메뉴 건너뛰기




Volumn 13, Issue 1, 2005, Pages 93-101

Migration of keratinocytes is impaired on glycated collagen I

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN TYPE 1; VERY LATE ACTIVATION ANTIGEN 2;

EID: 13844274937     PISSN: 10671927     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1067-1927.2005.130112.x     Document Type: Article
Times cited : (28)

References (44)
  • 3
    • 0026555835 scopus 로고
    • The distribution and severity of diabetic foot disease: A community study with comparison to a non-diabetic group
    • Walters DP, Gatling W, Mullee MA, Hill RD. The distribution and severity of diabetic foot disease: a community study with comparison to a non-diabetic group. Diabet Med 1992;9:354-8.
    • (1992) Diabet Med , vol.9 , pp. 354-358
    • Walters, D.P.1    Gatling, W.2    Mullee, M.A.3    Hill, R.D.4
  • 4
    • 0035990790 scopus 로고    scopus 로고
    • Cutaneous manifestations of diabetes mellitus
    • Ferringer T, Miller F 3rd. Cutaneous manifestations of diabetes mellitus. Dermatol Clin 2002;20:483-92.
    • (2002) Dermatol Clin , vol.20 , pp. 483-492
    • Ferringer, T.1    Miller III, F.2
  • 5
    • 0019972240 scopus 로고
    • The cutaneous manifestations of diabetes mellitus
    • Huntley AC. The cutaneous manifestations of diabetes mellitus. J Am Acad Dermatol 1982;7:427-55.
    • (1982) J Am Acad Dermatol , vol.7 , pp. 427-455
    • Huntley, A.C.1
  • 6
    • 0034523160 scopus 로고    scopus 로고
    • Characterization of glucose transport system in keratinocytes, insulin and IGF-1 differentially affect specific transporters
    • Shen S, Wertheimer E, Sampson SR, Tennenbaum T. Characterization of glucose transport system in keratinocytes, insulin and IGF-1 differentially affect specific transporters. J Invest Dermatol 2000;115:949-54.
    • (2000) J Invest Dermatol , vol.115 , pp. 949-954
    • Shen, S.1    Wertheimer, E.2    Sampson, S.R.3    Tennenbaum, T.4
  • 10
  • 11
    • 0021804647 scopus 로고
    • Nonenzymatic glycation of fibronectin and alterations in the molecular association of cell matrix and basement membrane components in diabetes mellitus
    • Tarsio JF, Wigness B, Rhode TD, Rupp WM, Buchwald H, Furcht LT. Nonenzymatic glycation of fibronectin and alterations in the molecular association of cell matrix and basement membrane components in diabetes mellitus. Diabetes 1985;34:477-84.
    • (1985) Diabetes , vol.34 , pp. 477-484
    • Tarsio, J.F.1    Wigness, B.2    Rhode, T.D.3    Rupp, W.M.4    Buchwald, H.5    Furcht, L.T.6
  • 12
    • 0025939381 scopus 로고
    • Decrease in skin collagen glycation with improved glycemic control in patients with insulin-dependent diabetes mellitus
    • Lyons TJ, Bailie KE, Dyer DG, Dunn JA, Baynes JW. Decrease in skin collagen glycation with improved glycemic control in patients with insulin-dependent diabetes mellitus. J Clin Invest 1991;87:1910-5.
    • (1991) J Clin Invest , vol.87 , pp. 1910-1915
    • Lyons, T.J.1    Bailie, K.E.2    Dyer, D.G.3    Dunn, J.A.4    Baynes, J.W.5
  • 14
    • 0032997958 scopus 로고    scopus 로고
    • Skin collagen glycation, glycoxidation, and crosslinking are lower in subjects with long-term intensive versus conventional therapy of type 1 diabetes: Relevance of glycated collagen products versus HbA1c as markers of diabetic complications
    • DCCT skin collagen ancillary study group. Diabetes control and complications trial.
    • Monnier VM, Bautista O, Kenny D, Sell DR, Fogarty J, Dahms W, Cleary PA, Lachin J, Genuth S. Skin collagen glycation, glycoxidation, and crosslinking are lower in subjects with long-term intensive versus conventional therapy of type 1 diabetes: relevance of glycated collagen products versus HbA1c as markers of diabetic complications. DCCT skin collagen ancillary study group. Diabetes control and complications trial. Diabetes 1999;48:870-80.
