobulin and advanced glycation end products in the development of dialysis related-amyloidosis
    • PID: 9150467, COI: 1:CAS:528:DyaK2sXjsFShtLs%3D
    • Hou FF, Chertow GM, Kay J, et al.: Interaction between beta 2- microglobulin and advanced glycation end products in the development of dialysis related-amyloidosis. Kidney Int 1997, 51:1514–1519. DOI: 10.1038/ki.1997.208
    • (1997) Kidney Int , vol.51 , pp. 1514-1519
    • Hou, F.F.1    Chertow, G.M.2    Kay, J.3
  • 19
    • 0032489290 scopus 로고    scopus 로고
    • Increased pentosidine, an advanced glycation end product, in plasma and synovial fluid from patients with rheumatoid arthritis and its relation with inflammatory markers
    • PID: 9514872, COI: 1:CAS:528:DyaK1cXhslCmur0%3D
    • Miyata T, Ishiguro N, Yasuda Y, et al.: Increased pentosidine, an advanced glycation end product, in plasma and synovial fluid from patients with rheumatoid arthritis and its relation with inflammatory markers. Biochem Biophys Res Commun 1998, 244:45–49. DOI: 10.1006/bbrc.1998.8203
    • (1998) Biochem Biophys Res Commun , vol.244 , pp. 45-49
    • Miyata, T.1    Ishiguro, N.2    Yasuda, Y.3
  • 20
    • 0005649096 scopus 로고    scopus 로고
    • Pentosidine in synovial fluid in osteoarthritis and rheumatoid arthritis: relationship with disease activity in rheumatoid arthritis
    • PID: 9858442, COI: 1:CAS:528:DyaK1MXhsVKn
    • Chen JR, Takahashi M, Suzuki M, et al.: Pentosidine in synovial fluid in osteoarthritis and rheumatoid arthritis: relationship with disease activity in rheumatoid arthritis. J Rheumatol 1998, 25:2440–2444.
    • (1998) J Rheumatol , vol.25 , pp. 2440-2444
    • Chen, J.R.1    Takahashi, M.2    Suzuki, M.3
  • 21
    • 0032761646 scopus 로고    scopus 로고
    • Comparison of the concentrations of pentosidine in the synovial fluid, serum and urine of patients with rheumatoid arthritis and osteoarthritis
    • PID: 10587559, COI: 1:STN:280:DC%2BD3c%2Fls1Cgsw%3D%3D, Pentosidine is present serum, urine, and synovial fluid but levels are lower patients with OA than those with RA
    • Chen JR, Takahashi M, Suzuki M, et al.: Comparison of the concentrations of pentosidine in the synovial fluid, serum and urine of patients with rheumatoid arthritis and osteoarthritis. Rheumatology 1999, 38:1275–1278. Pentosidine is present in serum, urine, and synovial fluid but levels are lower in patients with OA than in those with RA. DOI: 10.1093/rheumatology/38.12.1275
    • (1999) Rheumatology , vol.38 , pp. 1275-1278
    • Chen, J.R.1    Takahashi, M.2    Suzuki, M.3
  • 22
    • 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 nonenzymatic glycation affects biomechanical properties of cartilage
    • PID: 9461529, COI: 1:CAS:528:DyaK1cXhs12jsrY%3D
    • Bank RA, Bayliss MT, Lafeber FP, et al.: Ageing and zonal variation in post-translational modification of collagen in normal human articular cartilage: the age-related increase in nonenzymatic glycation affects biomechanical properties of cartilage. Biochem J 1998, 330:345–351.
