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Volumn 118, Issue 10, 2010, Pages 753-764

Skin wound healing in diabetic β6 integrin-deficient mice

Author keywords

advanced glycated endproducts; diabetes mellitus; fibronectin; integrins; Wound healing

Indexed keywords

ADVANCED GLYCATION END PRODUCT; ALPHAVBETA6 INTEGRIN; BETA1 INTEGRIN; BETA6 INTEGRIN; FIBRONECTIN; MATRIX PROTEIN; METHYLGLYOXAL; BETA INTEGRIN;

EID: 77956938338     PISSN: 09034641     EISSN: 16000463     Source Type: Journal    
DOI: 10.1111/j.1600-0463.2010.02654.x     Document Type: Article
Times cited : (18)

References (55)
  • 1
    • 2342466734 scopus 로고    scopus 로고
    • Global prevalence of diabetes: Estimates for the year 2000 and projections for 2030
    • Wild S, Roglic G, Green A, Sicree R, King H. Global prevalence of diabetes: estimates for the year 2000 and projections for 2030. Diabetes Care 2004 27 : 1047 53.
    • (2004) Diabetes Care , vol.27 , pp. 1047-53
    • Wild, S.1    Roglic, G.2    Green, A.3    Sicree, R.4    King, H.5
  • 2
    • 33644651282 scopus 로고    scopus 로고
    • Severely impaired insulin signaling in chronic wounds of diabetic obob mice: A potential role of tumor necrosis factor-alpha
    • Goren I, Muller E, Pfeilschifter J, Frank S. Severely impaired insulin signaling in chronic wounds of diabetic obob mice: a potential role of tumor necrosis factor-alpha. Am J Pathol 2006 168 : 765 77.
    • (2006) Am J Pathol , vol.168 , pp. 765-77
    • Goren, I.1    Muller, E.2    Pfeilschifter, J.3    Frank, S.4
  • 3
    • 33749142760 scopus 로고    scopus 로고
    • Chemokines, cytokines, and growth factors in keratinocytes and dermal endothelial cells in the margin of chronic diabetic foot ulcers
    • Galkowska H, Wojewodzka U, Olszewski WL. Chemokines, cytokines, and growth factors in keratinocytes and dermal endothelial cells in the margin of chronic diabetic foot ulcers. Wound Repair Regen 2006 14 : 558 65.
    • (2006) Wound Repair Regen , vol.14 , pp. 558-65
    • Galkowska, H.1    Wojewodzka, U.2    Olszewski, W.L.3
  • 4
    • 27744448125 scopus 로고    scopus 로고
    • Wound healing and its impairment in the diabetic foot
    • Falanga V. Wound healing and its impairment in the diabetic foot. Lancet 2005 366 : 1736 43.
    • (2005) Lancet , vol.366 , pp. 1736-43
    • Falanga, V.1
  • 5
    • 2442717879 scopus 로고    scopus 로고
    • Topical vascular endothelial growth factor accelerates diabetic wound healing through increased angiogenesis and by mobilizing and recruiting bone marrow-derived cells
    • Galiano RD, Tepper OM, Pelo CR, Bhatt KA, Callaghan M, Bastidas N, et al. Topical vascular endothelial growth factor accelerates diabetic wound healing through increased angiogenesis and by mobilizing and recruiting bone marrow-derived cells. Am J Pathol 2004 164 : 1935 47.
    • (2004) Am J Pathol , vol.164 , pp. 1935-47
    • Galiano, R.D.1    Tepper, O.M.2    Pelo, C.R.3    Bhatt, K.A.4    Callaghan, M.5    Bastidas, N.6
  • 6
    • 34247874642 scopus 로고    scopus 로고
    • Decreased macrophage number and activation lead to reduced lymphatic vessel formation and contribute to impaired diabetic wound healing
    • Maruyama K, Asai J, Ii M, Thorne T, Losordo DW, D'Amore PA. Decreased macrophage number and activation lead to reduced lymphatic vessel formation and contribute to impaired diabetic wound healing. Am J Pathol 2007 170 : 1178 91.
