메뉴 건너뛰기




Volumn 288, Issue 48, 2013, Pages 34871-34881

Elastin degradation by cathepsin v requires two exosites

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; CATHEPSIN L; EXTRACELLULAR MATRIX DEGRADATION; INSOLUBLE ELASTIN; MECHANISM OF ACTION; PROTEOLYTIC ACTIVITIES; STRUCTURAL DOMAINS; SURFACE LOOPS;

EID: 84889060938     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.510008     Document Type: Article
Times cited : (39)

References (30)
  • 1
    • 0033006918 scopus 로고    scopus 로고
    • Elastin: Molecular description and function
    • Debelle, L., and Tamburro, A. M. (1999) Elastin: molecular description and function. Int. J. Biochem. Cell Biol. 31, 261-272
    • (1999) Int. J. Biochem. Cell Biol , vol.31 , pp. 261-272
    • Debelle, L.1    Tamburro, A.M.2
  • 2
    • 33747084768 scopus 로고    scopus 로고
    • Localizing α-helices in human tropoelastin: Assembly of the elastin "puzzle"
    • Tamburro, A. M., Pepe, A., and Bochicchio, B. (2006) Localizing α-helices in human tropoelastin: assembly of the elastin "puzzle". Biochemistry 45, 9518-9530
    • (2006) Biochemistry , vol.45 , pp. 9518-9530
    • Tamburro, A.M.1    Pepe, A.2    Bochicchio, B.3
  • 3
    • 0025780051 scopus 로고
    • Marked longevity of human lung parenchymal elastic fibers deduced from prevalence of D-aspartate and nuclear weapons-related radiocarbon
    • Shapiro, S. D., Endicott, S. K., Province, M. A., Pierce, J. A., and Campbell, E. J. (1991) Marked longevity of human lung parenchymal elastic fibers deduced from prevalence of D-aspartate and nuclear weapons-related radiocarbon. J. Clin. Invest. 87, 1828-1834
    • (1991) J. Clin. Invest , vol.87 , pp. 1828-1834
    • Shapiro, S.D.1    Endicott, S.K.2    Province, M.A.3    Pierce, J.A.4    Campbell, E.J.5
  • 4
    • 39949085233 scopus 로고    scopus 로고
    • Rapid increase in human life expectancy: Will it soon be limited by the aging of elastin?
    • Robert, L., Robert, A. M., and Fülöp, T. (2008) Rapid increase in human life expectancy: will it soon be limited by the aging of elastin? Biogerontology 9, 119-133
    • (2008) Biogerontology , vol.9 , pp. 119-133
    • Robert, L.1    Robert, A.M.2    Fülöp, T.3
  • 6
    • 34247540771 scopus 로고    scopus 로고
    • William J. Cunliffe Scientific Awards. Characteristics and pathomechanisms of endogenously aged skin
    • Makrantonaki, E., and Zouboulis, C. C. (2007) William J. Cunliffe Scientific Awards. Characteristics and pathomechanisms of endogenously aged skin. Dermatology 214, 352-360
    • (2007) Dermatology , vol.214 , pp. 352-360
    • Makrantonaki, E.1    Zouboulis, C.C.2
  • 7
    • 0031728107 scopus 로고    scopus 로고
    • Elastin-elastase-atherosclerosis revisited
    • Robert, L., Robert, A. M., and Jacotot, B. (1998) Elastin-elastase- atherosclerosis revisited. Atherosclerosis 140, 281-295
    • (1998) Atherosclerosis , vol.140 , pp. 281-295
    • Robert, L.1    Robert, A.M.2    Jacotot, B.3
  • 9
    • 0031671855 scopus 로고    scopus 로고
    • Matrix metalloproteinase degradation of extracellular matrix: Biological consequences
    • Shapiro, S. D. (1998) Matrix metalloproteinase degradation of extracellular matrix: biological consequences. Curr. Opin. Cell Biol. 10, 602-608
    • (1998) Curr. Opin. Cell Biol , vol.10 , pp. 602-608
    • Shapiro, S.D.1
  • 10
    • 0037322932 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases (cathepsins): Promising drug targets