    • (1998) Biochem J , vol.330 , pp. 345-351
    • Bank, R.A.1    Bayliss, M.T.2    Lafeber, F.P.3
  • 23
    • 0031955304 scopus 로고    scopus 로고
    • The effect of aging and osteoarthritis on the mature and senescent cross-links of collagen in human meniscus
    • PID: 9620647, COI: 1:STN:280:DyaK1c3otF2luw%3D%3D
    • Takahashi M, Suzuki M, Kushida K, et al.: The effect of aging and osteoarthritis on the mature and senescent cross-links of collagen in human meniscus. Arthroscopy 1998, 14:366–372. DOI: 10.1016/S0749-8063(98)70003-9
    • (1998) Arthroscopy , vol.14 , pp. 366-372
    • Takahashi, M.1    Suzuki, M.2    Kushida, K.3
  • 24
    • 0036154138 scopus 로고    scopus 로고
    • Putative role of lysyl hydroxylation and pyridinoline cross-linking during adolescence in the occurrence of osteoarthritis at old age
    • PID: 11869072, COI: 1:STN:280:DC%2BD387jt1OmtA%3D%3D
    • Bank RA, Verzijl N, Lafeber FP, Tekoppele JM: Putative role of lysyl hydroxylation and pyridinoline cross-linking during adolescence in the occurrence of osteoarthritis at old age. Osteoarthritis Cartilage 2002, 10:127–134. DOI: 10.1053/joca.2001.0487
    • (2002) Osteoarthritis Cartilage , vol.10 , pp. 127-134
    • Bank, R.A.1    Verzijl, N.2    Lafeber, F.P.3    Tekoppele, J.M.4
  • 25
    • 0035003348 scopus 로고    scopus 로고
    • Degradation of the cartilage collagen matrix associated with changes in chondrocytes in osteoarthrosis: assessment by loss of background fluorescence and immunodetection of matrix components
    • PID: 11332618, COI: 1:CAS:528:DC%2BD3MXjvVChtLY%3D, This study uses background fluorescence to measure total AGE content articular cartilage from individuals with OA and demonstrates decreased fluorescence around chondrocytes
    • Gibson GJ, Verner JJ, Nelson FR, Lin DL: Degradation of the cartilage collagen matrix associated with changes in chondrocytes in osteoarthrosis: assessment by loss of background fluorescence and immunodetection of matrix components. J Orthop Res 2001, 19:33–42. This study uses background fluorescence to measure total AGE content in articular cartilage from individuals with OA and demonstrates decreased fluorescence around chondrocytes. DOI: 10.1016/S0736-0266(00)00008-5
    • (2001) J Orthop Res , vol.19 , pp. 33-42
    • Gibson, G.J.1    Verner, J.J.2    Nelson, F.R.3    Lin, D.L.4
  • 26
    • 0032910459 scopus 로고    scopus 로고
    • Age-related decrease in proteoglycan synthesis of human articular chondrocytes: the role of nonenzymatic glycation
    • PID: 10323457, COI: 1:STN:280:DyaK1M3lsFSgtA%3D%3D, Pentosidine levels articular cartilage increase linearly with chronologic aging. Proteoglycan synthesis decreases articular cartilage after vitro incubation with ribose and correlates with an increase pentosidine content
    • DeGroot J, Verzijl N, Bank RA, et al.: Age-related decrease in proteoglycan synthesis of human articular chondrocytes: the role of nonenzymatic glycation. Arthritis Rheum 1999, 42:1003–1009. Pentosidine levels in articular cartilage increase linearly with chronologic aging. Proteoglycan synthesis decreases in articular cartilage after in vitro incubation with ribose and correlates with an increase in pentosidine content. DOI: 10.1002/1529-0131(199905)42:5<1003::AID-ANR20>3.0.CO;2-K
    • (1999) Arthritis Rheum , vol.42 , pp. 1003-1009
    • DeGroot, J.1    Verzijl, N.2    Bank, R.A.3
  • 27
    • 0028910233 scopus 로고
    • Lysyl oxidase and Maillard reaction-mediated crosslinks in aging and osteoarthritic rabbit cartilage
    • PID: 7853094, COI: 1:CAS:528:DyaK2MXktlylu7k%3D
    • Pokharna HK, Monnier V, Boja B, Moskowitz RW: Lysyl oxidase and Maillard reaction-mediated crosslinks in aging and osteoarthritic rabbit cartilage. J Orthop Res 1995, 13:13–21. DOI: 10.1002/jor.1100130105
    • (1995) J Orthop Res , vol.13 , pp. 13-21
    • Pokharna, H.K.1    Monnier, V.2    Boja, B.3    Moskowitz, R.W.4
  • 28
    • 0025853743 scopus 로고
    • Age-dependent accumulation of N epsilon-(carboxymethyl)lysine and N epsilon- (carboxymethyl)hydroxylysine in human skin collagen
    • PID: 1899338, COI: 1:CAS:528:DyaK3MXlvFCmug%3D%3D
    • Dunn JA, McCance DR, Thorpe SR, et al.: Age-dependent accumulation of N epsilon-(carboxymethyl)lysine and N epsilon- (carboxymethyl)hydroxylysine in human skin collagen. Biochemistry 1991, 30:1205–1210. DOI: 10.1021/bi00219a007
    • (1991) Biochemistry , vol.30 , pp. 1205-1210
    • Dunn, J.A.1    McCance, D.R.2    Thorpe, S.R.3
  • 29
    • 0024377756 scopus 로고
    • Some biochemical and biophysical parameters for the study of the pathogenesis of osteoarthritis: a comparison between the processes of aging and degeneration in human hip cartilage
    • PID: 2805680, COI: 1:STN:280:DyaK3c%2FjtFGmsg%3D%3D
    • Grushko G, Schneiderman R, Maroudas A: Some biochemical and biophysical parameters for the study of the pathogenesis of osteoarthritis: a comparison between the processes of aging and degeneration in human hip cartilage. Connect Tissue Res 1989, 19:149–176.