    • (2007) Am J Pathol , vol.170 , pp. 1178-91
    • Maruyama, K.1    Asai, J.2    Ii, M.3    Thorne, T.4    Losordo, D.W.5    D'Amore, P.A.6
  • 7
    • 0036436789 scopus 로고    scopus 로고
    • Diminished neuropeptide levels contribute to the impaired cutaneous healing response associated with diabetes mellitus
    • Gibran NS, Jang YC, Isik FF, Greenhalgh DG, Muffley LA, Underwood RA, et al. Diminished neuropeptide levels contribute to the impaired cutaneous healing response associated with diabetes mellitus. J Surg Res 2002 108 : 122 8.
    • (2002) J Surg Res , vol.108 , pp. 122-8
    • Gibran, N.S.1    Jang, Y.C.2    Isik, F.F.3    Greenhalgh, D.G.4    Muffley, L.A.5    Underwood, R.A.6
  • 8
    • 0036020282 scopus 로고    scopus 로고
    • Expression of matrix-metalloproteinases and their inhibitors in the wounds of diabetic and non-diabetic patients
    • Lobmann R, Ambrosch A, Schultz G, Waldmann K, Schiweck S, Lehnert H. Expression of matrix-metalloproteinases and their inhibitors in the wounds of diabetic and non-diabetic patients. Diabetologia 2002 45 : 1011 6.
    • (2002) Diabetologia , vol.45 , pp. 1011-6
    • Lobmann, R.1    Ambrosch, A.2    Schultz, G.3    Waldmann, K.4    Schiweck, S.5    Lehnert, H.6
  • 9
    • 55749086406 scopus 로고    scopus 로고
    • Advanced glycation of type i collagen and fibronectin modifies periodontal cell behavior
    • Murillo J, Wang Y, Xu X, Klebe RJ, Chen Z, Zardeneta G, et al. Advanced glycation of type I collagen and fibronectin modifies periodontal cell behavior. J Periodontol 2008 79 : 2190 9.
    • (2008) J Periodontol , vol.79 , pp. 2190-9
    • Murillo, J.1    Wang, Y.2    Xu, X.3    Klebe, R.J.4    Chen, Z.5    Zardeneta, G.6
  • 10
    • 23044451988 scopus 로고    scopus 로고
    • Integrins as a distinct subtype of dependence receptors
    • Stupack DG. Integrins as a distinct subtype of dependence receptors. Cell Death Differ 2005 12 : 1021 30.
    • (2005) Cell Death Differ , vol.12 , pp. 1021-30
    • Stupack, D.G.1
  • 11
    • 0034283814 scopus 로고    scopus 로고
    • Integrin and ECM functions: Roles in vertebrate development
    • De Arcangelis A, Georges-Labouesse E. Integrin and ECM functions: roles in vertebrate development. Trends Genet 2000 16 : 389 95.
    • (2000) Trends Genet , vol.16 , pp. 389-95
    • De Arcangelis, A.1    Georges-Labouesse, E.2
  • 12
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes RO. Integrins: bidirectional, allosteric signaling machines. Cell 2002 110 : 673 87.
    • (2002) Cell , vol.110 , pp. 673-87
    • Hynes, R.O.1
  • 13
    • 0027217908 scopus 로고
    • Expression of integrins and basement membrane components by wound keratinocytes
    • Larjava H, Salo T, Haapasalmi K, Kramer RH, Heino J. Expression of integrins and basement membrane components by wound keratinocytes. J Clin Invest 1993 92 : 1425 35.
    • (1993) J Clin Invest , vol.92 , pp. 1425-35
    • Larjava, H.1    Salo, T.2    Haapasalmi, K.3    Kramer, R.H.4    Heino, J.5
  • 14
    • 13544259736 scopus 로고    scopus 로고
    • Cellular and molecular facets of keratinocyte reepithelization during wound healing
    • Santoro MM, Gaudino G. Cellular and molecular facets of keratinocyte reepithelization during wound healing. Exp Cell Res 2005 304 : 274 86.
    • (2005) Exp Cell Res , vol.304 , pp. 274-86
    • Santoro, M.M.1    Gaudino, G.2
  • 15
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark EA, Brugge JS. Integrins and signal transduction pathways: the road taken. Science 1995 268 : 233 9.
