메뉴 건너뛰기




Volumn 50, Issue 1-2, 2012, Pages 60-65

Cathepsin D is released after severe tissue trauma in vivo and is capable of generating C5a in vitro

Author keywords

Apoptosis; C5a; Cathepsin d; Complement; Polytrauma

Indexed keywords

CATHEPSIN D; COMPLEMENT COMPONENT C5A; PEPSTATIN;

EID: 84857041124     PISSN: 01615890     EISSN: 18729142     Source Type: Journal    
DOI: 10.1016/j.molimm.2011.12.005     Document Type: Article
Times cited : (32)

References (46)
  • 2
    • 77952329423 scopus 로고    scopus 로고
    • Early expression changes of complement regulatory proteins and C5A receptor (CD88) on leukocytes after multiple injury in humans
    • Amara U., Kalbitz M., Perl M., Flierl M.A., Rittirsch D., Weiss M., Schneider M., Gebhard F., Huber-Lang M. Early expression changes of complement regulatory proteins and C5A receptor (CD88) on leukocytes after multiple injury in humans. Shock 2010, 33:568-575.
    • (2010) Shock , vol.33 , pp. 568-575
    • Amara, U.1    Kalbitz, M.2    Perl, M.3    Flierl, M.A.4    Rittirsch, D.5    Weiss, M.6    Schneider, M.7    Gebhard, F.8    Huber-Lang, M.9
  • 4
    • 0342614999 scopus 로고    scopus 로고
    • Tissue and intracellular pH in normal periarticular soft tissue and during different phases of antigen induced arthritis in the rat
    • Andersson S.E., Lexmuller K., Johansson A., Ekstrom G.M. Tissue and intracellular pH in normal periarticular soft tissue and during different phases of antigen induced arthritis in the rat. J. Rheumatol. 1999, 26:2018-2024.
    • (1999) J. Rheumatol. , vol.26 , pp. 2018-2024
    • Andersson, S.E.1    Lexmuller, K.2    Johansson, A.3    Ekstrom, G.M.4
  • 8
    • 0043234207 scopus 로고    scopus 로고
    • Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis
    • Bidere N., Lorenzo H.K., Carmona S., Laforge M., Harper F., Dumont C., Senik A. Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis. J. Biol. Chem. 2003, 278:31401-31411.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31401-31411
    • Bidere, N.1    Lorenzo, H.K.2    Carmona, S.3    Laforge, M.4    Harper, F.5    Dumont, C.6    Senik, A.7
  • 9
    • 0028155959 scopus 로고
    • Site-specific mutagenesis of residues in the human C5a anaphylatoxin which are involved in possible interaction with the C5a receptor
    • Bubeck P., Grotzinger J., Winkler M., Kohl J., Wollmer A., Klos A., Bautsch W. Site-specific mutagenesis of residues in the human C5a anaphylatoxin which are involved in possible interaction with the C5a receptor. Eur. J. Biochem. 1994, 219:897-904.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 897-904
    • Bubeck, P.1    Grotzinger, J.2    Winkler, M.3    Kohl, J.4    Wollmer, A.5    Klos, A.6    Bautsch, W.7
  • 11
    • 33645079378 scopus 로고    scopus 로고
    • Complement regulator loss on apoptotic neuronal cells causes increased complement activation and promotes both phagocytosis and cell lysis
    • Cole D.S., Hughes T.R., Gasque P., Morgan B.P. Complement regulator loss on apoptotic neuronal cells causes increased complement activation and promotes both phagocytosis and cell lysis. Mol. Immunol. 2006, 43:1953-1964.
    • (2006) Mol. Immunol. , vol.43 , pp. 1953-1964
    • Cole, D.S.1    Hughes, T.R.2    Gasque, P.3    Morgan, B.P.4
  • 12
    • 41149098534 scopus 로고    scopus 로고
    • Caspase-8 is activated by cathepsin D initiating neutrophil apoptosis during the resolution of inflammation
    • Conus S., Perozzo R., Reinheckel T., Peters C., Scapozza L., Yousefi S., Simon H.U. Caspase-8 is activated by cathepsin D initiating neutrophil apoptosis during the resolution of inflammation. J. Exp. Med. 2008, 205:685-698.
    • (2008) J. Exp. Med. , vol.205 , pp. 685-698
    • Conus, S.1    Perozzo, R.2    Reinheckel, T.3    Peters, C.4    Scapozza, L.5    Yousefi, S.6    Simon, H.U.7
  • 13
    • 0016723595 scopus 로고
    • Direct evidence of importance of lysosomes in degradation of intracellular proteins
    • Dean R.T. Direct evidence of importance of lysosomes in degradation of intracellular proteins. Nature 1975, 257:414-416.
    • (1975) Nature , vol.257 , pp. 414-416
    • Dean, R.T.1
  • 14
    • 0029782494 scopus 로고    scopus 로고
    • Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNF-alpha
