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Volumn 582, Issue 9, 2008, Pages 1307-1312

Extracellular catalase activity protects cysteine cathepsins from inactivation by hydrogen peroxide

Author keywords

Cathepsin; Cysteine protease; Inflammation; Oxidation; Proteolysis; THP 1 cell

Indexed keywords

CATALASE; CATHEPSIN; CATHEPSIN H; CATHEPSIN K; CATHEPSIN L; HYDROGEN PEROXIDE; PROTEINASE;

EID: 41449113496     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.03.007     Document Type: Article
Times cited : (20)

References (37)
  • 1
    • 0027231742 scopus 로고
    • Nitric oxide-mediated apoptosis in murine peritoneal macrophages
    • Albina J.E., Cui S., Mateo R.B., and Reichner J.S. Nitric oxide-mediated apoptosis in murine peritoneal macrophages. J. Immunol. 150 (1993) 5080-5085
    • (1993) J. Immunol. , vol.150 , pp. 5080-5085
    • Albina, J.E.1    Cui, S.2    Mateo, R.B.3    Reichner, J.S.4
  • 2
    • 2542500561 scopus 로고    scopus 로고
    • Measurement of exhaled hydrogen peroxide from rabbit lungs
    • Weissmann N., et al. Measurement of exhaled hydrogen peroxide from rabbit lungs. Biol. Chem. 385 (2004) 259-264
    • (2004) Biol. Chem. , vol.385 , pp. 259-264
    • Weissmann, N.1
  • 4
    • 0037115158 scopus 로고    scopus 로고
    • Reactive oxygen species and cell signaling: respiratory burst in macrophage signaling
    • Forman H.J., and Torres M. Reactive oxygen species and cell signaling: respiratory burst in macrophage signaling. Am. J. Respir. Crit. Care Med. 166 (2002) S4-S8
    • (2002) Am. J. Respir. Crit. Care Med. , vol.166
    • Forman, H.J.1    Torres, M.2
  • 5
    • 33645780410 scopus 로고    scopus 로고
    • Nitric oxide protects macrophages from hydrogen peroxide-induced apoptosis by inducing the formation of catalase
    • Yoshioka Y., Kitao T., Kishino T., Yamamuro A., and Maeda S. Nitric oxide protects macrophages from hydrogen peroxide-induced apoptosis by inducing the formation of catalase. J. Immunol. 176 (2006) 4675-4681
    • (2006) J. Immunol. , vol.176 , pp. 4675-4681
    • Yoshioka, Y.1    Kitao, T.2    Kishino, T.3    Yamamuro, A.4    Maeda, S.5
  • 6
    • 0025121957 scopus 로고
    • Macrophages and polymorphonuclear neutrophils in lung defense and injury
    • Sibille Y., and Reynolds H.Y. Macrophages and polymorphonuclear neutrophils in lung defense and injury. Am. Rev. Respir. Dis. 141 (1990) 471-501
    • (1990) Am. Rev. Respir. Dis. , vol.141 , pp. 471-501
    • Sibille, Y.1    Reynolds, H.Y.2
  • 7
    • 28244456240 scopus 로고    scopus 로고
    • Proteinases and oxidants as targets in the treatment of chronic obstructive pulmonary disease
    • Owen C.A. Proteinases and oxidants as targets in the treatment of chronic obstructive pulmonary disease. Proc. Am. Thorac. Soc. 2 (2005) 373-385
    • (2005) Proc. Am. Thorac. Soc. , vol.2 , pp. 373-385
    • Owen, C.A.1
  • 8
    • 38649111363 scopus 로고    scopus 로고
    • Cysteine cathepsins: cellular roadmap to different functions
    • Brix K., Dunkhorst A., Mayer K., and Jordans S. Cysteine cathepsins: cellular roadmap to different functions. Biochimie 90 (2008) 194-207
    • (2008) Biochimie , vol.90 , pp. 194-207
    • Brix, K.1    Dunkhorst, A.2    Mayer, K.3    Jordans, S.4
  • 9
    • 18944365919 scopus 로고    scopus 로고
    • The role of cathepsins in osteoporosis and arthritis: rationale for the design of new therapeutics
    • Yasuda Y., Kaleta J., and Bromme D. The role of cathepsins in osteoporosis and arthritis: rationale for the design of new therapeutics. Adv. Drug Deliv. Rev. 57 (2005) 973-993
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , pp. 973-993
    • Yasuda, Y.1    Kaleta, J.2    Bromme, D.3
  • 10
    • 33748308883 scopus 로고    scopus 로고
    • Targeting proteases: successes, failures and future prospects
    • Turk B. Targeting proteases: successes, failures and future prospects. Nat. Rev. Drug. Discov. 5 (2006) 785-799
    • (2006) Nat. Rev. Drug. Discov. , vol.5 , pp. 785-799
