메뉴 건너뛰기




Volumn 57, Issue 6, 1999, Pages 431-442

Activity of cathepsin G, elastase, and their inhibitors in plasma during methanol intoxication

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN; ALPHA 2 MACROGLOBULIN; CATHEPSIN G; ELASTASE; FORMALDEHYDE; FREE RADICAL; METHANOL; PROTEINASE; PROTEINASE INHIBITOR;

EID: 0032813010     PISSN: 15287394     EISSN: 10872620     Source Type: Journal    
DOI: 10.1080/009841099157629     Document Type: Article
Times cited : (4)

References (39)
  • 1
    • 0019193338 scopus 로고
    • Identification of 4-hydroxynonenal as a cytotoxic product originating from the peroxidation of liver microsomal lipids
    • Benedetti, A., Comporti, M., and Esterbauer, H. 1980. Identification of 4-hydroxynonenal as a cytotoxic product originating from the peroxidation of liver microsomal lipids. Biochem. Biophys. Acta 620:281-96.
    • (1980) Biochem. Biophys. Acta , vol.620 , pp. 281-296
    • Benedetti, A.1    Comporti, M.2    Esterbauer, H.3
  • 2
    • 0016363174 scopus 로고
    • The synthesis and analytical use of highly sensitive and convenient substrate of elastase
    • Bieth, J., Spieces, B., and Wermuth, C. G. 1974. The synthesis and analytical use of highly sensitive and convenient substrate of elastase. Biochem. Med. 11:350-357
    • (1974) Biochem. Med. , vol.11 , pp. 350-357
    • Bieth, J.1    Spieces, B.2    Wermuth, C.G.3
  • 3
    • 0023156723 scopus 로고
    • Stimulated release of neutral proteinases elastase and cathepsin G from inflammatory rat polymorphonuclear l eukocytes
    • Bray, M. A., McKearn-Smith, C., Metz-Virca, G., Bodmer, J. L., and Virca, G. D. 1987. Stimulated release of neutral proteinases elastase and cathepsin G from inflammatory rat polymorphonuclear l eukocytes. Inflammation 11:23-37.
    • (1987) Inflammation , vol.11 , pp. 23-37
    • Bray, M.A.1    McKearn-Smith, C.2    Metz-Virca, G.3    Bodmer, J.L.4    Virca, G.D.5
  • 4
    • 0026602386 scopus 로고
    • Inhibition of neutrophil superoxide production by human plasma alpha-antitrypsin
    • Bucurenci, N., Blake, R., Chidwick, K., and Winyard, P. G. 1992. Inhibition of neutrophil superoxide production by human plasma alpha-antitrypsin. FEBS Lett. 300:21-34.
    • (1992) FEBS Lett , vol.300 , pp. 21-34
    • Bucurenci, N.1    Blake, R.2    Chidwick, K.3    Winyard, P.G.4
  • 5
    • 0027944443 scopus 로고
    • Alterations in mitochondrial membrane fluidity by lipid peroxidation products
    • Chen, J. J., and Yu, B. P. 1984. Alterations in mitochondrial membrane fluidity by lipid peroxidation products. Free Radical Biol. Med. 17:411-418.
    • (1984) Free Radical Biol. Med. , vol.17 , pp. 411-418
    • Chen, J.J.1    Yu, B.P.2
  • 6
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals. I. General aspects
    • Davies, K. J. A. 1987. Protein damage and degradation by oxygen radicals. I. General aspects.J. Biol. Chem. 262:9895-9901.
