메뉴 건너뛰기




Volumn 287, Issue 2, 2012, Pages 1178-1188

Cathepsin B overexpression due to acid sphingomyelinase ablation promotes liver fibrosis in Niemann-Pick disease

Author keywords

[No Author keywords available]

Indexed keywords

ACID SPHINGOMYELINASE; BASAL LEVELS; CATHEPSIN B; CHRONIC TREATMENT; FUNCTIONAL RELATIONSHIP; HEPATIC STELLATE CELLS; IN-VITRO; IN-VIVO; LIVER DISEASE; LIVER FIBROSIS; MICE MODELS; NEURODEGENERATION; OVER-EXPRESSION; PHARMACOLOGICAL INHIBITION; PROTEOLYTIC PROCESSING; SMOOTH MUSCLE ACTINS; WILD TYPES;

EID: 84855503594     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.272393     Document Type: Article
Times cited : (50)

References (38)
  • 1
    • 62749184862 scopus 로고    scopus 로고
    • Roles and regulation of secretory and lysosomal acid sphingomyelinase
    • Jenkins, R. W., Canals, D., and Hannun, Y. A. (2009) Roles and regulation of secretory and lysosomal acid sphingomyelinase. Cell. Signal. 21, 836-846
    • (2009) Cell. Signal. , vol.21 , pp. 836-846
    • Jenkins, R.W.1    Canals, D.2    Hannun, Y.A.3
  • 2
    • 34047242070 scopus 로고    scopus 로고
    • Sphingolipids and cell death
    • DOI 10.1007/s10495-007-0721-0, Special Issue on Mitochondria in Apoptosis
    • Morales, A., Lee, H., Goñi, F. M., Kolesnick, R., and Fernandez-Checa, J. C. (2007) Sphingolipids and cell death. Apoptosis 12, 923-939 (Pubitemid 46653290)
    • (2007) Apoptosis , vol.12 , Issue.5 , pp. 923-939
    • Morales, A.1    Lee, H.2    Goni, F.M.3    Kolesnick, R.4    Fernandez-Checa, J.C.5
  • 3
    • 54049092827 scopus 로고    scopus 로고
    • The unexpected role of acid sphingomyelinase in cell death and the pathophysiology of common diseases
    • Smith, E. L., and Schuchman, E. H. (2008) The unexpected role of acid sphingomyelinase in cell death and the pathophysiology of common diseases. FASEB J. 22, 3419-3431
    • (2008) FASEB J. , vol.22 , pp. 3419-3431
    • Smith, E.L.1    Schuchman, E.H.2
  • 4
    • 79952809986 scopus 로고    scopus 로고
    • A novel mechanism of lysosomal acid sphingomyelinase maturation: Requirement for carboxylterminal proteolytic processing
    • Jenkins, R. W., Idkowiak-Baldys, J., Simbari, F., Canals, D., Roddy, P., Riner, C. D., Clarke, C. J., and Hannun, Y. A. (2011) A novel mechanism of lysosomal acid sphingomyelinase maturation: requirement for carboxylterminal proteolytic processing. J. Biol. Chem. 286, 3777-3788
    • (2011) J. Biol. Chem. , vol.286 , pp. 3777-3788
    • Jenkins, R.W.1    Idkowiak-Baldys, J.2    Simbari, F.3    Canals, D.4    Roddy, P.5    Riner, C.D.6    Clarke, C.J.7    Hannun, Y.A.8
  • 5
    • 0014083339 scopus 로고
    • Sphingomyelinase in normal human spleens and in spleens from subjects with Niemann-Pick disease
    • Schneider, P. B., and Kennedy, E. P. (1967) Sphingomyelinase in normal human spleens and in spleens from subjects with Niemann-Pick disease. J. Lipid Res. 8, 202-209
    • (1967) J. Lipid Res. , vol.8 , pp. 202-209
    • Schneider, P.B.1    Kennedy, E.P.2
  • 6
    • 77951893147 scopus 로고    scopus 로고
    • Acid sphingomyelinase, cell membranes and human disease: Lessons from Niemann-Pick disease
    • Schuchman, E. H. (2010) Acid sphingomyelinase, cell membranes and human disease: lessons from Niemann-Pick disease. FEBS Lett. 584, 1895-1900
    • (2010) FEBS Lett. , vol.584 , pp. 1895-1900
    • Schuchman, E.H.1
  • 7
    • 77649223760 scopus 로고    scopus 로고
    • The pathogenesis and treatment of acid sphingomyelinase- deficient Niemann-Pick disease
    • Schuchman, E. H. (2009) The pathogenesis and treatment of acid sphingomyelinase- deficient Niemann-Pick disease. Int. J. Clin. Pharmacol. Ther. 47, S48-57
    • (2009) Int. J. Clin. Pharmacol. Ther. , vol.47
    • Schuchman, E.H.1
  • 9
    • 0029014350 scopus 로고