    • (1989) Connect Tissue Res , vol.19 , pp. 149-176
    • Grushko, G.1    Schneiderman, R.2    Maroudas, A.3
  • 30
    • 0035159518 scopus 로고    scopus 로고
    • Accumulation of advanced glycation endproducts reduces chondrocyte-mediated extracellular matrix turnover in human articular cartilage
    • PID: 11795991, COI: 1:STN:280:DC%2BD38%2FmvVyltw%3D%3D, Both proteoglycan synthesis and chondrocyte-mediated cartilage degradation decrease after human articular cartilage has been AGE-modified by incubation with reducing sugars
    • DeGroot J, Verzijl N, Jacobs KM, et al.: Accumulation of advanced glycation endproducts reduces chondrocyte-mediated extracellular matrix turnover in human articular cartilage. Osteoarthritis Cartilage 2001, 9:720–726. Both proteoglycan synthesis and chondrocyte-mediated cartilage degradation decrease after human articular cartilage has been AGE-modified by incubation with reducing sugars. DOI: 10.1053/joca.2001.0469
    • (2001) Osteoarthritis Cartilage , vol.9 , pp. 720-726
    • DeGroot, J.1    Verzijl, N.2    Jacobs, K.M.3
  • 31
    • 0035157665 scopus 로고    scopus 로고
    • Age-related decrease in susceptibility of human articular cartilage to matrix metalloproteinase-mediated degradation: the role of advanced glycation end products
    • PID: 11710713, COI: 1:CAS:528:DC%2BD38XpslY%3D, Glycosaminoglycan release from normal human articular cartilage, after vitro incubation with synovial fluid obtained from patients with RA or OA, is decreased proportional to the pentosidine content of the cartilage and is independent of the cartilage donor’s chronologic age
    • DeGroot J, Verzijl N, Wenting-Van Wijk MJ, et al.: Age-related decrease in susceptibility of human articular cartilage to matrix metalloproteinase-mediated degradation: the role of advanced glycation end products. Arthritis Rheum 2001, 44:2562–2571. Glycosaminoglycan release from normal human articular cartilage, after in vitro incubation with synovial fluid obtained from patients with RA or OA, is decreased proportional to the pentosidine content of the cartilage and is independent of the cartilage donor’s chronologic age. DOI: 10.1002/1529-0131(200111)44:11<2562::AID-ART437>3.0.CO;2-1
    • (2001) Arthritis Rheum , vol.44 , pp. 2562-2571
    • DeGroot, J.1    Verzijl, N.2    Wenting-Van Wijk, M.J.3
  • 32
    • 0030859290 scopus 로고    scopus 로고
    • Activation of the receptor for advanced glycation end products triggers a p21(ras)-dependent mitogen-activated protein kinase pathway regulated by oxidant stress
    • PID: 9211935, COI: 1:CAS:528:DyaK2sXksFyjsbc%3D
    • Lander HM, Tauras JM, Ogiste JS, et al.: Activation of the receptor for advanced glycation end products triggers a p21(ras)-dependent mitogen-activated protein kinase pathway regulated by oxidant stress. J Biol Chem 1997, 272:17810–17814. DOI: 10.1074/jbc.272.28.17810
    • (1997) J Biol Chem , vol.272 , pp. 17810-17814
    • Lander, H.M.1    Tauras, J.M.2    Ogiste, J.S.3
  • 33
    • 0028304625 scopus 로고
    • Enhanced cellular oxidant stress by the interaction of advanced glycation end products with their receptors/binding proteins
    • PID: 8144582, COI: 1:CAS:528:DyaK2cXis1Ogsrg%3D
    • Yan SD, Schmidt AM, Anderson GM, et al.: Enhanced cellular oxidant stress by the interaction of advanced glycation end products with their receptors/binding proteins. J Biol Chem 1994, 269:9889–9897.