    • Deiss L.P., Galinka H., Berissi H., Cohen O., Kimchi A. Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNF-alpha. EMBO J. 1996, 15:3861-3870.
    • (1996) EMBO J. , vol.15 , pp. 3861-3870
    • Deiss, L.P.1    Galinka, H.2    Berissi, H.3    Cohen, O.4    Kimchi, A.5
  • 18
    • 0026022865 scopus 로고
    • Complete cDNA sequence of human complement pro-C5. Evidence of truncated transcripts derived from a single copy gene
    • Haviland D.L., Haviland J.C., Fleischer D.T., Hunt A., Wetsel R.A. Complete cDNA sequence of human complement pro-C5. Evidence of truncated transcripts derived from a single copy gene. J. Immunol. 1991, 146:362-368.
    • (1991) J. Immunol. , vol.146 , pp. 362-368
    • Haviland, D.L.1    Haviland, J.C.2    Fleischer, D.T.3    Hunt, A.4    Wetsel, R.A.5
  • 20
    • 0031573151 scopus 로고    scopus 로고
    • Natural processing sites for human cathepsin E and cathepsin D in tetanus toxin: implications for T cell epitope generation
    • Hewitt E.W., Treumann A., Morrice N., Tatnell P.J., Kay J., Watts C. Natural processing sites for human cathepsin E and cathepsin D in tetanus toxin: implications for T cell epitope generation. J. Immunol. 1997, 159:4693-4699.
    • (1997) J. Immunol. , vol.159 , pp. 4693-4699
    • Hewitt, E.W.1    Treumann, A.2    Morrice, N.3    Tatnell, P.J.4    Kay, J.5    Watts, C.6
  • 21
    • 0037426726 scopus 로고    scopus 로고
    • The pathophysiology and treatment of sepsis
    • Hotchkiss R.S., Karl I.E. The pathophysiology and treatment of sepsis. N. Engl. J. Med. 2003, 348:138-150.
    • (2003) N. Engl. J. Med. , vol.348 , pp. 138-150
    • Hotchkiss, R.S.1    Karl, I.E.2
  • 27
    • 19544365744 scopus 로고    scopus 로고
    • Pathophysiology of polytrauma
    • Keel M., Trentz O. Pathophysiology of polytrauma. Injury 2005, 36:691-709.
    • (2005) Injury , vol.36 , pp. 691-709
    • Keel, M.1    Trentz, O.2
  • 28
    • 41149118513 scopus 로고    scopus 로고
    • How dying cells alert the immune system to danger
    • Kono H., Rock K.L. How dying cells alert the immune system to danger. Nat. Rev. Immunol. 2008, 8:279-289.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 279-289
    • Kono, H.1    Rock, K.L.2
  • 30
    • 67649620040 scopus 로고    scopus 로고
    • Release of endo-lysosomal cathepsins B, D, and L from IEC6 cells in a cell culture model mimicking intestinal manipulation
    • Mayer K., Vreemann A., Qu H., Brix K. Release of endo-lysosomal cathepsins B, D, and L from IEC6 cells in a cell culture model mimicking intestinal manipulation. Biol. Chem. 2009, 390:471-480.
    • (2009) Biol. Chem. , vol.390 , pp. 471-480
    • Mayer, K.1    Vreemann, A.2    Qu, H.3    Brix, K.4
  • 31
    • 0035174975 scopus 로고    scopus 로고
    • Defective neutrophil degranulation induced by interleukin-8 and complement 5a and down-regulation of associated receptors in children vertically infected with human immunodeficiency virus type 1
    • Meddows-Taylor S., Kuhn L., Meyers T.M., Sherman G., Tiemessen C.T. Defective neutrophil degranulation induced by interleukin-8 and complement 5a and down-regulation of associated receptors in children vertically infected with human immunodeficiency virus type 1. Clin. Diagn. Lab Immunol. 2001, 8:21-30.
    • (2001) Clin. Diagn. Lab Immunol. , vol.8 , pp. 21-30
    • Meddows-Taylor, S.1    Kuhn, L.2    Meyers, T.M.3    Sherman, G.4    Tiemessen, C.T.5
  • 33
    • 40549111917 scopus 로고    scopus 로고
    • Modeling molecular mechanisms of binding of the anaphylatoxin C5a to the C5a receptor
    • Nikiforovich G.V., Marshall G.R., Baranski T.J. Modeling molecular mechanisms of binding of the anaphylatoxin C5a to the C5a receptor. Biochemistry 2008, 47:3117-3130.
    • (2008) Biochemistry , vol.47 , pp. 3117-3130
    • Nikiforovich, G.V.1    Marshall, G.R.2    Baranski, T.J.3
  • 34
    • 78651326476 scopus 로고    scopus 로고
    • Increased serum soluble Fas after major trauma is associated with delayed neutrophil apoptosis and development of sepsis
    • Paunel-Gorgulu A., Flohe S., Scholz M., Windolf J., Logters T. Increased serum soluble Fas after major trauma is associated with delayed neutrophil apoptosis and development of sepsis. Crit. Care 2011, 15:R20.
    • (2011) Crit. Care , vol.15
    • Paunel-Gorgulu, A.1    Flohe, S.2    Scholz, M.3    Windolf, J.4    Logters, T.5
  • 35
  • 36
    • 0015978285 scopus 로고