    • (1999) Diabetes , vol.48 , pp. 870-880
    • Monnier, V.M.1    Bautista, O.2    Kenny, D.3    Sell, D.R.4    Fogarty, J.5    Dahms, W.6    Cleary, P.A.7    Lachin, J.8    Genuth, S.9
  • 15
    • 0030477949 scopus 로고    scopus 로고
    • Glycation of collagen, the basis of its central role in the late complications of ageing and diabetes
    • Paul RG, Bailey AJ. Glycation of collagen, the basis of its central role in the late complications of ageing and diabetes. Int J Biochem Cell Biol 1996;28:1297-310.
    • (1996) Int J Biochem Cell Biol , vol.28 , pp. 1297-1310
    • Paul, R.G.1    Bailey, A.J.2
  • 16
    • 0031977631 scopus 로고    scopus 로고
    • Nonenzymatic glycation of collagen in aging and diabetes
    • Reiser KM. Nonenzymatic glycation of collagen in aging and diabetes. Proc Soc Exp Biol Medical 1998;218:23-37.
    • (1998) Proc Soc Exp Biol Medical , vol.218 , pp. 23-37
    • Reiser, K.M.1
  • 17
    • 0028980749 scopus 로고
    • Improved metabolic control in patients with non-insulin-dependent diabetes mellitus is associated with a slower accumulation of glycation products in collagen
    • Salmela PI, Oikarinen AI, Ukkola O, Karjalainen A, Linnaluoto M, Puukka R, Ryhanen L. Improved metabolic control in patients with non-insulin-dependent diabetes mellitus is associated with a slower accumulation of glycation products in collagen. Eur J Clin Invest 1995;25:494-500.
    • (1995) Eur J Clin Invest , vol.25 , pp. 494-500
    • Salmela, P.I.1    Oikarinen, A.I.2    Ukkola, O.3    Karjalainen, A.4    Linnaluoto, M.5    Puukka, R.6    Ryhanen, L.7
  • 18
    • 0022523006 scopus 로고
    • Glycation of skin collagen in type I diabetes mellitus. Correlation with long-term complications
    • Vishwanath V, Frank KE, Elmets CA, Dauchot PJ, Monnier VM. Glycation of skin collagen in type I diabetes mellitus. Correlation with long-term complications. Diabetes 1986;35:916-21.
    • (1986) Diabetes , vol.35 , pp. 916-921
    • Vishwanath, V.1    Frank, K.E.2    Elmets, C.A.3    Dauchot, P.J.4    Monnier, V.M.5
  • 19
    • 0034787428 scopus 로고    scopus 로고
    • Extracellular matrix and keratinocyte migration
    • O'Toole EA. Extracellular matrix and keratinocyte migration. Clin Exp Dermatol 2001;26:525-30.
    • (2001) Clin Exp Dermatol , vol.26 , pp. 525-530
    • O'Toole, E.A.1
  • 20
    • 0025773632 scopus 로고
    • Immunochemical approach to characterize advanced glycation end products of the Maillard reaction. Evidence for the presence of a common structure
    • Horiuchi S, Araki N, Morino Y. Immunochemical approach to characterize advanced glycation end products of the Maillard reaction. Evidence for the presence of a common structure. J Biol Chem 1991;266:7329-32.
    • (1991) J Biol Chem , vol.266 , pp. 7329-7332
    • Horiuchi, S.1    Araki, N.2    Morino, Y.3
  • 21
    • 0033820618 scopus 로고    scopus 로고
    • Glycolaldehyde, a reactive intermediate for advanced glycation end products, plays an important role in the generation of an active ligand for the macrophage scavenger receptor
    • Nagai R, Matsumoto K, Ling X, Suzuki H, Araki T, Horiuchi S. Glycolaldehyde, a reactive intermediate for advanced glycation end products, plays an important role in the generation of an active ligand for the macrophage scavenger receptor. Diabetes 2000;49:1714-23.
    • (2000) Diabetes , vol.49 , pp. 1714-1723
    • Nagai, R.1    Matsumoto, K.2    Ling, X.3    Suzuki, H.4    Araki, T.5    Horiuchi, S.6
  • 22
    • 0028934990 scopus 로고
    • Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates of the Maillard reaction
    • Glomb MA, Monnier VM. Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates of the Maillard reaction. J Biol Chem 1995;270:10017-26.
    • (1995) J Biol Chem , vol.270 , pp. 10017-10026
    • Glomb, M.A.1    Monnier, V.M.2
  • 24
    • 0026443080 scopus 로고
    • Nonenzymatic glycation of type I collagen. The effects of aging on preferential glycation sites
    • Reiser KM, Amigable MA, Last JA. Nonenzymatic glycation of type I collagen. The effects of aging on preferential glycation sites. J Biol Chem 1992;267:24207-16.