    • Turk, D., and Guncar, G. (2003) Lysosomal cysteine proteases (cathepsins): promising drug targets. Acta Crystallogr. D Biol. Crystallogr. 59, 203-213
    • (2003) Acta Crystallogr. D Biol. Crystallogr , vol.59 , pp. 203-213
    • Turk, D.1    Guncar, G.2
  • 11
    • 0025168332 scopus 로고
    • Elafin: An elastase-specific inhibitor of human skin. Purification, characterization, and complete amino acid sequence
    • Wiedow, O., Schröder, J. M., Gregory, H., Young, J. A., and Christophers, E. (1990) Elafin: an elastase-specific inhibitor of human skin. Purification, characterization, and complete amino acid sequence. J. Biol. Chem. 265, 14791-14795
    • (1990) J. Biol. Chem , vol.265 , pp. 14791-14795
    • Wiedow, O.1    Schröder, J.M.2    Gregory, H.3    Young, J.A.4    Christophers, E.5
  • 12
    • 79955047967 scopus 로고    scopus 로고
    • The cell-elastin-elastase(s) interacting triade directs elastolysis
    • Hornebeck, W., and Emonard, H. (2011) The cell-elastin-elastase(s) interacting triade directs elastolysis. Front. Biosci. 16, 707-722
    • (2011) Front. Biosci , vol.16 , pp. 707-722
    • Hornebeck, W.1    Emonard, H.2
  • 13
    • 0031847419 scopus 로고    scopus 로고
    • Expression and localization of matrix metalloproteinase-12 in the aorta of cholesterol-fed rabbits: Relationship to lesion development
    • Matsumoto, S., Kobayashi, T., Katoh, M., Saito, S., Ikeda, Y., Kobori, M., Masuho, Y., and Watanabe, T. (1998) Expression and localization of matrix metalloproteinase-12 in the aorta of cholesterol-fed rabbits: relationship to lesion development. Am. J. Pathol. 153, 109-119
    • (1998) Am. J. Pathol , vol.153 , pp. 109-119
    • Matsumoto, S.1    Kobayashi, T.2    Katoh, M.3    Saito, S.4    Ikeda, Y.5    Kobori, M.6    Masuho, Y.7    Watanabe, T.8
  • 14
    • 4344670363 scopus 로고    scopus 로고
    • Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages
    • Yasuda, Y., Li, Z., Greenbaum, D., Bogyo, M., Weber, E., and Brömme, D. (2004) Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages. J. Biol. Chem. 279, 36761-36770
    • (2004) J. Biol. Chem , vol.279 , pp. 36761-36770
    • Yasuda, Y.1    Li, Z.2    Greenbaum, D.3    Bogyo, M.4    Weber, E.5    Brömme, D.6
  • 15
    • 0038687865 scopus 로고    scopus 로고
    • Human cathepsin v functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization
    • Brömme, D., Li, Z., Barnes, M., and Mehler, E. (1999) Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization. Biochemistry 38, 2377-2385
    • (1999) Biochemistry , vol.38 , pp. 2377-2385
    • Brömme, D.1    Li, Z.2    Barnes, M.3    Mehler, E.4
  • 17
    • 33744961634 scopus 로고    scopus 로고
    • Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities
    • Choe, Y., Leonetti, F., Greenbaum, D. C., Lecaille, F., Bogyo, M., Brömme, D., Ellman, J. A., and Craik, C. S. (2006) Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities. J. Biol. Chem. 281, 12824-12832
    • (2006) J. Biol. Chem , vol.281 , pp. 12824-12832
    • Choe, Y.1    Leonetti, F.2    Greenbaum, D.C.3    Lecaille, F.4    Bogyo, M.5    Brömme, D.6    Ellman, J.A.7    Craik, C.S.8
  • 18
    • 34247213889 scopus 로고    scopus 로고
    • Interaction between human cathepsins K, L, and S and elastins: Mechanism of elastinolysis and inhibition by macromolecular inhibitors
    • Novinec, M., Grass, R. N., Stark, W. J., Turk, V., Baici, A., and Lenarcic, B. (2007) Interaction between human cathepsins K, L, and S and elastins: mechanism of elastinolysis and inhibition by macromolecular inhibitors. J. Biol. Chem. 282, 7893-7902