    • (1987) J. Biol. Chem , vol.262 , pp. 9895-9901
    • Davies, K.J.A.1
  • 7
    • 0023655407 scopus 로고
    • Protein damage and degradation by oxygen radicals. II. Modification of amino acids
    • Davies, K. J. A., Delsignore, M. E., and Lin, S. W. 1987. Protein damage and degradation by oxygen radicals. II. Modification of amino acids. J. Biol. Chem. 262:9902-9920.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9902-9920
    • Davies, K.J.A.1    Delsignore, M.E.2    Lin, S.W.3
  • 8
    • 0023655531 scopus 로고
    • Protein damage and degradation by oxygen radicals. III. Modification of secondary and tertiary structure
    • Davies, K. J. M., and Delsignore, M. E. 1987. Protein damage and degradation by oxygen radicals. III. Modification of secondary and tertiary structure. J. Biol. Chem. 262:9908-9913.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9908-9913
    • Davies, K.J.M.1    Delsignore, M.E.2
  • 9
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malondialdehyde and related aldehydes
    • Esterbauer, H., Schaur, R. J., and Zollner, J. 1991. Chemistry and biochemistry of 4-hydroxynonenal, malondialdehyde and related aldehydes. Free Radical Biol. Med. 11:81-128.
    • (1991) Free Radical Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, J.3
  • 10
    • 0017466886 scopus 로고
    • Reaction of proteins with formaldehyde in the presence and absence of sodium borohydride
    • Galembeck, F., Ryan, J. R., and Feeney, R. E. 1977. Reaction of proteins with formaldehyde in the presence and absence of sodium borohydride. J. Agric. Food Chem. 25:238-245.
    • (1977) J. Agric. Food Chem. , vol.25 , pp. 238-245
    • Galembeck, F.1    Ryan, J.R.2    Feeney, R.E.3
  • 12
    • 0027389280 scopus 로고
    • Formation of peroxides in amino acids proteins exposed to oxygen free radicals
    • Gebicki, S., and Gebicki, J. M. 1993. Formation of peroxides in amino acids proteins exposed to oxygen free radicals. Biochem. J. 289:743-749.
    • (1993) Biochem. J. , vol.289 , pp. 743-749
    • Gebicki, S.1    Gebicki, J.M.2
  • 13
    • 29744466425 scopus 로고
    • Determination of plasma proteins by means of the biuret reaction
    • Gornall, A. C., Bardawill, C. J., and David, H. M. 1949. Determination of plasma proteins by means of the biuret reaction. J. Biol. Chem. 177:751-766.
    • (1949) J. Biol. Chem. , vol.177 , pp. 751-766
    • Gornall, A.C.1    Bardawill, C.J.2    David, H.M.3
  • 14
    • 0018800894 scopus 로고
    • The oxidative inactivation of human a-1-proteinase inhibitor. Further evidence for methionine at the reactive center
    • Johnson, D., and Travis, J. 1979. The oxidative inactivation of human a-1-proteinase inhibitor. Further evidence for methionine at the reactive center. J. Biol. Chem. 254:4022-4026.
    • (1979) J. Biol. Chem. , vol.254 , pp. 4022-4026
    • Johnson, D.1    Travis, J.2
  • 15
    • 0016018008 scopus 로고
    • Rol' fermentativnogo perekisnogo okisleniia fosfolipidov v mekhanizme razborki membran endoplazmaticheskogo retikuluma in vivo
    • Kagan, V. E., Kotelevtsev, S. V., and Kozlov, Iu. P. 1974. Rol' fermentativnogo perekisnogo okisleniia fosfolipidov v mekhanizme razborki membran endoplazmaticheskogo retikuluma in vivo. Dokl. Akad. Nauk (Mosk.) 217:213-216.
    • (1974) Dokl. Akad. Nauk (Mosk.) , vol.217 , pp. 213-216
    • Kagan, V.E.1    Kotelevtsev, S.V.2    Kozlov, I.P.3
  • 17
    • 0023897364 scopus 로고
    • The microsomal ethanol oxidizing system: I ts role in ethanol and xenobiotics metabolism
    • Lieber, C. 1988. The microsomal ethanol oxidizing system: i ts role in ethanol and xenobiotics metabolism. Biochem. Soc. Trans. 16:232-239.