    • (1995) Science , vol.268 , pp. 233-9
    • Clark, E.A.1    Brugge, J.S.2
  • 17
    • 0033524949 scopus 로고    scopus 로고
    • The integrin alpha v beta 6 binds and activates latent TGF beta 1: A mechanism for regulating pulmonary inflammation and fibrosis
    • Munger JS, Huang X, Kawakatsu H, Griffiths MJ, Dalton SL, Wu J, et al. The integrin alpha v beta 6 binds and activates latent TGF beta 1: a mechanism for regulating pulmonary inflammation and fibrosis. Cell 1999 96 : 319 28.
    • (1999) Cell , vol.96 , pp. 319-28
    • Munger, J.S.1    Huang, X.2    Kawakatsu, H.3    Griffiths, M.J.4    Dalton, S.L.5    Wu, J.6
  • 18
    • 0026660349 scopus 로고
    • Characterization of the integrin alpha v beta 6 as a fibronectin-binding protein
    • Busk M, Pytela R, Sheppard D. Characterization of the integrin alpha v beta 6 as a fibronectin-binding protein. J Biol Chem 1992 267 : 5790 6.
    • (1992) J Biol Chem , vol.267 , pp. 5790-6
    • Busk, M.1    Pytela, R.2    Sheppard, D.3
  • 19
    • 0032794389 scopus 로고    scopus 로고
    • Different integrins mediate cell spreading, haptotaxis and lateral migration of HaCaT keratinocytes on fibronectin
    • Koivisto L, Larjava K, Hakkinen L, Uitto VJ, Heino J, Larjava H. Different integrins mediate cell spreading, haptotaxis and lateral migration of HaCaT keratinocytes on fibronectin. Cell Adhes Commun 1999 7 : 245 57.
    • (1999) Cell Adhes Commun , vol.7 , pp. 245-57
    • Koivisto, L.1    Larjava, K.2    Hakkinen, L.3    Uitto, V.J.4    Heino, J.5    Larjava, H.6
  • 20
    • 0037439630 scopus 로고    scopus 로고
    • Making sense of latent TGFbeta activation
    • Annes JP, Munger JS, Rifkin DB. Making sense of latent TGFbeta activation. J Cell Sci 2003 116 : 217 24.
    • (2003) J Cell Sci , vol.116 , pp. 217-24
    • Annes, J.P.1    Munger, J.S.2    Rifkin, D.B.3
  • 21
    • 2942653435 scopus 로고    scopus 로고
    • Integrin alphaVbeta6-mediated activation of latent TGF-beta requires the latent TGF-beta binding protein-1
    • Annes JP, Chen Y, Munger JS, Rifkin DB. Integrin alphaVbeta6-mediated activation of latent TGF-beta requires the latent TGF-beta binding protein-1. J Cell Biol 2004 165 : 723 34.
    • (2004) J Cell Biol , vol.165 , pp. 723-34
    • Annes, J.P.1    Chen, Y.2    Munger, J.S.3    Rifkin, D.B.4
  • 22
    • 61949349656 scopus 로고    scopus 로고
    • Mice that lack activity of alphavbeta6- and alphavbeta8-integrins reproduce the abnormalities of Tgfb1- and Tgfb3-null mice
    • Aluwihare P, Mu Z, Zhao Z, Yu D, Weinreb PH, Horan GS, et al. Mice that lack activity of alphavbeta6- and alphavbeta8-integrins reproduce the abnormalities of Tgfb1- and Tgfb3-null mice. J Cell Sci 2009 122 : 227 32.
    • (2009) J Cell Sci , vol.122 , pp. 227-32
    • Aluwihare, P.1    Mu, Z.2    Zhao, Z.3    Yu, D.4    Weinreb, P.H.5    Horan, G.S.6
  • 23
    • 1542679109 scopus 로고    scopus 로고
    • Increased expression of beta6-integrin in skin leads to spontaneous development of chronic wounds
    • Hakkinen L, Koivisto L, Gardner H, Saarialho-Kere U, Carroll JM, Lakso M, et al. Increased expression of beta6-integrin in skin leads to spontaneous development of chronic wounds. Am J Pathol 2004 164 : 229 42.