    • (1994) J Biol Chem , vol.269 , pp. 9889-9897
    • Yan, S.D.1    Schmidt, A.M.2    Anderson, G.M.3
  • 34
    • 0029882671 scopus 로고    scopus 로고
    • RAGE: a novel cellular receptor for advanced glycation end products
    • Schmidt AM, Hori O, Cao R, et al.: RAGE: a novel cellular receptor for advanced glycation end products. Diabetes 2003 45(suppl):S77-S80.
    • (2003) Diabetes , vol.45 , pp. S77-S80
    • Schmidt, A.M.1    Hori, O.2    Cao, R.3
  • 35
    • 0029366113 scopus 로고
    • Identification of galectin-3 as a high-affinity binding protein for advanced glycation end products (AGE): a new member of the AGE-receptor complex
    • PID: 8529130, COI: 1:CAS:528:DyaK2MXpsVClsrs%3D
    • Vlassara H, Li YM, Imani F, et al.: Identification of galectin-3 as a high-affinity binding protein for advanced glycation end products (AGE): a new member of the AGE-receptor complex. Mol Med 1995, 1:634–646.
    • (1995) Mol Med , vol.1 , pp. 634-646
    • Vlassara, H.1    Li, Y.M.2    Imani, F.3
  • 36
    • 85131832569 scopus 로고    scopus 로고
    • The advanced glycosylation endproduct binding protein AGE-R3 (galectin-3) is present in synovial tissues from patients with b2m amyloidosis [abstract]
    • Kay J, Hou F-F, Quigley C, et al.: The advanced glycosylation endproduct binding protein AGE-R3 (galectin-3) is present in synovial tissues from patients with b2m amyloidosis [abstract]. Arthritis Rheum 1999, 42(suppl):S159.
    • (1999) Arthritis Rheum , vol.42 , pp. S159
    • Kay, J.1    Hou, F.-F.2    Quigley, C.3
  • 37
    • 85131836945 scopus 로고    scopus 로고
    • Galectin-3 and galectin- 3 binding protein are up-regulated in rheumatoid arthritis and contribute to joint destruction [abstract]
    • Oshima S, Kuchen S, Seemayer CA, et al.: Galectin-3 and galectin- 3 binding protein are up-regulated in rheumatoid arthritis and contribute to joint destruction [abstract]. Arthritis Rheum 2002, 46(suppl):S502.
    • (2002) Arthritis Rheum , vol.46 , pp. S502
    • Oshima, S.1    Kuchen, S.2    Seemayer, C.A.3
  • 38
    • 4243679423 scopus 로고    scopus 로고
    • Galectin-3 is expressed on the surface of adult chondrocytes. What’s for? [abstract]
    • Reboul PY, Boileau C, Guévremont M, et al.: Galectin-3 is expressed on the surface of adult chondrocytes. What’s for? [abstract]. Arthritis Rheum 2002, 46(suppl):S86.
