메뉴 건너뛰기




Volumn 16, Issue 6, 1997, Pages 625-638

Enhanced serine protease activities in the sulfur mustard-exposed homogenates of hairless guinea pig skin

Author keywords

Chymase; Elastase; Inhibitor; Serine protease; Substrate; Sulfur mustard; Trypsin

Indexed keywords

ASPARTATE AMMONIA LYASE; CHROMOGENIC SUBSTRATE; CHYMASE; ELASTASE; ELASTASE INHIBITOR; MUSTARD GAS; SERINE PROTEINASE; TRYPSIN INHIBITOR; TRYPTASE;

EID: 0030812735     PISSN: 10915818     EISSN: None     Source Type: Journal    
DOI: 10.1080/109158197226937     Document Type: Article
Times cited : (12)

References (26)
  • 1
    • 7344266820 scopus 로고
    • Estimation of neutrophil infiltration into hairless guinea pig skin treated with 2,2′-dichlorodiethyl sulfide
    • Bongiovanni, R., Millard, C. B., Schulz, S. M., and Romano, J. M. 1993. Estimation of neutrophil infiltration into hairless guinea pig skin treated with 2,2′-dichlorodiethyl sulfide. Proc. 1993 Medical Defense Biosci. Rev. 1:389-395.
    • (1993) Proc. 1993 Medical Defense Biosci. Rev. , vol.1 , pp. 389-395
    • Bongiovanni, R.1    Millard, C.B.2    Schulz, S.M.3    Romano, J.M.4
  • 2
    • 0021684932 scopus 로고
    • Kinetics of hydrolysis of peptide thioester derivatives of arginine by human and bovine thrombins
    • Cook, R. R., McRae, B. J., and Powers, J. C. 1984. Kinetics of hydrolysis of peptide thioester derivatives of arginine by human and bovine thrombins. Arch. Biochem. Biophys. 234:82-88.
    • (1984) Arch. Biochem. Biophys. , vol.234 , pp. 82-88
    • Cook, R.R.1    McRae, B.J.2    Powers, J.C.3
  • 3
    • 0026784492 scopus 로고
    • Inhibition of sulfur mustard-increased protease activity by niacinamide, N-acetyl-L-cysteine or dexamethasone
    • Cowan, F. M., Broomfield, C. A., and Smith, W. J. 1992. Inhibition of sulfur mustard-increased protease activity by niacinamide, N-acetyl-L-cysteine or dexamethasone. Cell Biol. Toxicol. 8:129-138.
    • (1992) Cell Biol. Toxicol. , vol.8 , pp. 129-138
    • Cowan, F.M.1    Broomfield, C.A.2    Smith, W.J.3
  • 6
    • 0024461432 scopus 로고
    • Response of mouse brain to a single subcutaneous injection of the monofunctional sulfur mustard, butyl 2-chloroethyl sulfide (BCS)
    • Elsayed, N. B., Omaye, S. T., Klain, G. J., Inase, J. L., Dahlberg, E. T., Wheeler, C. R., and Korte, D. W. 1989. Response of mouse brain to a single subcutaneous injection of the monofunctional sulfur mustard, butyl 2-chloroethyl sulfide (BCS). Toxicology 58:11-20.
    • (1989) Toxicology , vol.58 , pp. 11-20
    • Elsayed, N.B.1    Omaye, S.T.2    Klain, G.J.3    Inase, J.L.4    Dahlberg, E.T.5    Wheeler, C.R.6    Korte, D.W.7
  • 7
    • 50549163362 scopus 로고
    • Preparation and properties of two new chromogenic substrates of trypsin
    • Erlanger, B. F., Kokowsky, N., and Cohen, W. 1961. Preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochem. Biophys. 95:271-278.
    • (1961) Arch. Biochem. Biophys. , vol.95 , pp. 271-278
    • Erlanger, B.F.1    Kokowsky, N.2    Cohen, W.3
  • 8
    • 0016801316 scopus 로고
    • Use of N-benzoyl-L-tyrosine thiobenzyl ester as a protease substrate. Hydrolysis by α-chymotrypsin and subtilisin BPN
    • Farmer, D. A., and Hageman, J. H. 1975. Use of N-benzoyl-L-tyrosine thiobenzyl ester as a protease substrate. Hydrolysis by α-chymotrypsin and subtilisin BPN'. J. Biol. Chem. 250:7366-7371.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7366-7371
    • Farmer, D.A.1    Hageman, J.H.2
  • 9
    • 0019807240 scopus 로고
    • Reaction of peptidyl thiobenzyl esters with mammalian chymotrypsin like enzymes: A sensitive assay method