    • (2004) Am J Pathol , vol.164 , pp. 229-42
    • Hakkinen, L.1    Koivisto, L.2    Gardner, H.3    Saarialho-Kere, U.4    Carroll, J.M.5    Lakso, M.6
  • 24
    • 15844376477 scopus 로고    scopus 로고
    • Inactivation of the integrin beta 6 subunit gene reveals a role of epithelial integrins in regulating inflammation in the lung and skin
    • Huang XZ, Wu JF, Cass D, Erle DJ, Corry D, Young SG, et al. Inactivation of the integrin beta 6 subunit gene reveals a role of epithelial integrins in regulating inflammation in the lung and skin. J Cell Biol 1996 133 : 921 8.
    • (1996) J Cell Biol , vol.133 , pp. 921-8
    • Huang, X.Z.1    Wu, J.F.2    Cass, D.3    Erle, D.J.4    Corry, D.5    Young, S.G.6
  • 25
    • 33745524940 scopus 로고    scopus 로고
    • The alphavbeta6 integrin plays a role in compromised epidermal wound healing
    • AlDahlawi S, Eslami A, Hakkinen L, Larjava HS. The alphavbeta6 integrin plays a role in compromised epidermal wound healing. Wound Repair Regen 2006 14 : 289 97.
    • (2006) Wound Repair Regen , vol.14 , pp. 289-97
    • Aldahlawi, S.1    Eslami, A.2    Hakkinen, L.3    Larjava, H.S.4
  • 26
    • 34848830242 scopus 로고    scopus 로고
    • Agent-based model of inflammation and wound healing: Insights into diabetic foot ulcer pathology and the role of transforming growth factor-beta1
    • Mi Q, Riviere B, Clermont G, Steed DL, Vodovotz Y. Agent-based model of inflammation and wound healing: insights into diabetic foot ulcer pathology and the role of transforming growth factor-beta1. Wound Repair Regen 2007 15 : 671 82.
    • (2007) Wound Repair Regen , vol.15 , pp. 671-82
    • Mi, Q.1    Riviere, B.2    Clermont, G.3    Steed, D.L.4    Vodovotz, Y.5
  • 27
    • 34848870970 scopus 로고    scopus 로고
    • Dbdb mice exhibit severe wound-healing impairments compared with other murine diabetic strains in a silicone-splinted excisional wound model
    • Michaels J, Churgin SS, Blechman KM, Greives MR, Aarabi S, Galiano RD, et al. dbdb mice exhibit severe wound-healing impairments compared with other murine diabetic strains in a silicone-splinted excisional wound model. Wound Repair Regen 2007 15 : 665 70.
    • (2007) Wound Repair Regen , vol.15 , pp. 665-70
    • Michaels, J.1    Churgin, S.S.2    Blechman, K.M.3    Greives, M.R.4    Aarabi, S.5    Galiano, R.D.6
  • 28
    • 33846893225 scopus 로고    scopus 로고
    • Effects of Plasma Fibronectin on the Healing of Full-Thickness Skin Wounds in Streptozotocin-Induced Diabetic Rats
    • DOI 10.1016/j.jss.2006.06.034, PII S0022480406003155
    • Qiu Z, Kwon AH, Kamiyama Y. Effects of plasma fibronectin on the healing of full-thickness skin wounds in streptozotocin-induced diabetic rats. J Surg Res 2007 138 : 64 70. (Pubitemid 46227451)
    • (2007) Journal of Surgical Research , vol.138 , Issue.1 , pp. 64-70
    • Qiu, Z.1    Kwon, A.-H.2    Kamiyama, Y.3
  • 29
    • 0025359279 scopus 로고
    • PDGF and FGF stimulate wound healing in the genetically diabetic mouse
    • Greenhalgh DG, Sprugel KH, Murray MJ, Ross R. PDGF and FGF stimulate wound healing in the genetically diabetic mouse. Am J Pathol 1990 136 : 1235 46.