    • (2002) Arthritis Rheum , vol.46 , pp. S86
    • Reboul, P.Y.1    Boileau, C.2    Guévremont, M.3
  • 39
    • 0033863012 scopus 로고    scopus 로고
    • Role of galectin-3 as a receptor for advanced glycosylation end products
    • PID: 10997688, COI: 1:CAS:528:DC%2BD3cXms1Oiurg%3D
    • Pricci F, Leto G, Amadio L, et al.: Role of galectin-3 as a receptor for advanced glycosylation end products. Kidney Int Suppl 2000, 77:S31-S39. DOI: 10.1046/j.1523-1755.2000.07706.x
    • (2000) Kidney Int Suppl , vol.77 , pp. S31-S39
    • Pricci, F.1    Leto, G.2    Amadio, L.3
  • 40
    • 17644434954 scopus 로고    scopus 로고
    • The diabetic milieu modulates the advanced glycation end product-receptor complex in the mesangium by inducing or upregulating galectin-3 expression
    • PID: 10909985, COI: 1:CAS:528:DC%2BD3cXkslOqt7c%3D
    • Pugliese G, Pricci F, Leto G, et al.: The diabetic milieu modulates the advanced glycation end product-receptor complex in the mesangium by inducing or upregulating galectin-3 expression. Diabetes 2000, 49:1249–1257. DOI: 10.2337/diabetes.49.7.1249
    • (2000) Diabetes , vol.49 , pp. 1249-1257
    • Pugliese, G.1    Pricci, F.2    Leto, G.3
  • 41
    • 0033599504 scopus 로고    scopus 로고
    • Characterization of the advanced glycation end-product receptor complex in human vascular endothelial cells
    • PID: 10080935, COI: 1:CAS:528:DyaK1MXhvVaht7c%3D
    • Stitt AW, He C, Vlassara H: Characterization of the advanced glycation end-product receptor complex in human vascular endothelial cells. Biochem Biophys Res Commun 1999, 256:549–556. DOI: 10.1006/bbrc.1999.0291
    • (1999) Biochem Biophys Res Commun , vol.256 , pp. 549-556
    • Stitt, A.W.1    He, C.2    Vlassara, H.3
  • 42
    • 0036232299 scopus 로고    scopus 로고
    • Receptor for advanced glycation end products on human synovial fibroblasts: role in the pathogenesis of dialysis-related amyloidosis
    • PID: 11961018, COI: 1:CAS:528:DC%2BD38XktFaitro%3D
    • Hou FF, Jiang JP, Guo JQ, et al.: Receptor for advanced glycation end products on human synovial fibroblasts: role in the pathogenesis of dialysis-related amyloidosis. J Am Soc Nephrol 2002, 13:1296–1306. DOI: 10.1097/01.ASN.0000013702.73570.3B
    • (2002) J Am Soc Nephrol , vol.13 , pp. 1296-1306
    • Hou, F.F.1    Jiang, J.P.2    Guo, J.Q.3
  • 43
    • 0027176945 scopus 로고
    • Regulation of human mononuclear phagocyte migration by cell surface-binding proteins for advanced glycation end products
    • PID: 8387541, COI: 1:CAS:528:DyaK3sXkt1GrsLg%3D
    • Schmidt AM, Yan SD, Brett J, et al.: Regulation of human mononuclear phagocyte migration by cell surface-binding proteins for advanced glycation end products. J Clin Invest 1993, 91:2155–2168.
    • (1993) J Clin Invest , vol.91 , pp. 2155-2168
    • Schmidt, A.M.1    Yan, S.D.2    Brett, J.3
  • 44
    • 0029076397 scopus 로고
    • Non-enzymatically glycated tau in Alzheimer’s disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid beta-peptide
    • PID: 7585153, COI: 1:CAS:528:DyaK2MXms1Kgtr8%3D
    • Yan SD, Yan SF, Chen X, et al.: Non-enzymatically glycated tau in Alzheimer’s disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid beta-peptide. Nat Med 1995, 1:693–699. DOI: 10.1038/nm0795-693
    • (1995) Nat Med , vol.1 , pp. 693-699
    • Yan, S.D.1    Yan, S.F.2    Chen, X.3
  • 45
    • 0023940640 scopus 로고
    • Cachectin/TNF and IL-1 induced by glucose-modified proteins: role in normal tissue remodeling
    • PID: 3259727, COI: 1:CAS:528:DyaL1cXktlKgtLs%3D
    • Vlassara H, Brownlee M, Manogue KR, et al.: Cachectin/TNF and IL-1 induced by glucose-modified proteins: role in normal tissue remodeling. Science 1988, 240:1546–1548. DOI: 10.1126/science.3259727
    • (1988) Science , vol.240 , pp. 1546-1548
    • Vlassara, H.1    Brownlee, M.2    Manogue, K.R.3
  • 46
    • 0028960341 scopus 로고
    • The effect of glucose and advanced glycosylation end products on IL-6 production by human monocytes
    • PID: 7695204, COI: 1:CAS:528:DyaK2MXovVSisrY%3D
    • Morohoshi M, Fujisawa K, Uchimura I, Numano F: The effect of glucose and advanced glycosylation end products on IL-6 production by human monocytes. Ann N Y Acad Sci 1995, 748:562–570. DOI: 10.1111/j.1749-6632.1994.tb17362.x
    • (1995) Ann N Y Acad Sci , vol.748 , pp. 562-570
    • Morohoshi, M.1    Fujisawa, K.2    Uchimura, I.3    Numano, F.4
  • 47
    • 0028364606 scopus 로고
    • Macrophages adhere to glucose-modified basement membrane collagen IV via their scavenger receptors
    • PID: 8144597
    • el Khoury J, Thomas CA, Loike JD, et al.: Macrophages adhere to glucose-modified basement membrane collagen IV via their scavenger receptors. J Biol Chem 1994, 269:10197–10200.
