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Volumn 133, Issue 9, 1998, Pages 1002-1006

Augmented inflammatory responses and altered wound healing in cathepsin G-deficient mice

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN G; MYELOPEROXIDASE;

EID: 0031716089     PISSN: 00040010     EISSN: None     Source Type: Journal    
DOI: 10.1001/archsurg.133.9.1002     Document Type: Article
Times cited : (42)

References (31)
  • 1
    • 0002282084 scopus 로고
    • Oxygen-independent antimicrobial systems of phagocytosis
    • Gallin JI, Goldstein IM, Snyderman R, eds. New York, NY: Raven Press
    • Elsbach P, Weiss J. Oxygen-independent antimicrobial systems of phagocytosis. In: Gallin JI, Goldstein IM, Snyderman R, eds. Inflammation: Basic Principles and Clinical Correlates. New York, NY: Raven Press; 1992:603-636.
    • (1992) Inflammation: Basic Principles and Clinical Correlates , pp. 603-636
    • Elsbach, P.1    Weiss, J.2
  • 2
    • 0001883969 scopus 로고
    • Oxygen metabolites from phagocytes
    • Gallin JI, Goldstein IM, Snyderman R, eds. New York, NY: Raven Press
    • Klebanoff SJ. Oxygen metabolites from phagocytes. In: Gallin JI, Goldstein IM, Snyderman R, eds. Inflammation: Basic Principles and Clinical Correlates. New York, NY: Raven Press; 1992:541-601.
    • (1992) Inflammation: Basic Principles and Clinical Correlates , pp. 541-601
    • Klebanoff, S.J.1
  • 3
    • 0015383163 scopus 로고
    • The neutrophilic leukocyte in wound repair: A study with antineutrophil serum
    • Simpson DM, Ross R. The neutrophilic leukocyte in wound repair: a study with antineutrophil serum. J Clin Invest. 1972;51:2009-2023.
    • (1972) J Clin Invest , vol.51 , pp. 2009-2023
    • Simpson, D.M.1    Ross, R.2
  • 4
    • 0016428338 scopus 로고
    • The role of the macrophage in wound repair: A study with hydrocortisone and antimacrophage serum
    • Leibovich SJ, Ross R. The role of the macrophage in wound repair: a study with hydrocortisone and antimacrophage serum. Am J Pathol. 1975;78:71-100.
    • (1975) Am J Pathol , vol.78 , pp. 71-100
    • Leibovich, S.J.1    Ross, R.2
  • 6
    • 0000610029 scopus 로고
    • Neutrophils in human diseases
    • Malech HD, Gallin JI. Neutrophils in human diseases. N Engl J Med. 1988;37: 687-694.
    • (1988) N Engl J Med , vol.37 , pp. 687-694
    • Malech, H.D.1    Gallin, J.I.2
  • 7
    • 0015139958 scopus 로고
    • The development of polymorphonuclear neutrophilic leukocytes in the human bone marrow
    • Bainton DF, Ullyot JL, Farquhar MG. The development of polymorphonuclear neutrophilic leukocytes in the human bone marrow. J Exp Med. 1971;134: 907-934.
    • (1971) J Exp Med , vol.134 , pp. 907-934
    • Bainton, D.F.1    Ullyot, J.L.2    Farquhar, M.G.3
  • 8
    • 0028865394 scopus 로고
    • A 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, et al. A 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. 1995;131:775-789.
    • (1995) J Cell Biol , vol.131 , pp. 775-789
    • Owen, C.A.1    Campbell, M.A.2    Sannes, P.L.3
  • 9
    • 0023951925 scopus 로고
    • Cathepsin G is a strong platelet agonist released by neutrophils
    • Selak MA, Chignard M, Smith JB. Cathepsin G is a strong platelet agonist released by neutrophils. J Biochem (Tokyo). 1988;251:293-299.
    • (1988) J Biochem (Tokyo) , vol.251 , pp. 293-299
    • Selak, M.A.1    Chignard, M.2    Smith, J.B.3
  • 10
    • 0025965846 scopus 로고
    • Human lysosomal cathepsin G and granzyme B share a functionally conserved broad spectrum antibacterial peptide
    • Shafer WM, Polh J, Onunka VC, et al. Human lysosomal cathepsin G and granzyme B share a functionally conserved broad spectrum antibacterial peptide. J Biochem. 1991;266:112-116.