    • (1990) Am J Pathol , vol.136 , pp. 1235-46
    • Greenhalgh, D.G.1    Sprugel, K.H.2    Murray, M.J.3    Ross, R.4
  • 30
    • 0029826378 scopus 로고    scopus 로고
    • Modification of Movat pentachrome stain with improved reliability of elastin staining
    • Schmidt R., Wirtala J. Modification of Movat pentachrome stain with improved reliability of elastin staining. J Histotechnol 1996 19 : 325 7.
    • (1996) J Histotechnol , vol.19 , pp. 325-7
    • Schmidt, R.1    Wirtala, J.2
  • 31
    • 0017375736 scopus 로고
    • Binding of soluble form of fibroblast surface protein, fibronectin, to collagen
    • Engvall E, Ruoslahti E. Binding of soluble form of fibroblast surface protein, fibronectin, to collagen. Int J Cancer 1977 20 : 1 5.
    • (1977) Int J Cancer , vol.20 , pp. 1-5
    • Engvall, E.1    Ruoslahti, E.2
  • 32
    • 77950204296 scopus 로고    scopus 로고
    • Co-purified gelatinases alter the stability and biological activities of human plasma fibronectin
    • Pal S, Chen Z, Xu X, Mikhailova M, Steffensen B. Co-purified gelatinases alter the stability and biological activities of human plasma fibronectin. J Periodont Res 2010 45 : 292 5.
    • (2010) J Periodont Res , vol.45 , pp. 292-5
    • Pal, S.1    Chen, Z.2    Xu, X.3    Mikhailova, M.4    Steffensen, B.5
  • 33
    • 0024213916 scopus 로고
    • Identification and characterization of enamel proteinases isolated from developing enamel. Amelogeninolytic serine proteinases are associated with enamel maturation in pig
    • Overall CM, Limeback H. Identification and characterization of enamel proteinases isolated from developing enamel. Amelogeninolytic serine proteinases are associated with enamel maturation in pig. Biochem J 1988 256 : 965 72.
    • (1988) Biochem J , vol.256 , pp. 965-72
    • Overall, C.M.1    Limeback, H.2
  • 34
    • 0029010660 scopus 로고
    • Extracellular matrix binding properties of recombinant fibronectin type II-like modules of human 72-kDa gelatinasetype IV collagenase. High affinity binding to native type i collagen but not native type IV collagen
    • Steffensen B, Wallon UM, Overall CM. Extracellular matrix binding properties of recombinant fibronectin type II-like modules of human 72-kDa gelatinasetype IV collagenase. High affinity binding to native type I collagen but not native type IV collagen. J Biol Chem 1995 270 : 11555 66.
    • (1995) J Biol Chem , vol.270 , pp. 11555-66
    • Steffensen, B.1    Wallon, U.M.2    Overall, C.M.3
  • 35
    • 0032549538 scopus 로고    scopus 로고
    • Immunological evidence for methylglyoxal-derived modifications in vivo. Determination of antigenic epitopes
    • Shamsi FA, Partal A, Sady C, Glomb MA, Nagaraj RH. Immunological evidence for methylglyoxal-derived modifications in vivo. Determination of antigenic epitopes. J Biol Chem 1998 273 : 6928 36.
    • (1998) J Biol Chem , vol.273 , pp. 6928-36
    • Shamsi, F.A.1    Partal, A.2    Sady, C.3    Glomb, M.A.4    Nagaraj, R.H.5
  • 36
    • 44349147177 scopus 로고    scopus 로고
    • Fibronectin fragmentation is a feature of periodontal disease sites and diabetic foot and leg wounds and modifies cell behavior
    • Stanley CM, Wang Y, Pal S, Klebe RJ, Harkless LB, Xu X, et al. Fibronectin fragmentation is a feature of periodontal disease sites and diabetic foot and leg wounds and modifies cell behavior. J Periodontol 2008 79 : 861 75.