    • (1992) J Biol Chem , vol.267 , pp. 24207-24216
    • Reiser, K.M.1    Amigable, M.A.2    Last, J.A.3
  • 25
    • 0033542665 scopus 로고    scopus 로고
    • Clinical evidence: Glycaemic control in diabetes
    • Herman WH. Clinical evidence: glycaemic control in diabetes. BMJ 1999;319:104-6.
    • (1999) BMJ , vol.319 , pp. 104-106
    • Herman, W.H.1
  • 27
    • 0034028713 scopus 로고    scopus 로고
    • Lack of insulin-like growth factor 1 (IGF1) in the basal keratinocyte layer of diabetic skin and diabetic foot ulcers
    • Blakytny R, Jude EB, Martin Gibson J, Boulton AJ, Ferguson MW. Lack of insulin-like growth factor 1 (IGF1) in the basal keratinocyte layer of diabetic skin and diabetic foot ulcers. J Pathol 2000;190:589-94.
    • (2000) J Pathol , vol.190 , pp. 589-594
    • Blakytny, R.1    Jude, E.B.2    Martin Gibson, J.3    Boulton, A.J.4    Ferguson, M.W.5
  • 28
    • 0034139519 scopus 로고    scopus 로고
    • Biology of wound healing
    • Aukhil I. Biology of wound healing. Periodontology 2000, 2000;22:44-50.
    • (2000) Periodontology 2000 , vol.22 , pp. 44-50
    • Aukhil, I.1
  • 29
    • 0030934532 scopus 로고    scopus 로고
    • Wound healing - Aiming for perfect skin regeneration
    • Martin P. Wound healing - aiming for perfect skin regeneration. Science 1997;276:75-81.
    • (1997) Science , vol.276 , pp. 75-81
    • Martin, P.1
  • 30
    • 0033002442 scopus 로고    scopus 로고
    • The effect of advanced glycation end-product formation upon cell-matrix interactions
    • Paul RG, Bailey AJ. The effect of advanced glycation end-product formation upon cell-matrix interactions. Int J Biochem Cell Biol 1999;31:653-60.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 653-660
    • Paul, R.G.1    Bailey, A.J.2
  • 31
    • 0026599837 scopus 로고
    • Human monocyte interactions with non-enzymatically glycated collagen
    • Gilcrease MZ, Hoover RL. Human monocyte interactions with non-enzymatically glycated collagen. Diabetologia 1992;35:160-4.
    • (1992) Diabetologia , vol.35 , pp. 160-164
    • Gilcrease, M.Z.1    Hoover, R.L.2
  • 32
    • 0034664942 scopus 로고    scopus 로고
    • In vitro glycoxidation alters the interactions between collagens and human polymorphonuclear leucocytes
    • Monboisse JC, Rittie L, Lamfarraj H, Garnotel R, Gillery P. In vitro glycoxidation alters the interactions between collagens and human polymorphonuclear leucocytes. Biochem J 2000;350 Part 3:777-83.
    • (2000) Biochem J , vol.350 , Issue.3 PART , pp. 777-783
    • Monboisse, J.C.1    Rittie, L.2    Lamfarraj, H.3    Garnotel, R.4    Gillery, P.5
  • 34
    • 0026523180 scopus 로고
    • Integrin receptors and RGD sequences in human keratinocyte migration: Unique anti-migratory function of alpha 3 beta 1 epiligrin receptor
    • Kim JP, Zhang K, Kramer RH, Schall TJ, Woodley DT. Integrin receptors and RGD sequences in human keratinocyte migration: unique anti-migratory function of alpha 3 beta 1 epiligrin receptor. J Invest Dermatol 1992;98:764-70.
    • (1992) J Invest Dermatol , vol.98 , pp. 764-770
    • Kim, J.P.1    Zhang, K.2    Kramer, R.H.3    Schall, T.J.4    Woodley, D.T.5
  • 35
    • 0034614620 scopus 로고    scopus 로고
    • The collagen-binding A-domains of integrins alpha (1) beta (1) and alpha (2) beta (1) recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens
    • Knight CG, Morton LF, Peachey AR, Tuckwell DS, Farndale RW, Barnes MJ. The collagen-binding A-domains of integrins alpha (1) beta (1) and alpha (2) beta (1) recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens. J Biol Chem 2000;275:35-40.