    • Turk, B.1
  • 11
    • 0036882393 scopus 로고    scopus 로고
    • Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design
    • Lecaille F., Kaleta J., and Bromme D. Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design. Chem. Rev. 102 (2002) 4459-4488
    • (2002) Chem. Rev. , vol.102 , pp. 4459-4488
    • Lecaille, F.1    Kaleta, J.2    Bromme, D.3
  • 12
    • 33846164404 scopus 로고    scopus 로고
    • Emerging roles of cysteine cathepsins in disease and their potential as drug targets
    • Vasiljeva O., Reinheckel T., Peters C., Turk D., Turk V., and Turk B. Emerging roles of cysteine cathepsins in disease and their potential as drug targets. Curr. Pharm. Des. 13 (2007) 385-401
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 385-401
    • Vasiljeva, O.1    Reinheckel, T.2    Peters, C.3    Turk, D.4    Turk, V.5    Turk, B.6
  • 14
    • 7044230857 scopus 로고    scopus 로고
    • Cys-His proteases are among the wired proteins of the cell
    • Lockwood T.D. Cys-His proteases are among the wired proteins of the cell. Arch. Biochem. Biophys. 432 (2004) 12-24
    • (2004) Arch. Biochem. Biophys. , vol.432 , pp. 12-24
    • Lockwood, T.D.1
  • 16
    • 41449118936 scopus 로고    scopus 로고
    • Godat, E., Hervé-Grépinet, V., Veillard, F., Lecaille, F., Belghazi, M., Brömme, D. and Lalmanach, G. (in press). Regulation of cathepsin K activity by hydrogen peroxide. Biol. Chem.
    • Godat, E., Hervé-Grépinet, V., Veillard, F., Lecaille, F., Belghazi, M., Brömme, D. and Lalmanach, G. (in press). Regulation of cathepsin K activity by hydrogen peroxide. Biol. Chem.
  • 17
    • 0035816440 scopus 로고    scopus 로고
    • Caspases are reversibly inactivated by hydrogen peroxide
    • Borutaite V., and Brown G.C. Caspases are reversibly inactivated by hydrogen peroxide. FEBS Lett. 500 (2001) 114-118
    • (2001) FEBS Lett. , vol.500 , pp. 114-118
    • Borutaite, V.1    Brown, G.C.2
  • 18
    • 15244350287 scopus 로고    scopus 로고
    • Nitric oxide-related species-induced protein oxidation: reversible, irreversible, and protective effects on enzyme function of papain
    • Vaananen A.J., Kankuri E., and Rauhala P. Nitric oxide-related species-induced protein oxidation: reversible, irreversible, and protective effects on enzyme function of papain. Free Radic. Biol. Med. 38 (2005) 1102-1111
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1102-1111
    • Vaananen, A.J.1    Kankuri, E.2    Rauhala, P.3
  • 19
    • 41449104569 scopus 로고    scopus 로고
    • Veillard, F., Lecaille, F. and Lalmanach, G. (in press) Lung cysteine cathepsins: intruders or unorthodox contributors to the kallikrein-kinin system? Int. J. Biochem. Cell Biol.
    • Veillard, F., Lecaille, F. and Lalmanach, G. (in press) Lung cysteine cathepsins: intruders or unorthodox contributors to the kallikrein-kinin system? Int. J. Biochem. Cell Biol.
  • 21
    • 33745058367 scopus 로고    scopus 로고
    • Cathepsin B is a differentiation-resistant target for nitroxyl (HNO) in THP-1 monocyte/macrophages
    • Vaananen A.J., Salmenpera P., Hukkanen M., Rauhala P., and Kankuri E. Cathepsin B is a differentiation-resistant target for nitroxyl (HNO) in THP-1 monocyte/macrophages. Free Radic. Biol. Med. 41 (2006) 120-131
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 120-131
    • Vaananen, A.J.1    Salmenpera, P.2    Hukkanen, M.3    Rauhala, P.4    Kankuri, E.5
  • 22
    • 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 Bromme D. Cathepsin v, a novel and potent elastolytic activity expressed in activated macrophages. J. Biol. Chem. 279 (2004) 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    Bromme, D.6
  • 24
    • 0019948262 scopus 로고
    • l-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L
    • Barrett A.J., Kembhavi A.A., Brown M.A., Kirschke H., Knight C.G., Tamai M., and Hanada K. l-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem. J. 201 (1982) 189-198
    • (1982) Biochem. J. , vol.201 , pp. 189-198