    • (2008) J Periodontol , vol.79 , pp. 861-75
    • Stanley, C.M.1    Wang, Y.2    Pal, S.3    Klebe, R.J.4    Harkless, L.B.5    Xu, X.6
  • 37
    • 0024359871 scopus 로고
    • Analysis of fibronectin receptor function with monoclonal antibodies: Roles in cell adhesion, migration, matrix assembly, and cytoskeletal organization
    • Akiyama SK, Yamada SS, Chen WT, Yamada KM. Analysis of fibronectin receptor function with monoclonal antibodies: roles in cell adhesion, migration, matrix assembly, and cytoskeletal organization. J Cell Biol 1989 109 : 863 75.
    • (1989) J Cell Biol , vol.109 , pp. 863-75
    • Akiyama, S.K.1    Yamada, S.S.2    Chen, W.T.3    Yamada, K.M.4
  • 38
    • 0031696891 scopus 로고    scopus 로고
    • The integrin alphavbeta6 is critical for keratinocyte migration on both its known ligand, fibronectin, and on vitronectin
    • Huang X, Wu J, Spong S, Sheppard D. The integrin alphavbeta6 is critical for keratinocyte migration on both its known ligand, fibronectin, and on vitronectin. J Cell Sci 1998 111 (Pt 15 2189 95.
    • (1998) J Cell Sci , vol.111 , Issue.15 , pp. 2189-95
    • Huang, X.1    Wu, J.2    Spong, S.3    Sheppard, D.4
  • 40
    • 38549143790 scopus 로고    scopus 로고
    • Proteomic analysis of mouse islets after multiple low-dose streptozotocin injection
    • Xie X, Li S, Liu S, Lu Y, Shen P, Ji J. Proteomic analysis of mouse islets after multiple low-dose streptozotocin injection. Biochim Biophys Acta 2008 1784 : 276 84.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 276-84
    • Xie, X.1    Li, S.2    Liu, S.3    Lu, Y.4    Shen, P.5    Ji, J.6
  • 41
    • 0017179001 scopus 로고
    • Streptozotocin-induced pancreatic insulitis: New model of diabetes mellitus
    • Like AA, Rossini AA. Streptozotocin-induced pancreatic insulitis: new model of diabetes mellitus. Science 1976 193 : 415 7.
    • (1976) Science , vol.193 , pp. 415-7
    • Like, A.A.1    Rossini, A.A.2
  • 42
    • 0019494189 scopus 로고
    • The diabetogenic effects of streptozotocin in mice are prolonged and inversely related to age
    • Riley WJ, McConnell TJ, Maclaren NK, McLaughlin JV, Taylor G. The diabetogenic effects of streptozotocin in mice are prolonged and inversely related to age. Diabetes 1981 30 : 718 23.
    • (1981) Diabetes , vol.30 , pp. 718-23
    • Riley, W.J.1    McConnell, T.J.2    MacLaren, N.K.3    McLaughlin, J.V.4    Taylor, G.5
  • 43
    • 0038782328 scopus 로고    scopus 로고
    • Immunization with streptozotocin-treated NOD mouse islets inhibits the onset of autoimmune diabetes in NOD mice
    • Rayat GR, Rajotte RV, Lyon JG, Dufour JM, Hacquoil BV, Korbutt GS. Immunization with streptozotocin-treated NOD mouse islets inhibits the onset of autoimmune diabetes in NOD mice. J Autoimmun 2003 21 : 11 5.
    • (2003) J Autoimmun , vol.21 , pp. 11-5
    • Rayat, G.R.1    Rajotte, R.V.2    Lyon, J.G.3    Dufour, J.M.4    Hacquoil, B.V.5    Korbutt, G.S.6
  • 44
    • 0018139377 scopus 로고
    • Obese and diabetes: Two mutant genes causing diabetes-obesity syndromes in mice
    • Coleman DL. Obese and diabetes: two mutant genes causing diabetes-obesity syndromes in mice. Diabetologia 1978 14 : 141 8.
    • (1978) Diabetologia , vol.14 , pp. 141-8
    • Coleman, D.L.1
  • 45
    • 0020045888 scopus 로고
    • Diabetes-obesity syndromes in mice
    • Coleman DL. Diabetes-obesity syndromes in mice. Diabetes 1982 31 : 1 6.
    • (1982) Diabetes , vol.31 , pp. 1-6
    • Coleman, D.L.1
  • 47
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature 2001 414 : 813 20.