    • (2000) J Biol Chem , vol.275 , pp. 35-40
    • Knight, C.G.1    Morton, L.F.2    Peachey, A.R.3    Tuckwell, D.S.4    Farndale, R.W.5    Barnes, M.J.6
  • 36
    • 0032913989 scopus 로고    scopus 로고
    • Sequence dependent conformational variations of collagen triple-helical structure
    • Kramer RZ, Bella J, Mayville P, Brodsky B, Berman HM. Sequence dependent conformational variations of collagen triple-helical structure. Nat Struct Biol 1999;6:454-7.
    • (1999) Nat Struct Biol , vol.6 , pp. 454-457
    • Kramer, R.Z.1    Bella, J.2    Mayville, P.3    Brodsky, B.4    Berman, H.M.5
  • 38
    • 0024470294 scopus 로고
    • Cross-linking and fluorescence changes of collagen by glycation and oxidation
    • Fujimori E. Cross-linking and fluorescence changes of collagen by glycation and oxidation. Biochim Biophys Acta 1989; 998:105-10.
    • (1989) Biochim Biophys Acta , vol.998 , pp. 105-110
    • Fujimori, E.1
  • 39
    • 0034651519 scopus 로고    scopus 로고
    • Direct detection of crosslinks of collagen and elastin in the hydrolysates of human yellow ligament using single-column high performance liquid chromatography
    • Chen JR, Takahashi M, Kushida K, Suzuki M, Suzuki K, Horiuchi K, Nagano A. Direct detection of crosslinks of collagen and elastin in the hydrolysates of human yellow ligament using single-column high performance liquid chromatography. Anal Biochem 2000;278:99-105.
    • (2000) Anal Biochem , vol.278 , pp. 99-105
    • Chen, J.R.1    Takahashi, M.2    Kushida, K.3    Suzuki, M.4    Suzuki, K.5    Horiuchi, K.6    Nagano, A.7
  • 40
    • 0032427387 scopus 로고    scopus 로고
    • Advanced glycation end products induce crosslinking of collagen in vitro
    • Sajithlal GB, Chithra P, Chandrakasan G. Advanced glycation end products induce crosslinking of collagen in vitro. Biochim Biophys Acta 1998;1407:215-24.
    • (1998) Biochim Biophys Acta , vol.1407 , pp. 215-224
    • Sajithlal, G.B.1    Chithra, P.2    Chandrakasan, G.3
  • 41
    • 0035060783 scopus 로고    scopus 로고
    • Glycation cross-links inhibit matrix metalloproteinase-2 activation in vascular smooth muscle cells cultured on collagen lattice
    • Kuzuya M, Asai T, Kanda S, Maeda K, Cheng XW, Iguchi A. Glycation cross-links inhibit matrix metalloproteinase-2 activation in vascular smooth muscle cells cultured on collagen lattice. Diabetologia 2001;44:433-6.
    • (2001) Diabetologia , vol.44 , pp. 433-436
    • Kuzuya, M.1    Asai, T.2    Kanda, S.3    Maeda, K.4    Cheng, X.W.5    Iguchi, A.6
  • 42
    • 0029893422 scopus 로고    scopus 로고
    • The role of glycation cross-links in diabetic vascular stiffening
    • Sims TJ, Rasmussen LM, Oxlund H, Bailey AJ. The role of glycation cross-links in diabetic vascular stiffening. Diabetologia 1996;39:946-51.
    • (1996) Diabetologia , vol.39 , pp. 946-951
    • Sims, T.J.1    Rasmussen, L.M.2    Oxlund, H.3    Bailey, A.J.4
  • 43
    • 0023705750 scopus 로고
    • Glycation induces expansion of the molecular packing of collagen
    • Tanaka S, Avigad G, Brodsky B, Eikenberry EF. Glycation induces expansion of the molecular packing of collagen. J Mol Biol 1988;203:495-505.
    • (1988) J Mol Biol , vol.203 , pp. 495-505
    • Tanaka, S.1    Avigad, G.2    Brodsky, B.3    Eikenberry, E.F.4
  • 44
    • 0033787215 scopus 로고    scopus 로고
    • Collagen structure and nonlinear susceptibility: Effects of heat, glycation, and enzymatic cleavage on second harmonic signal intensity
    • Kim BM, Eichler J, Reiser KM, Rubenchik AM, Da Silva LB. Collagen structure and nonlinear susceptibility: effects of heat, glycation, and enzymatic cleavage on second harmonic signal intensity. Lasers Surg Med 2000;27:329-35.
    • (2000) Lasers Surg Med , vol.27 , pp. 329-335
    • Kim, B.M.1    Eichler, J.2    Reiser, K.M.3    Rubenchik, A.M.4    Da Silva, L.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.