    • Cathepsin D in cartilage: the immunohistochemical demonstration of extracellular enzyme in normal and pathological conditions
    • Poole A.R., Hembry R.M., Dingle J.T. Cathepsin D in cartilage: the immunohistochemical demonstration of extracellular enzyme in normal and pathological conditions. J. Cell Sci. 1974, 14:139-161.
    • (1974) J. Cell Sci. , vol.14 , pp. 139-161
    • Poole, A.R.1    Hembry, R.M.2    Dingle, J.T.3
  • 37
    • 0017020846 scopus 로고
    • Secretion and localization of cathepsin D in synovial tissues removed from rheumatoid and traumatized joints. An immunohistochemical study
    • Poole A.R., Hembry R.M., Dingle J.T., Pinder I., Ring E.F., Cosh J. Secretion and localization of cathepsin D in synovial tissues removed from rheumatoid and traumatized joints. An immunohistochemical study. Arthritis Rheum. 1976, 19:1295-1307.
    • (1976) Arthritis Rheum. , vol.19 , pp. 1295-1307
    • Poole, A.R.1    Hembry, R.M.2    Dingle, J.T.3    Pinder, I.4    Ring, E.F.5    Cosh, J.6
  • 38
    • 0025690427 scopus 로고
    • Cathepsin D: a protease involved in breast cancer metastasis
    • Rochefort H., Capony F., Garcia M. Cathepsin D: a protease involved in breast cancer metastasis. Cancer Metastasis Rev. 1990, 9:321-331.
    • (1990) Cancer Metastasis Rev. , vol.9 , pp. 321-331
    • Rochefort, H.1    Capony, F.2    Garcia, M.3
  • 39
    • 0023882543 scopus 로고
    • Microelectrode studies on the acid microenvironment beneath adherent macrophages and osteoclasts
    • Silver I.A., Murrills R.J., Etherington D.J. Microelectrode studies on the acid microenvironment beneath adherent macrophages and osteoclasts. Exp. Cell Res. 1988, 175:266-276.
    • (1988) Exp. Cell Res. , vol.175 , pp. 266-276
    • Silver, I.A.1    Murrills, R.J.2    Etherington, D.J.3
  • 40
    • 0024549012 scopus 로고
    • Protective effects of a specific platelet activating factor (PAF) antagonist. WEB 2086, in traumatic shock
    • Stahl G.L., Bitterman H., Lefer A.M. Protective effects of a specific platelet activating factor (PAF) antagonist. WEB 2086, in traumatic shock. Thromb. Res. 1989, 53:327-338.
    • (1989) Thromb. Res. , vol.53 , pp. 327-338
    • Stahl, G.L.1    Bitterman, H.2    Lefer, A.M.3
  • 42
    • 1142310879 scopus 로고    scopus 로고
    • The dark side of C5a in sepsis
    • Ward P.A. The dark side of C5a in sepsis. Nat. Rev. Immunol. 2004, 4:133-142.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 133-142
    • Ward, P.A.1
  • 43
    • 77956057326 scopus 로고    scopus 로고
    • The harmful role of c5a on innate immunity in sepsis
    • Ward P.A. The harmful role of c5a on innate immunity in sepsis. J. Innate Immun. 2010, 2:439-445.
    • (2010) J. Innate Immun. , vol.2 , pp. 439-445
    • Ward, P.A.1
  • 44
    • 0026725842 scopus 로고
    • Activation of complement components C3 and C5 by a cysteine proteinase (gingipain-1) from Porphyromonas (Bacteroides) gingivalis
    • Wingrove J.A., DiScipio R.G., Chen Z., Potempa J., Travis J., Hugli T.E. Activation of complement components C3 and C5 by a cysteine proteinase (gingipain-1) from Porphyromonas (Bacteroides) gingivalis. J. Biol. Chem. 1992, 267:18902-18907.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18902-18907
    • Wingrove, J.A.1    DiScipio, R.G.2    Chen, Z.3    Potempa, J.4    Travis, J.5    Hugli, T.E.6
  • 45
    • 0015351253 scopus 로고
    • The mobilization and extracellular release of granular enzymes from human leukocytes during phagocytosis
    • Wright D.G., Malawista S.E. The mobilization and extracellular release of granular enzymes from human leukocytes during phagocytosis. J. Cell Biol. 1972, 53:788-797.
    • (1972) J. Cell Biol. , vol.53 , pp. 788-797
    • Wright, D.G.1    Malawista, S.E.2
  • 46
    • 0020578295 scopus 로고
    • Molecular forms of beta-hexosaminidase and cathepsin D in serum and urine of healthy subjects and patients with elevated activity of lysosomal enzymes
    • Zuhlsdorf M., Imort M., Hasilik A., von F.K. Molecular forms of beta-hexosaminidase and cathepsin D in serum and urine of healthy subjects and patients with elevated activity of lysosomal enzymes. Biochem. J. 1983, 213:733-740.
    • (1983) Biochem. J. , vol.213 , pp. 733-740
    • Zuhlsdorf, M.1    Imort, M.2    Hasilik, A.3    von, F.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.