메뉴 건너뛰기




Volumn 29, Issue 2, 1997, Pages 353-359

Hydrophobic interactions are involved in the inhibition of human leukocyte elastase by alkyltrimethylammonium salts

Author keywords

Alkyltrimethylammonium bromides; Elastin; Elastolysis; Leukocyte elastase

Indexed keywords

ELASTIN; LEUKOCYTE ELASTASE; TRIMETHYLAMMONIUM SALT DERIVATIVE;

EID: 0030978669     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(96)00108-2     Document Type: Article
Times cited : (5)

References (33)
  • 1
    • 0003064682 scopus 로고
    • Reduction of dimensionality in biological diffusion processes
    • (Eds Rich A. and Davidson N.), Freeman W.H., San Francisco
    • Adam G. and Delbrück M. (1968) Reduction of dimensionality in biological diffusion processes. In Structural Chemistry and Molecular Biology (Eds Rich A. and Davidson N.), pp. 198-215, Freeman W.H., San Francisco.
    • (1968) Structural Chemistry and Molecular Biology , pp. 198-215
    • Adam, G.1    Delbrück, M.2
  • 2
    • 0017324868 scopus 로고
    • Specific inhibition of human granulocyte elastase by cis-unsaturated fatty acids and activation by the corresponding alcohols
    • Ashe B. M. and Zimmerman M. (1977) Specific inhibition of human granulocyte elastase by cis-unsaturated fatty acids and activation by the corresponding alcohols. Biochem. Biophys. Res. Commun. 75, 194-199.
    • (1977) Biochem. Biophys. Res. Commun. , vol.75 , pp. 194-199
    • Ashe, B.M.1    Zimmerman, M.2
  • 3
    • 0018234794 scopus 로고
    • Determination of elastolytic activity using a conductimetric method
    • Bakala H., Wallach J. and Hanss M. (1978) Determination of elastolytic activity using a conductimetric method. Biochimie 60, 1205-1205.
    • (1978) Biochimie , vol.60 , pp. 1205-1205
    • Bakala, H.1    Wallach, J.2    Hanss, M.3
  • 4
    • 0028964376 scopus 로고
    • DNA binds neutrophil elastase and mucus proteinase inhibitor and impairs their functional activity
    • Belorgey D. and Bieth J. G. (1995) DNA binds neutrophil elastase and mucus proteinase inhibitor and impairs their functional activity. FEBS Lett. 361, 265-268.
    • (1995) FEBS Lett. , vol.361 , pp. 265-268
    • Belorgey, D.1    Bieth, J.G.2
  • 5
    • 0002787184 scopus 로고
    • Human neutrophil elastase
    • CRC Press, Boca Raton, Florida
    • Bieth J. (1989) Human neutrophil elastase. In Elastin and Elastases, Vol. 2, pp. 23-31. CRC Press, Boca Raton, Florida.
    • (1989) Elastin and Elastases , vol.2 , pp. 23-31
    • Bieth, J.1
  • 6
    • 0022625326 scopus 로고
    • Determination of the critical micelle concentration of surfactants using the fluorescent probe N-phenyl-L-naphtylamine
    • Brito R. M. M. and Vaz W. L. C. (1986) Determination of the critical micelle concentration of surfactants using the fluorescent probe N-phenyl-L-naphtylamine. Anal. Blochem. 152, 250-255.
    • (1986) Anal. Blochem. , vol.152 , pp. 250-255
    • Brito, R.M.M.1    Vaz, W.L.C.2
  • 7
    • 0023689698 scopus 로고
    • Deleterious effect of Brij 35 on alkyl-2-pyrones and other hydrophobic inhibition of human sputum and leucokyte elastase
    • Cook L. and Ternai B. (1988a) Deleterious effect of Brij 35 on alkyl-2-pyrones and other hydrophobic inhibition of human sputum and leucokyte elastase. Biochem. Int. 17, 637-646.
    • (1988) Biochem. Int. , vol.17 , pp. 637-646
    • Cook, L.1    Ternai, B.2
  • 8
    • 0023729631 scopus 로고
    • Similar binding sites for unsaturated fatty acids and alkyl-2-pyrone inhibitors of human sputum elastase
    • Cook L. and Ternai B. (1988b) Similar binding sites for unsaturated fatty acids and alkyl-2-pyrone inhibitors of human sputum elastase. Biol. Chem. Hoppe-Seyler 369, 627-637.
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 627-637
    • Cook, L.1    Ternai, B.2
  • 9
    • 0024399417 scopus 로고
    • Pathogenesis of the Pseudomonas lung lesion in cystic fibrosis
    • Fick R. B. (1989) Pathogenesis of the Pseudomonas lung lesion in cystic fibrosis. Chest 96, 158-164.
    • (1989) Chest , vol.96 , pp. 158-164
    • Fick, R.B.1
  • 10
    • 0018822165 scopus 로고
    • Conformational changes induced in α-elastin by cholesterol, taurocholate and unsaturated fatty acids
