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Volumn 77, Issue 3, 1997, Pages 281-288

Up-regulation of elastase in acute wounds of healthy aged humans and chronic venous leg ulcers are associated with matrix degradation

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; LEUKOCYTE ELASTASE; SERINE PROTEINASE;

EID: 0030880539     PISSN: 00236837     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (136)

References (31)
  • 1
    • 0029154515 scopus 로고
    • The effects of ageing on cutaneous wound healing in mammals
    • Ashcroft GS, Horan MA, and Ferguson MWJ (1995). The effects of ageing on cutaneous wound healing in mammals. J Anat 187:1-26.
    • (1995) J Anat , vol.187 , pp. 1-26
    • Ashcroft, G.S.1    Horan, M.A.2    Ferguson, M.W.J.3
  • 2
    • 0030890616 scopus 로고    scopus 로고
    • Aging is associated with reduced deposition of specific extracellular matrix components, an upregulation of angiogenesis, and an altered inflammatory response in a murine incisional wound healing model
    • Ashcroft GS, Horan MA, and Ferguson MWJ (1997). Aging is associated with reduced deposition of specific extracellular matrix components, an upregulation of angiogenesis, and an altered inflammatory response in a murine incisional wound healing model. J Invest Dermatot 108:430-437.
    • (1997) J Invest Dermatot , vol.108 , pp. 430-437
    • Ashcroft, G.S.1    Horan, M.A.2    Ferguson, M.W.J.3
  • 3
    • 0021184525 scopus 로고
    • Degradation of the epidermal-dermal junction by proteolytic enzymes from human skin and human polymorphonuclear leukocytes
    • Briggaman RA, Schechter NM, Fraki J, and Lazuras GS (1984). Degradation of the epidermal-dermal junction by proteolytic enzymes from human skin and human polymorphonuclear leukocytes. J Exp Med 160:1027-1042.
    • (1984) J Exp Med , vol.160 , pp. 1027-1042
    • Briggaman, R.A.1    Schechter, N.M.2    Fraki, J.3    Lazuras, G.S.4
  • 4
    • 0001426708 scopus 로고
    • Wound repair: Overview and general considerations
    • Clark RAF, editor. New York: Plenum Press
    • Clark RAF (1988). Wound repair: Overview and general considerations. In: Clark RAF, editor. The molecular and cellular biology of wound repair. New York: Plenum Press, 3-50.
    • (1988) The Molecular and Cellular Biology of Wound Repair , pp. 3-50
    • Clark, R.A.F.1
  • 6
    • 0027998135 scopus 로고
    • The role of neutrophil elastase in chronic inflammation
    • Döring G (1994). The role of neutrophil elastase in chronic inflammation. Am J Respir Crit Care Med 150:5114-117.
    • (1994) Am J Respir Crit Care Med , vol.150 , pp. 5114-5117
    • Döring, G.1
  • 7
    • 0027155669 scopus 로고
    • Chronic wounds: Pathophysiology and experimental considerations
    • Falanga V (1993). Chronic wounds: Pathophysiology and experimental considerations. J Invest Dermatol 100:721-725.
    • (1993) J Invest Dermatol , vol.100 , pp. 721-725
    • Falanga, V.1
  • 9
    • 0026605281 scopus 로고
    • Degradation of fibronectin and vitronectin in chronic wound fluid: Analysis by cell blotting, immunoblotting and cell adhesion assays
    • Grinnell F, Ho CH, and Wysocki A (1992). Degradation of fibronectin and vitronectin in chronic wound fluid: Analysis by cell blotting, immunoblotting and cell adhesion assays. J Invest Dermatol 984:410-416.
    • (1992) J Invest Dermatol , vol.984 , pp. 410-416
    • Grinnell, F.1    Ho, C.H.2    Wysocki, A.3
  • 10
    • 0028129140 scopus 로고
    • Identification of neutrophil elastase as the proteinase in burn wound fluid responsible for degradation of fibronectin
    • Grinnell F and Zhu M (1994). Identification of neutrophil elastase as the proteinase in burn wound fluid responsible for degradation of fibronectin. J Invest Dermatol 103:155-161.
    • (1994) J Invest Dermatol , vol.103 , pp. 155-161
    • Grinnell, F.1    Zhu, M.2
  • 11
    • 0029938994 scopus 로고    scopus 로고
    • Fibronectin degradation in chronic wounds depends on the relative levels of elastase, α1-proteinase inhibitor and α2-macroglobulin
    • Grinnell F and Zhu M (1996). Fibronectin degradation in chronic wounds depends on the relative levels of elastase, α1-proteinase inhibitor and α2-macroglobulin. J Invest Dermatol 106:335-341.