    • (1991) J Biochem , vol.266 , pp. 112-116
    • Shafer, W.M.1    Polh, J.2    Onunka, V.C.3
  • 11
    • 0020312338 scopus 로고
    • Rapid conversion of angiotensin I to angiotensin II by neutrophil and mast cell proteinases
    • Reily CF, Tewksbury DA, Schechter NM, Travis J. Rapid conversion of angiotensin I to angiotensin II by neutrophil and mast cell proteinases. J Biol Chem. 1982; 257:8619-8622.
    • (1982) J Biol Chem , vol.257 , pp. 8619-8622
    • Reily, C.F.1    Tewksbury, D.A.2    Schechter, N.M.3    Travis, J.4
  • 12
    • 0026666102 scopus 로고
    • Cathepsin G: A regulator of human vitamin K dependent clotting factors and inhibitors
    • Turkington PT. Cathepsin G: a regulator of human vitamin K dependent clotting factors and inhibitors. Thromb Res. 1992;67:147-155.
    • (1992) Thromb Res , vol.67 , pp. 147-155
    • Turkington, P.T.1
  • 13
    • 0025732513 scopus 로고
    • Cathepsin G and leukocyte elastase inactivate human tumor necrosis factor and lymphotoxin
    • Scuderi P, Nez PA, Derr ML, et al. Cathepsin G and leukocyte elastase inactivate human tumor necrosis factor and lymphotoxin. Cell Immunol. 1991;135:299-313.
    • (1991) Cell Immunol , vol.135 , pp. 299-313
    • Scuderi, P.1    Nez, P.A.2    Derr, M.L.3
  • 14
    • 0028136620 scopus 로고
    • Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3
    • Padrines M, Wolf M, Walz A, Baggiolini M. Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3. FEBS Lett. 1994;352:231-235.
    • (1994) FEBS Lett , vol.352 , pp. 231-235
    • Padrines, M.1    Wolf, M.2    Walz, A.3    Baggiolini, M.4
  • 15
    • 0025220123 scopus 로고
    • Processing of precursor interleukin-1 beta and inflammatory disease
    • Hazuda DJ, Strickler J, Kueppers F, et al. Processing of precursor interleukin-1 beta and inflammatory disease. J Biol Chem. 1990;265:6318-6322.
    • (1990) J Biol Chem , vol.265 , pp. 6318-6322
    • Hazuda, D.J.1    Strickler, J.2    Kueppers, F.3
  • 16
    • 0024313227 scopus 로고
    • Cathepsin G degrades denatured collagen
    • Capodici C, Berg RA. Cathepsin G degrades denatured collagen. Inflammation. 1989;13:137-145.
    • (1989) Inflammation , vol.13 , pp. 137-145
    • Capodici, C.1    Berg, R.A.2
  • 17
    • 0016793671 scopus 로고
    • Identification of neutral proteases in human neutrophil granules that degrade articular cartilage proteoglycan
    • Malemud CJ, Janoff A. Identification of neutral proteases in human neutrophil granules that degrade articular cartilage proteoglycan. Arthritis Rheum. 1975; 18:361-368.
    • (1975) Arthritis Rheum , vol.18 , pp. 361-368
    • Malemud, C.J.1    Janoff, A.2
  • 18
    • 0018876040 scopus 로고
    • The degradation of human lung elastin by neutrophil proteinases
    • Reilly CF, Travis J. The degradation of human lung elastin by neutrophil proteinases. Biochim Biophys Acta. 1980;621:147-157.
    • (1980) Biochim Biophys Acta , vol.621 , pp. 147-157
    • Reilly, C.F.1    Travis, J.2
  • 19
    • 0019876460 scopus 로고
    • Susceptibility of soluble and matrix fibronectins to degradation by tissue proteinases, mast cell chymase, and cathepsin G
    • Vartio T, Seppa H, Vaheri A. Susceptibility of soluble and matrix fibronectins to degradation by tissue proteinases, mast cell chymase, and cathepsin G. J Biol Chem. 1981;256:471-477.
    • (1981) J Biol Chem , vol.256 , pp. 471-477
    • Vartio, T.1    Seppa, H.2    Vaheri, A.3
  • 20
    • 0023262932 scopus 로고
    • Accelerated healing of incisional wounds in rats induced by TGF-beta
    • Mustoe TA, Pierce GF, Thomason A, et al. Accelerated healing of incisional wounds in rats induced by TGF-beta. Science. 1987;237:1333-1336.