    • Acid sphingomyelinase-deficient mice mimic the neurovisceral form of human lysosomal storage disease (Niemann-Pick disease)
    • Otterbach, B., and Stoffel, W. (1995) Acid sphingomyelinase-deficient mice mimic the neurovisceral form of human lysosomal storage disease (Niemann-Pick disease). Cell 81, 1053-1061
    • (1995) Cell , vol.81 , pp. 1053-1061
    • Otterbach, B.1    Stoffel, W.2
  • 10
    • 65449128051 scopus 로고    scopus 로고
    • Cathepsins B and D drive hepatic stellate cell proliferation and promote their fibrogenic potential
    • Moles, A., Tarrats, N., Fernández-Checa, J. C., and Marí, M. (2009) Cathepsins B and D drive hepatic stellate cell proliferation and promote their fibrogenic potential. Hepatology 49, 1297-1307
    • (2009) Hepatology , vol.49 , pp. 1297-1307
    • Moles, A.1    Tarrats, N.2    Fernández-Checa, J.C.3    Marí, M.4
  • 11
    • 35248897299 scopus 로고    scopus 로고
    • Cathepsin cysteine proteases in cardiovascular disease
    • DOI 10.1096/fj.06-7924com
    • Lutgens, S. P., Cleutjens, K. B., Daemen, M. J., and Heeneman, S. (2007) Cathepsin cysteine proteases in cardiovascular disease. FASEB J. 21, 3029-3041 (Pubitemid 47565524)
    • (2007) FASEB Journal , vol.21 , Issue.12 , pp. 3029-3041
    • Lutgens, S.P.M.1    Cleutjens, K.B.J.M.2    Daemen, M.J.A.P.3    Heeneman, S.4
  • 12
    • 48249121176 scopus 로고    scopus 로고
    • New insights into the roles of endolysosomal cathepsins in the pathogenesis of Alzheimer's disease: Cathepsin inhibitors as potential therapeutics
    • Haque, A., Banik, N. L., and Ray, S. K. (2008) New insights into the roles of endolysosomal cathepsins in the pathogenesis of Alzheimer's disease: cathepsin inhibitors as potential therapeutics. CNS Neurol. Disord. Drug Targets 7, 270-277
    • (2008) CNS Neurol. Disord. Drug Targets , vol.7 , pp. 270-277
    • Haque, A.1    Banik, N.L.2    Ray, S.K.3
  • 13
    • 33846164404 scopus 로고    scopus 로고
    • Emerging roles of cysteine cathepsins in disease and their potential as drug targets
    • DOI 10.2174/138161207780162962
    • Vasiljeva, O., Reinheckel, T., Peters, C., Turk, D., Turk, V., and Turk, B. (2007) Emerging roles of cysteine cathepsins in disease and their potential as drug targets. Curr. Pharm. Des. 13, 387-403 (Pubitemid 46477760)
    • (2007) Current Pharmaceutical Design , vol.13 , Issue.4 , pp. 387-403
    • Vasiljeva, O.1    Reinheckel, T.2    Peters, C.3    Turk, D.4    Turk, V.5    Turk, B.6
  • 19
    • 0026057831 scopus 로고
    • Cirrhosis and portal hypertension in a patient with adult Niemann-Pick disease
    • Tassoni, J. P., Jr., Fawaz, K. A., and Johnston, D. E. (1991) Cirrhosis and portal hypertension in a patient with adult Niemann-Pick disease. Gastroenterology 100, 567-569
    • (1991) Gastroenterology , vol.100 , pp. 567-569
    • Tassoni Jr., J.P.1    Fawaz, K.A.2    Johnston, D.E.3
  • 22
    • 2142657911 scopus 로고    scopus 로고
    • Acidic sphingomyelinase downregulates the liver-specific methionine adenosyltransferase 1A, contributing to tumor necrosis factor-induced lethal hepatitis
    • Marí, M., Colell, A., Morales, A., Pañeda, C., Varela-Nieto, I., García-Ruiz, C., and Fernández-Checa, J. C. (2004) Acidic sphingomyelinase downregulates the liver-specific methionine adenosyltransferase 1A, contributing to tumor necrosis factor-induced lethal hepatitis. J. Clin. Invest. 113, 895-904
    • (2004) J. Clin. Invest. , vol.113 , pp. 895-904
    • Marí, M.1    Colell, A.2    Morales, A.3    Pañeda, C.4    Varela-Nieto, I.5    García-Ruiz, C.6    Fernández-Checa, J.C.7
  • 23
    • 0019880528 scopus 로고
    • A simple method to determine nanogram levels of 4-hydroxyproline in biological tissues