    • (2007) J. Biol. Chem , vol.282 , pp. 7893-7902
    • Novinec, M.1    Grass, R.N.2    Stark, W.J.3    Turk, V.4    Baici, A.5    Lenarcic, B.6
  • 19
    • 80155126194 scopus 로고    scopus 로고
    • Remote exosites of the catalytic domain of matrix metalloproteinase-12 enhance elastin degradation
    • Fulcher, Y. G., and Van Doren, S. R. (2011) Remote exosites of the catalytic domain of matrix metalloproteinase-12 enhance elastin degradation. Biochemistry 50, 9488-9499
    • (2011) Biochemistry , vol.50 , pp. 9488-9499
    • Fulcher, Y.G.1    Van Doren, S.R.2
  • 20
    • 77957285621 scopus 로고    scopus 로고
    • NMRand bioinformatics discovery of exosites that tune metalloelastase specificity for solubilized elastin and collagen triple helices
    • Palmier, M. O., Fulcher, Y. G., Bhaskaran, R., Duong, V. Q., Fields, G. B., and Van Doren, S. R. (2010)NMRand bioinformatics discovery of exosites that tune metalloelastase specificity for solubilized elastin and collagen triple helices. J. Biol. Chem. 285, 30918-30930
    • (2010) J. Biol. Chem , vol.285 , pp. 30918-30930
    • Palmier, M.O.1    Fulcher, Y.G.2    Bhaskaran, R.3    Duong, V.Q.4    Fields, G.B.5    Van Doren, S.R.6
  • 21
    • 0029310512 scopus 로고
    • Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution
    • Brömme, D., and Okamoto, K. (1995) Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution. Biol. Chem. Hoppe-Seyler 376, 379-384
    • (1995) Biol. Chem. Hoppe-Seyler , vol.376 , pp. 379-384
    • Brömme, D.1    Okamoto, K.2
  • 22
    • 0036882393 scopus 로고    scopus 로고
    • Human and parasitic papainlike cysteine proteases: Their role in physiology and pathology and recent developments in inhibitor design
    • Lecaille, F., Kaleta, J., and Brömme, D. (2002) Human and parasitic papainlike cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design. Chem. Rev. 102, 4459-4488
    • (2002) Chem. Rev , vol.102 , pp. 4459-4488
    • Lecaille, F.1    Kaleta, J.2    Brömme, D.3
  • 25
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132
    • (1982) J. Mol. Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 27
    • 84856831064 scopus 로고    scopus 로고
    • Molecular orientation of tropoelastin is determined by surface hydrophobicity
    • Le Brun, A. P., Chow, J., Bax, D. V., Nelson, A., Weiss, A. S., and James, M. (2012) Molecular orientation of tropoelastin is determined by surface hydrophobicity. Biomacromolecules 13, 379-386
    • (2012) Biomacromolecules , vol.13 , pp. 379-386
    • Le Brun, A.P.1    Chow, J.2    Bax, D.V.3    Nelson, A.4    Weiss, A.S.5    James, M.6
  • 30
    • 33847746237 scopus 로고    scopus 로고
    • Generation of endostatin by matrix metalloproteinase and cathepsin from human limbocorneal epithelial cells cultivated on amniotic membrane
    • Ma, D. H., Yao, J. Y., Kuo, M. T., See, L. C., Lin, K. Y., Chen, S. C., Chen, J. K., Chao, A. S., Wang, S. F., and Lin, K. K. (2007) Generation of endostatin by matrix metalloproteinase and cathepsin from human limbocorneal epithelial cells cultivated on amniotic membrane. Invest. Ophthalmol. Vis. Sci. 48, 644-651
    • (2007) Invest. Ophthalmol. Vis. Sci , vol.48 , pp. 644-651
    • Ma, D.H.1    Yao, J.Y.2    Kuo, M.T.3    See, L.C.4    Lin, K.Y.5    Chen, S.C.6    Chen, J.K.7    Chao, A.S.8    Wang, S.F.9    Lin, K.K.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.