    • Harper, J. W., Ramirez, G., and Powers, J. C. 1981. Reaction of peptidyl thiobenzyl esters with mammalian chymotrypsin like enzymes: A sensitive assay method. Anal. Biochem. 118:382-387.
    • (1981) Anal. Biochem. , vol.118 , pp. 382-387
    • Harper, J.W.1    Ramirez, G.2    Powers, J.C.3
  • 11
    • 0028942267 scopus 로고
    • Mammalian tissue trypsin-like enzymes: Substrate specificity and inhibitory potency of substituted isocoumarin mechanism-based inhibitors, benzamidine derivatives, and arginine fluoroalkylketone transition-state inhibitors
    • Kam, C.-M., Hernandez, M. A., Patil, G. S., Ueda, T., Simmons, W. H., Braganza, V. J., and Powers, J. C. 1995. Mammalian tissue trypsin-like enzymes: Substrate specificity and inhibitory potency of substituted isocoumarin mechanism-based inhibitors, benzamidine derivatives, and arginine fluoroalkylketone transition-state inhibitors. Arch. Biochem. Biophys. 316: 808-814.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 808-814
    • Kam, C.-M.1    Hernandez, M.A.2    Patil, G.S.3    Ueda, T.4    Simmons, W.H.5    Braganza, V.J.6    Powers, J.C.7
  • 12
    • 9844231015 scopus 로고
    • The prevention of 2,2′-dichlorodiethyl sulfide (sulfur mustard, HD) cytotoxicity in human lymphocytes by inhibitors of poly(ADP-ribose) polymerase
    • Meier, H. L., Gross, C. L., Graham, L. M., Lusco, C. T., and Johnson, J. B. 1987. The prevention of 2,2′-dichlorodiethyl sulfide (sulfur mustard, HD) cytotoxicity in human lymphocytes by inhibitors of poly(ADP-ribose) polymerase. Proc. Sixth Medical Chemical Defense Biosci. Rev. 313-316.
    • (1987) Proc. Sixth Medical Chemical Defense Biosci. Rev. , pp. 313-316
    • Meier, H.L.1    Gross, C.L.2    Graham, L.M.3    Lusco, C.T.4    Johnson, J.B.5
  • 14
    • 0018862652 scopus 로고
    • Plasminogen activator: Induction of synthesis by DNA damage
    • Miskin, R., and Reich, E. 1980. Plasminogen activator: Induction of synthesis by DNA damage. Cell 190:217.
    • (1980) Cell , vol.190 , pp. 217
    • Miskin, R.1    Reich, E.2
  • 16
    • 0025971396 scopus 로고
    • Human and murine cytotoxic T lymphocyte serine proteases: Subsite mapping with peptide thioester substrates and inhibition of enzyme activity and cytolysis by isocoumarins
    • Odake, S., Kam, C. M., Narasimhan, L., Poe, M., Blake, J. T., Krahenbuhl, O., Tschopp, J., and Powers, J. C. 1991. Human and murine cytotoxic T lymphocyte serine proteases: Subsite mapping with peptide thioester substrates and inhibition of enzyme activity and cytolysis by isocoumarins. Biochemistry 30:2217-2227.
    • (1991) Biochemistry , vol.30 , pp. 2217-2227
    • Odake, S.1    Kam, C.M.2    Narasimhan, L.3    Poe, M.4    Blake, J.T.5    Krahenbuhl, O.6    Tschopp, J.7    Powers, J.C.8
  • 17
    • 0028057482 scopus 로고
    • Novel amidine-containing peptidyl phosphonates as irreversible inhibitors for blood coagulation and related serine proteases
    • Oleksyszyn, J., Boduszek, B., Kam, C. M., and Powers, J. C. 1994. Novel amidine-containing peptidyl phosphonates as irreversible inhibitors for blood coagulation and related serine proteases. J. Med. Chem. 37:226-231.
    • (1994) J. Med. Chem. , vol.37 , pp. 226-231
    • Oleksyszyn, J.1    Boduszek, B.2    Kam, C.M.3    Powers, J.C.4
  • 18
    • 3643108880 scopus 로고
    • Does apoptosis (programmed cell death) play a role in sulfur mustard injury?
    • Papirmeister, B. 1994. Does apoptosis (programmed cell death) play a role in sulfur mustard injury? Med. Chem. Defense Bull. Res. Dev. 7:1-12.
    • (1994) Med. Chem. Defense Bull. Res. Dev. , vol.7 , pp. 1-12
    • Papirmeister, B.1
  • 21
    • 0017732763 scopus 로고
    • Specificity for porcine pancreatic elastase, human leukocyte elastase, and cathepsin G. Inhibition with peptide chloromethyl ketones