    • (1987) Science , vol.237 , pp. 1333-1336
    • Mustoe, T.A.1    Pierce, G.F.2    Thomason, A.3
  • 21
    • 0028344688 scopus 로고
    • Myeloperoxidase as a biomarker of skin irritation and inflammation
    • Trush MA, Egner PA, Kensler TW. Myeloperoxidase as a biomarker of skin irritation and inflammation. Food Chem Toxicol. 1994;32:143-147.
    • (1994) Food Chem Toxicol , vol.32 , pp. 143-147
    • Trush, M.A.1    Egner, P.A.2    Kensler, T.W.3
  • 22
    • 0028937893 scopus 로고
    • Separation of neutrophils from blood in human and laboratory animals and comparison of the chemotaxis
    • Sugawara T, Miyamoto M, Takayama S, Kato M. Separation of neutrophils from blood in human and laboratory animals and comparison of the chemotaxis. J Pharmacol Toxicol Methods. 1995;33:91-100.
    • (1995) J Pharmacol Toxicol Methods , vol.33 , pp. 91-100
    • Sugawara, T.1    Miyamoto, M.2    Takayama, S.3    Kato, M.4
  • 23
    • 0023065580 scopus 로고
    • Mechanisms and prevention of decrease in wound margin strength in intestinal anastomosis and laparatomy wounds
    • Hogstrom H. Mechanisms and prevention of decrease in wound margin strength in intestinal anastomosis and laparatomy wounds. Acta Chem Scand. 1987;539: 1-63.
    • (1987) Acta Chem Scand , vol.539 , pp. 1-63
    • Hogstrom, H.1
  • 24
    • 0026066372 scopus 로고
    • Neutrophil-dependent decrease in early wound margin strength
    • Jonsson T, Hogstrom H. Neutrophil-dependent decrease in early wound margin strength. Arch Surg. 1991;126:1423-1426.
    • (1991) Arch Surg , vol.126 , pp. 1423-1426
    • Jonsson, T.1    Hogstrom, H.2
  • 25
    • 0014591928 scopus 로고
    • The tensile strength of wounds and factors that influence it
    • Van Winkle W Jr. The tensile strength of wounds and factors that influence it. Surg Gynecol Obstet. 1969;129:819-842.
    • (1969) Surg Gynecol Obstet , vol.129 , pp. 819-842
    • Van Winkle Jr., W.1
  • 26
    • 0026350538 scopus 로고
    • Tumor necrosis factor-alpha inhibits wound healing in the rat
    • Rapala K, Laato M, Niinikoski J, et al. Tumor necrosis factor-alpha inhibits wound healing in the rat. Eur Surg Res. 1991;23:261-268.
    • (1991) Eur Surg Res , vol.23 , pp. 261-268
    • Rapala, K.1    Laato, M.2    Niinikoski, J.3
  • 27
    • 0027522833 scopus 로고
    • Tumor necrosis factor inhibits in vivo collagen synthesis
    • Regan MC, Kirk SJ, Hurson M, et al. Tumor necrosis factor inhibits in vivo collagen synthesis. Surgery. 1993;113:173-177.
    • (1993) Surgery , vol.113 , pp. 173-177
    • Regan, M.C.1    Kirk, S.J.2    Hurson, M.3
  • 28
    • 0027768570 scopus 로고
    • Cytokine regulation of metalloproteinase gene expression
    • Mauviel A. Cytokine regulation of metalloproteinase gene expression. J Cell Biochem. 1993;53:288-295.
    • (1993) J Cell Biochem , vol.53 , pp. 288-295
    • Mauviel, A.1
  • 29
    • 0030909623 scopus 로고    scopus 로고
    • Tumor necrosis factor mediates impaired wound healing in chronic abdominal sepsis
    • Cooney R, Iocono J, Maish G, et al. Tumor necrosis factor mediates impaired wound healing in chronic abdominal sepsis. J Trauma. 1997;42:415-420.
    • (1997) J Trauma , vol.42 , pp. 415-420
    • Cooney, R.1    Iocono, J.2    Maish, G.3
  • 31
    • 0024536234 scopus 로고
    • Macrophage phagocytosis of aging neutrophils in inflammation: Programmed cell death leads to its recognition by macrophages
    • Savill JS, Wyllie AH, Henson JE, et al. Macrophage phagocytosis of aging neutrophils in inflammation: programmed cell death leads to its recognition by macrophages. J Clin Invest. 1989;83:865-875.
    • (1989) J Clin Invest , vol.83 , pp. 865-875
    • Savill, J.S.1    Wyllie, A.H.2    Henson, J.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.