    • (1996) J Invest Dermatol , vol.106 , pp. 335-341
    • Grinnell, F.1    Zhu, M.2
  • 12
    • 0030033745 scopus 로고    scopus 로고
    • Venous ulcer fibroblasts compared to normal fibroblasts, show differences in collagen but not fibronectin production under both normal and hypoxic conditions
    • Herrick SE, Ireland GW, Simon D, McCollum CN, and Ferguson MWJ (1996). Venous ulcer fibroblasts compared to normal fibroblasts, show differences in collagen but not fibronectin production under both normal and hypoxic conditions. J Invest Dermatol 106:187-193.
    • (1996) J Invest Dermatol , vol.106 , pp. 187-193
    • Herrick, S.E.1    Ireland, G.W.2    Simon, D.3    McCollum, C.N.4    Ferguson, M.W.J.5
  • 13
    • 0026437639 scopus 로고
    • Sequential changes in the histological pattern and extracellular matrix deposition during the healing of chronic venous ulcers
    • Herrick SE, Sloan P, McGurk M, Freak L, McCollum CN, and Ferguson MWJ (1992). Sequential changes in the histological pattern and extracellular matrix deposition during the healing of chronic venous ulcers. Am J Pathol 141:1085-1095.
    • (1992) Am J Pathol , vol.141 , pp. 1085-1095
    • Herrick, S.E.1    Sloan, P.2    McGurk, M.3    Freak, L.4    McCollum, C.N.5    Ferguson, M.W.J.6
  • 14
    • 0022979424 scopus 로고
    • Secretion of metalloproteinases by stimulated capillary endothelial cells
    • Herron GS, Banda MJ, Clark EJ, Gavrilovic J, and Werb Z (1986). Secretion of metalloproteinases by stimulated capillary endothelial cells. J Biol Chem 261:2814-2818.
    • (1986) J Biol Chem , vol.261 , pp. 2814-2818
    • Herron, G.S.1    Banda, M.J.2    Clark, E.J.3    Gavrilovic, J.4    Werb, Z.5
  • 15
    • 0014949207 scopus 로고
    • Cleavage of proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970). Cleavage of proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0002230624 scopus 로고
    • Extracellular matrix degradation
    • Royce P and Steinmann B, editors. New York: Wiley-Liss and Sons
    • Murphy G and Reynolds JJ (1993). Extracellular matrix degradation. In: Royce P and Steinmann B, editors. Connective tissue and its heritable disorders. New York: Wiley-Liss and Sons, 287-316.
    • (1993) Connective Tissue and Its Heritable Disorders , pp. 287-316
    • Murphy, G.1    Reynolds, J.J.2
  • 19
    • 0018747530 scopus 로고
    • Mapping the extended substrate site of Cathepsin G and human leucocyte elastase
    • Nakajima K, Powers JC, Ashe BM, and Zimmerman M (1979). Mapping the extended substrate site of Cathepsin G and human leucocyte elastase. J Biol Chem 254:4027-4032.
    • (1979) J Biol Chem , vol.254 , pp. 4027-4032
    • Nakajima, K.1    Powers, J.C.2    Ashe, B.M.3    Zimmerman, M.4
  • 20
    • 0028865394 scopus 로고
    • Cell surface-bound elastase and cathepsin G on human neutrophils: A novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases
    • Owen CA, Campbell MA, Sannes PL, Boukedes SS, and Campbell EJ (1995). Cell surface-bound elastase and cathepsin G on human neutrophils: A novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases. J Cell Biol 131:775-789.
    • (1995) J Cell Biol , vol.131 , pp. 775-789
    • Owen, C.A.1    Campbell, M.A.2    Sannes, P.L.3    Boukedes, S.S.4    Campbell, E.J.5
  • 23
    • 0028973014 scopus 로고
    • α1-antitrypsin is degraded and non-functional in chronic wounds but intact and functional in acute wounds: The inhibitior protects fibronectin from degradation by chronic wound fluid enzymes
    • Rao C, Ladin D, Liu Y, Chilukuri K, Hou Z, and Woodley D (1995). α1-antitrypsin is degraded and non-functional in chronic wounds but intact and functional in acute wounds: The inhibitior protects fibronectin from degradation by chronic wound fluid enzymes. J Invest Dermatol 105:572-578.