    • Guantieri V., Tamburro A. M. and Daga Gordini D. (1980) Conformational changes induced in α-elastin by cholesterol, taurocholate and unsaturated fatty acids. Int. J. Biol. Macromol. 2, 68-72.
    • (1980) Int. J. Biol. Macromol. , vol.2 , pp. 68-72
    • Guantieri, V.1    Tamburro, A.M.2    Daga Gordini, D.3
  • 11
    • 0021068588 scopus 로고
    • Interactions of human and bovine elastins with lipids: Their proteolysis by elastase
    • Guantieri V., Tamburro A. M. and Daga Gordini D. (1983) Interactions of human and bovine elastins with lipids: their proteolysis by elastase. Connect. Tissue Res. 12, 79-83.
    • (1983) Connect. Tissue Res. , vol.12 , pp. 79-83
    • Guantieri, V.1    Tamburro, A.M.2    Daga Gordini, D.3
  • 12
    • 0001664087 scopus 로고
    • Hydrodynamic studies of micellar systems of alkyltrimethylammonium bromides and the effect of added 1-alkanols
    • Guveli D. E., Kayes J. B. and Davis S. S. (1979) Hydrodynamic studies of micellar systems of alkyltrimethylammonium bromides and the effect of added 1-alkanols. J. Colloid Interface Sci. 72, 130-139.
    • (1979) J. Colloid Interface Sci. , vol.72 , pp. 130-139
    • Guveli, D.E.1    Kayes, J.B.2    Davis, S.S.3
  • 13
    • 0022368332 scopus 로고
    • Fatty acid peptide derivatives as model compounds to protect elastin against degradation by elastases
    • Hornebeck W., Moczar E., Szecsi J. and Robert L. (1985) Fatty acid peptide derivatives as model compounds to protect elastin against degradation by elastases. Biochem. Pharmacol. 34, 3315-3321.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 3315-3321
    • Hornebeck, W.1    Moczar, E.2    Szecsi, J.3    Robert, L.4
  • 14
    • 0016168705 scopus 로고
    • Regulation of elastase-catalyzed hydrolysis of insoluble elastin by synthetic and naturally occurring hydrophobic ligands
    • Jordan R. E., Hewitt N., Lewis W., Kagan H. M. and Franzblau C. (1974) Regulation of elastase-catalyzed hydrolysis of insoluble elastin by synthetic and naturally occurring hydrophobic ligands. Biochemistry 13, 3497-3503.
    • (1974) Biochemistry , vol.13 , pp. 3497-3503
    • Jordan, R.E.1    Hewitt, N.2    Lewis, W.3    Kagan, H.M.4    Franzblau, C.5
  • 15
    • 0015528772 scopus 로고
    • Proteolysis of elastin-ligand complexes. Stimulation of elastase digestion of insoluble elastin by sodium dodecyl sulfate
    • Kagan H. M., Crombie G. D., Jordan R. E., Lewis W. and Franzblau C. (1972) Proteolysis of elastin-ligand complexes. Stimulation of elastase digestion of insoluble elastin by sodium dodecyl sulfate. Biochemistry 11, 3412-3418.
    • (1972) Biochemistry , vol.11 , pp. 3412-3418
    • Kagan, H.M.1    Crombie, G.D.2    Jordan, R.E.3    Lewis, W.4    Franzblau, C.5
  • 16
    • 0021983279 scopus 로고
    • Enzyme diffusion and action on soluble and insoluble substrates biopolymers
    • Katchalski-Katzir E., Rishpon J., Sahar E., Lamed R. and Henis Y. I. (1985) Enzyme diffusion and action on soluble and insoluble substrates biopolymers. Biopolymers 24, 257-277.
    • (1985) Biopolymers , vol.24 , pp. 257-277
    • Katchalski-Katzir, E.1    Rishpon, J.2    Sahar, E.3    Lamed, R.4    Henis, Y.I.5
  • 17
    • 0020955341 scopus 로고
    • Regulation of elastolysis of insoluble elastin by human leucocyte elastase: Stimulation by lysine-rich ligands, anionic deterrents and ionic strength
    • Lonky S. A. and Wohl H. (1983) Regulation of elastolysis of insoluble elastin by human leucocyte elastase: stimulation by lysine-rich ligands, anionic deterrents and ionic strength. Biochemistry 22, 3714-3720.
    • (1983) Biochemistry , vol.22 , pp. 3714-3720
    • Lonky, S.A.1    Wohl, H.2
  • 18
  • 19
    • 0018747530 scopus 로고
    • Mapping the extended substrate binding site of cathepsin G and human leucocyte elastase. Studies with peptide substrates related to alpha 1-protease inhibitor reactive site
    • Nakajima K., Powers J. C., Ashe B. and Zimmerman M. (1979) Mapping the extended substrate binding site of cathepsin G and human leucocyte elastase. Studies with peptide substrates related to alpha 1-protease inhibitor reactive site. J. biol. Chem. 254, 4027-4032.
    • (1979) J. Biol. Chem. , vol.254 , pp. 4027-4032
    • Nakajima, K.1    Powers, J.C.2    Ashe, B.3    Zimmerman, M.4
  • 20
    • 0021909350 scopus 로고