    • (1988) Biochem. Soc. Trans. , vol.16 , pp. 232-239
    • Lieber, C.1
  • 18
    • 0025863482 scopus 로고
    • Methanol and formic acid toxicity: Biochemical mechanisms
    • Liesivuori, J., and Savolainen, H. 1991. Methanol and formic acid toxicity: Biochemical mechanisms. Pharmacol. Toxicol. 69:157-163.
    • (1991) Pharmacol. Toxicol. , vol.69 , pp. 157-163
    • Liesivuori, J.1    Savolainen, H.2
  • 19
  • 20
    • 0027509770 scopus 로고
    • A novel method for measuring antioxidant capacity and its application to monitoring the antioxidant status in premature neonates
    • Miller, N. J., Rice-Evans, C., Davies, M. J., Gopinathan, V., and Milner, A. 1993. A novel method for measuring antioxidant capacity and its application to monitoring the antioxidant status in premature neonates. Clin. Sci. 84:407-412.
    • (1993) Clin. Sci. , vol.84 , pp. 407-412
    • Miller, N.J.1    Rice-Evans, C.2    Davies, M.J.3    Gopinathan, V.4    Milner, A.5
  • 21
    • 0027234009 scopus 로고
    • Liver damage due to free radicals
    • Poli, G. 1993. Liver damage due to free radicals. Br. Med. Bull. 49:604-609.
    • (1993) Br. Med. Bull. , vol.49 , pp. 604-609
    • Poli, G.1
  • 22
    • 0023226343 scopus 로고
    • Protein 4.1in sickle erythrocytes. Evidence for oxidative damage
    • Schwartz, R. S., Rybicki, A. C., Healt, R. H., and Lubin, B. H. 1987 Protein 4.1in sickle erythrocytes. Evidence for oxidative damage. J. Biol. Chem. 262:15666-15672.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15666-15672
    • Schwartz, R.S.1    Rybicki, A.C.2    Healt, R.H.3    Lubin, B.H.4
  • 23
    • 0022625343 scopus 로고
    • Selective oxidation and reduction of methionine residues in peptides and proteins by oxygen exchange between sulfoxide and sulfide
    • Shechter, Y. 1986. Selective oxidation and reduction of methionine residues in peptides and proteins by oxygen exchange between sulfoxide and sulfide. J. Biol. Chem. 26:66-70.
    • (1986) J. Biol. Chem. , vol.26 , pp. 66-70
    • Shechter, Y.1
  • 24
    • 0030894162 scopus 로고    scopus 로고
    • Oxidative stress: Oxidants and antioxidants
    • Sies, H. 1997. Oxidative stress: oxidants and antioxidants. Exp. Physiol. 82:291-295.
    • (1997) Exp. Physiol. , vol.82 , pp. 291-295
    • Sies, H.1
  • 25
    • 0030048270 scopus 로고    scopus 로고
    • The phospholipase C/protein kinase C pathway is involved in cathepsin G-induced human platelet activation: Comparison with thrombin
    • Si-Tahar, M., Renesto, P., Falet, H., Rendu, F., and Chignard, M. 1996. The phospholipase C/protein kinase C pathway is involved in cathepsin G-induced human platelet activation: Comparison with thrombin. Biochem. J. 313:401-408.
    • (1996) Biochem. J. , vol.313 , pp. 401-408
    • Si-Tahar, M.1    Renesto, P.2    Falet, H.3    Rendu, F.4    Chignard, M.5
  • 26
    • 0012155181 scopus 로고
    • Interaction of formaldehyde with amino acids, peptides and proteins
    • Skrzydlewska, E. 1994. Interaction of formaldehyde with amino acids, peptides and proteins. Pol. J. Environ. Stud. 3:13-20.
    • (1994) Pol. J. Environ. Stud. , vol.3 , pp. 13-20
    • Skrzydlewska, E.1
  • 27
    • 0031473693 scopus 로고    scopus 로고
    • Decreased antioxidant defense mechanisms in rats liver after methanol intoxication
    • Skrzydlewska, E., and Farbiszewski, R. 1997a. Decreased antioxidant defense mechanisms in rats liver after methanol intoxication. Free Radical Res. 27:369-375.