    • (2001) Nature , vol.414 , pp. 813-20
    • Brownlee, M.1
  • 48
    • 65949105729 scopus 로고    scopus 로고
    • Mice lacking beta6 integrin in skin show accelerated wound repair in dexamethasone impaired wound healing model
    • Xie Y, Gao K, Hakkinen L, Larjava HS. Mice lacking beta6 integrin in skin show accelerated wound repair in dexamethasone impaired wound healing model. Wound Repair Regen 2009 17 : 326 39.
    • (2009) Wound Repair Regen , vol.17 , pp. 326-39
    • Xie, Y.1    Gao, K.2    Hakkinen, L.3    Larjava, H.S.4
  • 49
    • 0033628284 scopus 로고    scopus 로고
    • Glucocorticoid-regulated gene expression during cutaneous wound repair
    • Beer HD, Fassler R, Werner S. Glucocorticoid-regulated gene expression during cutaneous wound repair. Vitam Horm 2000 59 : 217 39.
    • (2000) Vitam Horm , vol.59 , pp. 217-39
    • Beer, H.D.1    Fassler, R.2    Werner, S.3
  • 50
    • 67651180895 scopus 로고    scopus 로고
    • Advanced glycoxidation products and impaired diabetic wound healing
    • Peppa M, Stavroulakis P, Raptis SA. Advanced glycoxidation products and impaired diabetic wound healing. Wound Repair Regen 2009 17 : 461 72.
    • (2009) Wound Repair Regen , vol.17 , pp. 461-72
    • Peppa, M.1    Stavroulakis, P.2    Raptis, S.A.3
  • 51
    • 0037093336 scopus 로고    scopus 로고
    • Assay of advanced glycation endproducts (AGEs): Surveying AGEs by chromatographic assay with derivatization by 6-aminoquinolyl-N- hydroxysuccinimidyl-carbamate and application to Nepsilon-carboxymethyl-lysine- and Nepsilon-(1-carboxyethyl)lysine-modified albumin
    • Ahmed N, Argirov OK, Minhas HS, Cordeiro CA, Thornalley PJ. Assay of advanced glycation endproducts (AGEs): surveying AGEs by chromatographic assay with derivatization by 6-aminoquinolyl-N-hydroxysuccinimidyl-carbamate and application to Nepsilon-carboxymethyl-lysine- and Nepsilon-(1-carboxyethyl) lysine-modified albumin. Biochem J 2002 364 : 1 14.
    • (2002) Biochem J , vol.364 , pp. 1-14
    • Ahmed, N.1    Argirov, O.K.2    Minhas, H.S.3    Cordeiro, C.A.4    Thornalley, P.J.5
  • 52
    • 21744448064 scopus 로고    scopus 로고
    • Methylglyoxal administration induces diabetes-like microvascular changes and perturbs the healing process of cutaneous wounds
    • Berlanga J, Cibrian D, Guillen I, Freyre F, Alba JS, Lopez-Saura P, et al. Methylglyoxal administration induces diabetes-like microvascular changes and perturbs the healing process of cutaneous wounds. Clin Sci (Lond) 2005 109 : 83 95.
    • (2005) Clin Sci (Lond) , vol.109 , pp. 83-95
    • Berlanga, J.1    Cibrian, D.2    Guillen, I.3    Freyre, F.4    Alba, J.S.5    Lopez-Saura, P.6
  • 55
    • 0033637498 scopus 로고    scopus 로고
    • Possible involvement of altered RGD sequence in reduced adhesive and spreading activities of advanced glycation end product-modified fibronectin to vascular smooth muscle cells
    • Sakata N, Sasatomi Y, Meng J, Ando S, Uesugi N, Takebayashi S, et al. Possible involvement of altered RGD sequence in reduced adhesive and spreading activities of advanced glycation end product-modified fibronectin to vascular smooth muscle cells. Connect Tissue Res 2000 41 : 213 28.
    • (2000) Connect Tissue Res , vol.41 , pp. 213-28
    • Sakata, N.1    Sasatomi, Y.2    Meng, J.3    Ando, S.4    Uesugi, N.5    Takebayashi, S.6


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