    • (1995) J Invest Dermatol , vol.105 , pp. 572-578
    • Rao, C.1    Ladin, D.2    Liu, Y.3    Chilukuri, K.4    Hou, Z.5    Woodley, D.6
  • 24
    • 0022929937 scopus 로고
    • Fibronectin synthesis and degradation in human fibroblasts with aging
    • Shevitz J, Jenkins CSP, and Hatcher VB (1986). Fibronectin synthesis and degradation in human fibroblasts with aging. Mech Ageing Dev 35:221-232.
    • (1986) Mech Ageing Dev , vol.35 , pp. 221-232
    • Shevitz, J.1    Jenkins, C.S.P.2    Hatcher, V.B.3
  • 25
    • 0021027518 scopus 로고
    • Age-related decline in lysosomal enzyme release from polymorphnuclear leukocytes after n-formyl-methioyl-leucyl-phenylalanine stimulation
    • Suzuki K, Swenson C, Sasagawa S, Sakatani T, Watanabe M, Kobayashi M, and Fuijkura T (1983). Age-related decline in lysosomal enzyme release from polymorphnuclear leukocytes after n-formyl-methioyl-leucyl-phenylalanine stimulation. Exp Hematol 11:1005-1013.
    • (1983) Exp Hematol , vol.11 , pp. 1005-1013
    • Suzuki, K.1    Swenson, C.2    Sasagawa, S.3    Sakatani, T.4    Watanabe, M.5    Kobayashi, M.6    Fuijkura, T.7
  • 26
    • 0026495389 scopus 로고
    • Similar, but not identical, modulation of expression of extracellular matrix components during in vitro and in vivo aging of human skin fibroblasts
    • Takeda K, Gosiewska A, and Peterkofsky B (1992). Similar, but not identical, modulation of expression of extracellular matrix components during in vitro and in vivo aging of human skin fibroblasts. J Cell Physiol 153:450-459.
    • (1992) J Cell Physiol , vol.153 , pp. 450-459
    • Takeda, K.1    Gosiewska, A.2    Peterkofsky, B.3
  • 27
    • 0023900470 scopus 로고
    • Fibronectin degradation products containing the cytoadhesive tetrapeptide stimulate human neutrophil degranulation
    • Wachtfogel YT, Abrams W, Kucich U, Weinbaum G, Schapira M, and Colman RW (1988). Fibronectin degradation products containing the cytoadhesive tetrapeptide stimulate human neutrophil degranulation. J Clin Invest 81:1310-1316.
    • (1988) J Clin Invest , vol.81 , pp. 1310-1316
    • Wachtfogel, Y.T.1    Abrams, W.2    Kucich, U.3    Weinbaum, G.4    Schapira, M.5    Colman, R.W.6
  • 28
    • 0024602827 scopus 로고
    • Tissue destruction by neutrophils
    • Weiss SJ (1989). Tissue destruction by neutrophils. N Engl J Med 320:365-376.
    • (1989) N Engl J Med , vol.320 , pp. 365-376
    • Weiss, S.J.1
  • 29
    • 0021361308 scopus 로고
    • Neutrophils degrade subendothelial matrices in the presence of alpha-1-proteinase inhibitor
    • Weiss SJ and Regiani S (1984). Neutrophils degrade subendothelial matrices in the presence of alpha-1-proteinase inhibitor. J Clin Invest 73:1297-1303.
    • (1984) J Clin Invest , vol.73 , pp. 1297-1303
    • Weiss, S.J.1    Regiani, S.2
  • 30
    • 0024335963 scopus 로고
    • Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression
    • Werb A, Temble PM, Behrendtsen O, Crowley E, and Damsky CH (1989). Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression. J Cell Biol 109:877-889.
    • (1989) J Cell Biol , vol.109 , pp. 877-889
    • Werb, A.1    Temble, P.M.2    Behrendtsen, O.3    Crowley, E.4    Damsky, C.H.5
  • 31
    • 0027202705 scopus 로고
    • Wound fluid from chronic leg ulcers contains elevated levels of metalloproteinases MMP-2 and MMP-9
    • Wysocki AB, Staiano-Coico L, and Grinnell F (1993). Wound fluid from chronic leg ulcers contains elevated levels of metalloproteinases MMP-2 and MMP-9. J Invest Dermatol 101:64-68.
    • (1993) J Invest Dermatol , vol.101 , pp. 64-68
    • Wysocki, A.B.1    Staiano-Coico, L.2    Grinnell, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.