    • (1997) Free Radical Res , vol.27 , pp. 369-375
    • Skrzydlewska, E.1    Farbiszewski, R.2
  • 28
    • 0030778547 scopus 로고    scopus 로고
    • Glutathione consumption and inactivation of gluta-tione-related enzymes in liver, erythrocytes and serum of rats after methanol intoxication
    • Skrzydlewska, E., and Farbiszewski, R. 1997b. Glutathione consumption and inactivation of gluta-tione-related enzymes in liver, erythrocytes and serum of rats after methanol intoxication. Arch. Toxicol. 71:741-745.
    • (1997) Arch. Toxicol. , vol.71 , pp. 741-745
    • Skrzydlewska, E.1    Farbiszewski, R.2
  • 29
  • 30
    • 0031010544 scopus 로고    scopus 로고
    • Decrease in accessible thiols as an index of oxidative damage to membrane proteins
    • Soszynski, M., and Bartosz, G. 1997. Decrease in accessible thiols as an index of oxidative damage to membrane proteins. Free Radical Biol. Med. 23:463-469.
    • (1997) Free Radical Biol. Med , vol.23 , pp. 463-469
    • Soszynski, M.1    Bartosz, G.2
  • 31
    • 0024333351 scopus 로고
    • A-Macroglobulin: Structure, shape, and mechanism of proteinase complex formation
    • Sottrup-Jensen, L. 1989. a-Macroglobulin: Structure, shape, and mechanism of proteinase complex formation. J. Biol. Chem. 264:11539-11542.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11539-11542
    • Sottrup-Jensen, L.1
  • 32
    • 0025927934 scopus 로고
    • The toxicity of methanol
    • Tephly, T. R. 1991. The toxicity of methanol. Life Sci. 48:1031-1041.
    • (1991) Life Sci , vol.48 , pp. 1031-1041
    • Tephly, T.R.1
  • 33
    • 85004788499 scopus 로고
    • C13-N.M.R. Characterization of formaldehyde bonds in model mixtures and proteins containing l ysine
    • 13-N.M.R. characterization of formaldehyde bonds in model mixtures and proteins containing l ysine. Int. J. Peptide Protein Res. 25:258-266.
    • (1985) Int. J. Peptide Protein Res. , vol.25 , pp. 258-266
    • Tome, D.1    Naulet, N.2    Kozlowski, A.3
  • 34
    • 0023937510 scopus 로고
    • Structure, function, and control of neutrophil proteinase
    • Travis, J. 1988. Structure, function, and control of neutrophil proteinase. Am. J. Med. 84:37-42.
    • (1988) Am. J. Med. , vol.84 , pp. 37-42
    • Travis, J.1
  • 37
    • 0024602827 scopus 로고
    • Tissue destruction by neutrophils
    • Weiss, S. J. 1989. Tissue destruction by neutrophils. New Engl. J. Med. 320:365-376.
    • (1989) New Engl. J. Med. , vol.320 , pp. 365-376
    • Weiss, S.J.1
  • 38
    • 0024451523 scopus 로고
    • Human leukocyte cathepsin G and elastase specifically suppress thrombin-induced prostacyclin production in human endothelial cells
    • Weksler, B. B., Jaffe, E. A., Brower, M. S., and Cole, O. F. 1989. Human leukocyte cathepsin G and elastase specifically suppress thrombin-induced prostacyclin production in human endothelial cells. Blood 74:1627-1634.
    • (1989) Blood , vol.74 , pp. 1627-1634
    • Weksler, B.B.1    Jaffe, E.A.2    Brower, M.S.3    Cole, O.F.4
  • 39
    • 0019133586 scopus 로고
    • Structure, specificity and localisation of the serine proteases of connective tissue
    • Woodbury, R. G., and Neurath, H. 1980. Structure, specificity and localisation of the serine proteases of connective tissue. FEBS Lett. 114:189-196.
    • (1980) FEBS Lett , vol.114 , pp. 189-196
    • Woodbury, R.G.1    Neurath, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.