    • (1994) J Biol Chem , vol.269 , pp. 10197-10200
    • el Khoury, J.1    Thomas, C.A.2    Loike, J.D.3
  • 48
    • 0035793602 scopus 로고    scopus 로고
    • Cd36, a member of the class b scavenger receptor family, as a receptor for advanced glycation end products
    • PID: 11035013, COI: 1:CAS:528:DC%2BD3MXhtFWjur8%3D
    • Ohgami N, Nagai R, Ikemoto M, et al.: Cd36, a member of the class b scavenger receptor family, as a receptor for advanced glycation end products. J Biol Chem 2001, 276:3195–3202. DOI: 10.1074/jbc.M006545200
    • (2001) J Biol Chem , vol.276 , pp. 3195-3202
    • Ohgami, N.1    Nagai, R.2    Ikemoto, M.3
  • 49
    • 0000212168 scopus 로고    scopus 로고
    • Pimagedine (PG) reduces progression of retinopathy and lowers lipid levels in patients with type I diabetes mellitus (DM) [abstract]
    • Raskin P, Cattran D, Williams M, et al.: Pimagedine (PG) reduces progression of retinopathy and lowers lipid levels in patients with type I diabetes mellitus (DM) [abstract]. J Am Soc Nephrol 1999, 10:179A.
    • (1999) J Am Soc Nephrol , vol.10 , pp. 179A
    • Raskin, P.1    Cattran, D.2    Williams, M.3
  • 50
    • 0000362052 scopus 로고    scopus 로고
    • Pimagedine (PG) lowers total urinary protein (TUP) and slows progression of overt diabetic nephropathy in patients with type I diabetes mellitus (DM) [abstract]
    • Appel G, Bolton K, Freedman B, et al.: Pimagedine (PG) lowers total urinary protein (TUP) and slows progression of overt diabetic nephropathy in patients with type I diabetes mellitus (DM) [abstract]. J Am Soc Nephrol 1999, 10:153A.
    • (1999) J Am Soc Nephrol , vol.10 , pp. 153A
    • Appel, G.1    Bolton, K.2    Freedman, B.3
  • 51
    • 0035076053 scopus 로고    scopus 로고
    • Downregulation of interleukin 1beta production in human osteoarthritic synovial tissue and cartilage cultures by aminoguanidine
    • PID: 11247871, COI: 1:CAS:528:DC%2BD3MXislylsrg%3D
    • Shirazi I, Yaron I, Wollman Y, et al.: Downregulation of interleukin 1beta production in human osteoarthritic synovial tissue and cartilage cultures by aminoguanidine. Ann Rheum Dis 2001, 60:391–394. DOI: 10.1136/ard.60.4.391
    • (2001) Ann Rheum Dis , vol.60 , pp. 391-394
    • Shirazi, I.1    Yaron, I.2    Wollman, Y.3
  • 52
    • 0022644227 scopus 로고
    • Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking
    • PID: 3487117, COI: 1:CAS:528:DyaL28Xkslantr8%3D
    • Brownlee M, Vlassara H, Kooney A, et al.: Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking. Science 1986, 232:1629–1632. DOI: 10.1126/science.3487117
    • (1986) Science , vol.232 , pp. 1629-1632
    • Brownlee, M.1    Vlassara, H.2    Kooney, A.3
  • 53
    • 0030741590 scopus 로고    scopus 로고
    • Nutrition: risk factors for osteoarthritis
    • PID: 9485998, COI: 1:STN:280:DyaK1c7ks12msA%3D%3D
    • McAlindon T, Felson DT: Nutrition: risk factors for osteoarthritis. Ann Rheum Dis 1997, 56:397–400. DOI: 10.1136/ard.56.7.397
    • (1997) Ann Rheum Dis , vol.56 , pp. 397-400
    • McAlindon, T.1    Felson, D.T.2
  • 54
    • 0029738444 scopus 로고    scopus 로고
    • The receptor for advanced glycation end products (RAGE) is a central mediator of the interaction of AGE-beta2microglobulin with human mononuclear phagocytes via an oxidant-sensitive pathway. Implications for the pathogenesis of dialysis-related amyloidosis