    • The interaction between alkyl derivatives and elastin
    • Norde W., Bosgoed H. M. M. and De Vries P. (1985) The interaction between alkyl derivatives and elastin. Biophys. Chem. 21, 115-126.
    • (1985) Biophys. Chem. , vol.21 , pp. 115-126
    • Norde, W.1    Bosgoed, H.M.M.2    De Vries, P.3
  • 22
    • 0011285229 scopus 로고
    • Mechanism of elastolysis by pancreatic elastase
    • Robert L. and Samuel P. (1957) Mechanism of elastolysis by pancreatic elastase. Experimentia 13, 167-168.
    • (1957) Experimentia , vol.13 , pp. 167-168
    • Robert, L.1    Samuel, P.2
  • 23
    • 0342549418 scopus 로고
    • Properties of naturally occurring elastase inhibitors
    • CRC Press, Boca Raton, Florida
    • Salvesen G. and Travis J. (1989) Properties of naturally occurring elastase inhibitors. In Elastin and Elastases, Vol. 2, pp. 95-108. CRC Press, Boca Raton, Florida.
    • (1989) Elastin and Elastases , vol.2 , pp. 95-108
    • Salvesen, G.1    Travis, J.2
  • 24
    • 0022659316 scopus 로고
    • The use of Coomassie Brillant Blue for critical micelle concentration determination of deterrents
    • Samsonoff C., Daily J., Almog R. and Berns D. S. (1986) The use of Coomassie Brillant Blue for critical micelle concentration determination of deterrents. J. Colloid Interface Sci. 109, 325-329.
    • (1986) J. Colloid Interface Sci. , vol.109 , pp. 325-329
    • Samsonoff, C.1    Daily, J.2    Almog, R.3    Berns, D.S.4
  • 26
    • 0023848613 scopus 로고
    • Inhibition of human neutrophil elastase by polyguanylic acid and other synthetic RNA homopolymers
    • Simon S., Vered M., Rinehart A. and Janoff A. (1988) Inhibition of human neutrophil elastase by polyguanylic acid and other synthetic RNA homopolymers. Exp. Lung Res. 14, 85-99.
    • (1988) Exp. Lung Res. , vol.14 , pp. 85-99
    • Simon, S.1    Vered, M.2    Rinehart, A.3    Janoff, A.4
  • 27
    • 0025649103 scopus 로고
    • Inhibition of the activity of human leucocyte elastase by lipids, particularly oleic and retinoic acid
    • Sklan D., Rappaport R. and Vered M. (1990) Inhibition of the activity of human leucocyte elastase by lipids, particularly oleic and retinoic acid. Lung 168, 323-332.
    • (1990) Lung , vol.168 , pp. 323-332
    • Sklan, D.1    Rappaport, R.2    Vered, M.3
  • 29
    • 0343041831 scopus 로고
    • Inactivation of glucose oxidase by the cationic detergent, hexadecyltrimethylammonium bromide
    • Tsuge H., Suzuki M., Nakanishi Y., Ohashi K. and Aoki K. (1984) Inactivation of glucose oxidase by the cationic detergent, hexadecyltrimethylammonium bromide. Agric. Biol. Chem. 48, 19-28.
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 19-28
    • Tsuge, H.1    Suzuki, M.2    Nakanishi, Y.3    Ohashi, K.4    Aoki, K.5
  • 30
    • 0026215836 scopus 로고
    • Interaction of neutrophil elastase with hydrophobic polyanionic chelations
    • Tyagi S. C. and Simon S. R. (1991a) Interaction of neutrophil elastase with hydrophobic polyanionic chelations. Biochem. Cell Biol. 69, 624-629.
    • (1991) Biochem. Cell Biol. , vol.69 , pp. 624-629
    • Tyagi, S.C.1    Simon, S.R.2
  • 31
    • 0025745310 scopus 로고
    • Parinaric acids as probes of binding domains in neutrophil elastase
    • Tyagi S. C. and Simon S. R. (1991b) Parinaric acids as probes of binding domains in neutrophil elastase. J. biol. Chem. 266, 15185-15191.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15185-15191
    • Tyagi, S.C.1    Simon, S.R.2
  • 32
    • 0023836384 scopus 로고
    • Inhibition of human neutrophil elastase by bacterial polyanions
    • Vered M., Simon B., Dearing R. and Janoff A. (1988) Inhibition of human neutrophil elastase by bacterial polyanions. Exp. Lung Res. 14, 67-83.
    • (1988) Exp. Lung Res. , vol.14 , pp. 67-83
    • Vered, M.1    Simon, B.2    Dearing, R.3    Janoff, A.4
  • 33
    • 0018269339 scopus 로고
    • Binding constants determined by conductivity titration: Application to ligand-nuclease interaction studies
    • Wallach J. and Hanss M. (1978) Binding constants determined by conductivity titration: application to ligand-nuclease interaction studies. Anal. Biochem. 88, 69-77.
    • (1978) Anal. Biochem. , vol.88 , pp. 69-77
    • Wallach, J.1    Hanss, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.