    • Barrett, A.J.1    Kembhavi, A.A.2    Brown, M.A.3    Kirschke, H.4    Knight, C.G.5    Tamai, M.6    Hanada, K.7
  • 26
    • 4644291564 scopus 로고    scopus 로고
    • Effect of macrophage differentiation and exposure to mildly oxidized LDL on the proteolytic repertoire of THP-1 monocytes
    • Whatling C., Bjork H., Gredmark S., Hamsten A., and Eriksson P. Effect of macrophage differentiation and exposure to mildly oxidized LDL on the proteolytic repertoire of THP-1 monocytes. J. Lipid Res. 45 (2004) 1768-1776
    • (2004) J. Lipid Res. , vol.45 , pp. 1768-1776
    • Whatling, C.1    Bjork, H.2    Gredmark, S.3    Hamsten, A.4    Eriksson, P.5
  • 27
    • 0345363292 scopus 로고    scopus 로고
    • Differentiating agents regulate cathepsin B gene expression in HL-60 cells
    • Berquin I.M., Yan S., Katiyar K., Sloane B.F., and Troen B.R. Differentiating agents regulate cathepsin B gene expression in HL-60 cells. J. Leukoc. Biol. 66 (1999) 609-616
    • (1999) J. Leukoc. Biol. , vol.66 , pp. 609-616
    • Berquin, I.M.1    Yan, S.2    Katiyar, K.3    Sloane, B.F.4    Troen, B.R.5
  • 28
    • 8544267975 scopus 로고    scopus 로고
    • Essential role of p38 mitogen-activated protein kinase in cathepsin K gene expression during osteoclastogenesis through association of NFATcl and PU.l
    • Matsumoto M., Kogawa M., Wada S., Takayanagi H., Tsujimoto M., Katayama S., Hisatake K., and Nogi Y. Essential role of p38 mitogen-activated protein kinase in cathepsin K gene expression during osteoclastogenesis through association of NFATcl and PU.l. J. Biol. Chem. 279 (2004) 45969-45979
    • (2004) J. Biol. Chem. , vol.279 , pp. 45969-45979
    • Matsumoto, M.1    Kogawa, M.2    Wada, S.3    Takayanagi, H.4    Tsujimoto, M.5    Katayama, S.6    Hisatake, K.7    Nogi, Y.8
  • 29
    • 38849159247 scopus 로고    scopus 로고
    • Biochemical properties and regulation of cathepsin K activity
    • Lecaille F., Brömme D., and Lalmanach G. Biochemical properties and regulation of cathepsin K activity. Biochimie 90 (2008) 208-226
    • (2008) Biochimie , vol.90 , pp. 208-226
    • Lecaille, F.1    Brömme, D.2    Lalmanach, G.3
  • 30
    • 0029007093 scopus 로고
    • Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages
    • Reddy V.Y., Zhang Q.Y., and Weiss S.J. Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages. Proc. Natl. Acad. Sci. USA 92 (1995) 3849-3853
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3849-3853
    • Reddy, V.Y.1    Zhang, Q.Y.2    Weiss, S.J.3
  • 31
    • 0032145836 scopus 로고    scopus 로고
    • Expression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells
    • Sukhova G.K., Shi G.P., Simon D.I., Chapman H.A., and Libby P. Expression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells. J. Clin. Invest. 102 (1998) 576-583
    • (1998) J. Clin. Invest. , vol.102 , pp. 576-583
    • Sukhova, G.K.1    Shi, G.P.2    Simon, D.I.3    Chapman, H.A.4    Libby, P.5
  • 33
    • 0033802292 scopus 로고    scopus 로고
    • Regulation of elastinolytic cysteine proteinase activity in normal and cathepsin K-deficient human macrophages
    • Punturieri A., Filippov S., Allen E., Caras I., Murray R., Reddy V., and Weiss S.J. Regulation of elastinolytic cysteine proteinase activity in normal and cathepsin K-deficient human macrophages. J. Exp. Med. 192 (2000) 789-799
    • (2000) J. Exp. Med. , vol.192 , pp. 789-799
    • Punturieri, A.1    Filippov, S.2    Allen, E.3    Caras, I.4    Murray, R.5    Reddy, V.6    Weiss, S.J.7
  • 34
    • 0026326943 scopus 로고
    • Hydrogen peroxide-induced renal injury. A protective role for pyruvate in vitro and in vivo
    • Salahudeen A.K., Clark E.C., and Nath K.A. Hydrogen peroxide-induced renal injury. A protective role for pyruvate in vitro and in vivo. J. Clin. Invest. 88 (1991) 1886-1893
    • (1991) J. Clin. Invest. , vol.88 , pp. 1886-1893
    • Salahudeen, A.K.1    Clark, E.C.2    Nath, K.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.