    • Miyata T, Hori O, Zhang J, et al.: The receptor for advanced glycation end products (RAGE) is a central mediator of the interaction of AGE-beta2microglobulin with human mononuclear phagocytes via an oxidant-sensitive pathway. Implications for the pathogenesis of dialysis-related amyloidosis. J Clin Invest 2003, 98:1088–1094. DOI: 10.1172/JCI118889
    • (2003) J Clin Invest , vol.98 , pp. 1088-1094
    • Miyata, T.1    Hori, O.2    Zhang, J.3
  • 55
    • 15844425230 scopus 로고    scopus 로고
    • An agent cleaving glucose- derived protein crosslinks in vitro and in vivo
    • Vasan S, Zhang X, Kapurniotu A, et al.: An agent cleaving glucose- derived protein crosslinks in vitro and in vivo. Nature 2003, 382:275–278. DOI: 10.1038/382275a0
    • (2003) Nature , vol.382 , pp. 275-278
    • Vasan, S.1    Zhang, X.2    Kapurniotu, A.3
  • 56
    • 0032515986 scopus 로고    scopus 로고
    • Breakers of advanced glycation end products restore large artery properties in experimental diabetes
    • PID: 9539789, COI: 1:CAS:528:DyaK1cXis1Ogsb0%3D
    • Wolffenbuttel BH, Boulanger CM, Crijns FR, et al.: Breakers of advanced glycation end products restore large artery properties in experimental diabetes. Proc Natl Acad Sci U S A 1998, 95:4630–4634. DOI: 10.1073/pnas.95.8.4630
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 4630-4634
    • Wolffenbuttel, B.H.1    Boulanger, C.M.2    Crijns, F.R.3
  • 57
    • 0034646372 scopus 로고    scopus 로고
    • An advanced glycation endproduct cross-link breaker can reverse age-related increases in myocardial stiffness
    • PID: 10706607, COI: 1:CAS:528:DC%2BD3cXitVahsb4%3D
    • Asif M, Egan J, Vasan S, et al.: An advanced glycation endproduct cross-link breaker can reverse age-related increases in myocardial stiffness. Proc Natl Acad Sci U S A 2000, 97:2809–2813. DOI: 10.1073/pnas.040558497
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 2809-2813
    • Asif, M.1    Egan, J.2    Vasan, S.3
  • 58
    • 0035970120 scopus 로고    scopus 로고
    • A cross-link breaker has sustained effects on arterial and ventricular properties in older rhesus monkeys
    • PID: 11158613, COI: 1:CAS:528:DC%2BD3MXht1SmtrY%3D
    • Vaitkevicius PV, Lane M, Spurgeon H, et al.: A cross-link breaker has sustained effects on arterial and ventricular properties in older rhesus monkeys. Proc Natl Acad Sci U S A 2001, 98:1171–1175. DOI: 10.1073/pnas.98.3.1171
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 1171-1175
    • Vaitkevicius, P.V.1    Lane, M.2    Spurgeon, H.3
  • 59
    • 0035949502 scopus 로고    scopus 로고
    • Improved arterial compliance by a novel advanced glycation endproduct crosslink breaker
    • PID: 11571237, COI: 1:CAS:528:DC%2BD3MXnvVeqtLY%3D
    • Kass DA, Shapiro EP, Kawaguchi M, et al.: Improved arterial compliance by a novel advanced glycation endproduct crosslink breaker. Circulation 2001, 104:1464–1470.
    • (2001) Circulation , vol.104 , pp. 1464-1470
    • Kass, D.A.1    Shapiro, E.P.2    Kawaguchi, M.3
  • 60
    • 0036167208 scopus 로고    scopus 로고
    • Diabetes and advanced glycation endproducts
    • PID: 11905595, COI: 1:CAS:528:DC%2BD38XitVChsro%3D
    • Vlassara H, Palace MR: Diabetes and advanced glycation endproducts. J Intern Med 2002, 251:87–101. DOI: 10.1046/j.1365-2796.2002.00932.x
    • (2002) J Intern Med , vol.251 , pp. 87-101
    • Vlassara, H.1    Palace, M.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.