    • Powers, J. C., Gupton, B. F., Harley, A. D., Nishino, N., and Whitley, R. J. 1977. Specificity for porcine pancreatic elastase, human leukocyte elastase, and cathepsin G. Inhibition with peptide chloromethyl ketones. Biochem. Biophys. Acta 485:158-166.
    • (1977) Biochem. Biophys. Acta , vol.485 , pp. 158-166
    • Powers, J.C.1    Gupton, B.F.2    Harley, A.D.3    Nishino, N.4    Whitley, R.J.5
  • 22
    • 0021879888 scopus 로고
    • Mammalian chymotrypsin-like enzymes. Comparative reactivities of rat mast cell proteases, human and dog skin chymases, and human cathepsin G with 4-nitroanilide substrates, and peptide chloromethyl ketone and sulfonyl fluoride inhibitors
    • Powers, J. C., Tanaka, T., Harper, J. W., Minematsu, Y., Barker, L., Lincoln, D., Crumley, K. W., Fraki, J. E., Schechter, N. M., Lazarus, G. G., Nakajima, K., Nakashino, K., Neurath, H., and Woodbury, R. G. 1985. Mammalian chymotrypsin-like enzymes. Comparative reactivities of rat mast cell proteases, human and dog skin chymases, and human cathepsin G with 4-nitroanilide substrates, and peptide chloromethyl ketone and sulfonyl fluoride inhibitors. Biochemistry 24:2048-2058.
    • (1985) Biochemistry , vol.24 , pp. 2048-2058
    • Powers, J.C.1    Tanaka, T.2    Harper, J.W.3    Minematsu, Y.4    Barker, L.5    Lincoln, D.6    Crumley, K.W.7    Fraki, J.E.8    Schechter, N.M.9    Lazarus, G.G.10    Nakajima, K.11    Nakashino, K.12    Neurath, H.13    Woodbury, R.G.14
  • 23
    • 0014211618 scopus 로고
    • On the size of the active site in protease. 1. Papain
    • Schecter, I., and Berger, A. 1967. On the size of the active site in protease. 1. Papain. Biochem. Biophys. Res. Commun. 27:157-162.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schecter, I.1    Berger, A.2
  • 24
    • 0021044821 scopus 로고
    • Mammalian tissue trypsin-like enzymes. Comparative reactivities of human skin tryptase, human lung tryptase and bovine trypsin with peptide 4-nitroanilide and thioester substrates
    • Tanaka, T., McRae, B. J., Cho, K., Cook, R., Fraki, J. E., Johnson, D. A., and Powers, J. C. 1983. Mammalian tissue trypsin-like enzymes. Comparative reactivities of human skin tryptase, human lung tryptase and bovine trypsin with peptide 4-nitroanilide and thioester substrates. J. Biol. Chem. 258:13552-13557.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13552-13557
    • Tanaka, T.1    McRae, B.J.2    Cho, K.3    Cook, R.4    Fraki, J.E.5    Johnson, D.A.6    Powers, J.C.7
  • 25
    • 0019320457 scopus 로고
    • Substrate specificity of two chymotrypsin-like proteases from rat mast cells. Studies with peptide 4-nitroanilides and comparison with cathepsin G
    • Yoshida, N., Everitt, M. T., Neurath, H., Woodbury, R. G., and Powers, J. C. 1980. Substrate specificity of two chymotrypsin-like proteases from rat mast cells. Studies with peptide 4-nitroanilides and comparison with cathepsin G. Biochemistry 19:5799-5804.
    • (1980) Biochemistry , vol.19 , pp. 5799-5804
    • Yoshida, N.1    Everitt, M.T.2    Neurath, H.3    Woodbury, R.G.4    Powers, J.C.5
  • 26
    • 77957176428 scopus 로고
    • Niacinamide pretreatment reduces microvesicle formation in hairless guinea pigs cutaneously exposed to sulfur mustard
    • Yourick, J. J., Clark, C. R., and Mitcheltree, L. W. 1991. Niacinamide pretreatment reduces microvesicle formation in hairless guinea pigs cutaneously exposed to sulfur mustard. Fundam. Appl. Toxicol. 17:533-542.
    • (1991) Fundam. Appl. Toxicol. , vol.17 , pp. 533-542
    • Yourick, J.J.1    Clark, C.R.2    Mitcheltree, L.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.