    • Jamall, I. S., Finelli, V. N., and Que Hee, S. S. (1981) A simple method to determine nanogram levels of 4-hydroxyproline in biological tissues. Anal. Biochem. 112, 70-75
    • (1981) Anal. Biochem. , vol.112 , pp. 70-75
    • Jamall, I.S.1    Finelli, V.N.2    Que Hee, S.S.3
  • 26
    • 77954164469 scopus 로고    scopus 로고
    • Connecting Hsp70, sphingolipid metabolism and lysosomal stability
    • Petersen, N. H., Kirkegaard, T, Olsen, O. D., and Jäättelä , M. (2010) Connecting Hsp70, sphingolipid metabolism and lysosomal stability. Cell Cycle 9, 2305-2309
    • (2010) Cell Cycle , vol.9 , pp. 2305-2309
    • Petersen, N.H.1    Kirkegaard, T.2    Olsen, O.D.3    Jäättelä, M.4
  • 27
    • 2942687937 scopus 로고    scopus 로고
    • The cell biology of lysosomal storage disorders
    • DOI 10.1038/nrm1423
    • Futerman, A. H., and van Meer, G. (2004) The cell biology of lysosomal storage disorders. Nat. Rev. Mol. Cell Biol. 5, 554-565 (Pubitemid 38868584)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.7 , pp. 554-565
    • Futerman, A.H.1    Van Meer, G.2
  • 29
    • 15744378799 scopus 로고    scopus 로고
    • Altered cholesterol metabolism in Niemann-Pick type C1 mouse brains affects mitochondrial function
    • DOI 10.1074/jbc.M412898200
    • Yu, W., Gong, J. S., Ko, M., Garver, W. S., Yanagisawa, K., and Michikawa, M. (2005) Altered cholesterol metabolism in Niemann-Pick type C1 mouse brains affects mitochondrial function. J. Biol. Chem. 280, 11731-11739 (Pubitemid 40418487)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 11731-11739
    • Yu, W.1    Gong, J.-S.2    Ko, M.3    Garver, W.S.4    Yanagisawa, K.5    Michikawa, M.6
  • 30
    • 73549105909 scopus 로고    scopus 로고
    • Increased activity and altered subcellular distribution of lysosomal enzymes determine neuronal vulnerability in Niemann-Pick type C1-deficient mice
    • Amritraj, A., Peake, K., Kodam, A., Salio, C., Merighi, A., Vance, J. E., and Kar, S. (2009) Increased activity and altered subcellular distribution of lysosomal enzymes determine neuronal vulnerability in Niemann-Pick type C1-deficient mice. Am. J. Pathol. 175, 2540-2556
    • (2009) Am. J. Pathol. , vol.175 , pp. 2540-2556
    • Amritraj, A.1    Peake, K.2    Kodam, A.3    Salio, C.4    Merighi, A.5    Vance, J.E.6    Kar, S.7
  • 34
    • 77953142003 scopus 로고    scopus 로고
    • Improvement in lipid and protein trafficking in Niemann- Pick C1 cells by correction of a secondary enzyme defect
    • Devlin, C., Pipalia, N. H., Liao, X., Schuchman, E. H., Maxfield, F. R., and Tabas, I. (2010) Improvement in lipid and protein trafficking in Niemann- Pick C1 cells by correction of a secondary enzyme defect. Traffic 11, 601-615
    • (2010) Traffic , vol.11 , pp. 601-615
    • Devlin, C.1    Pipalia, N.H.2    Liao, X.3    Schuchman, E.H.4    Maxfield, F.R.5    Tabas, I.6
  • 35
    • 53749099057 scopus 로고    scopus 로고
    • Characterization of common SMPD1 mutations causing types A and B Niemann-Pick disease and generation of mutation-specific mouse models
    • Jones, I., He, X., Katouzian, F., Darroch, P. I., and Schuchman, E. H. (2008) Characterization of common SMPD1 mutations causing types A and B Niemann-Pick disease and generation of mutation-specific mouse models. Mol. Genet. Metab. 95, 152-162
    • (2008) Mol. Genet. Metab. , vol.95 , pp. 152-162
    • Jones, I.1    He, X.2    Katouzian, F.3    Darroch, P.I.4    Schuchman, E.H.5
  • 36
    • 0027932927 scopus 로고
    • Accurate differentiation of neuronopathic and nonneuronopathic forms of Niemann-Pick disease by evaluation of the effective residual lysosomal sphingomyelinase activity in intact cells
    • Graber, D., Salvayre, R., and Levade, T. (1994) Accurate differentiation of neuronopathic and nonneuronopathic forms of Niemann-Pick disease by evaluation of the effective residual lysosomal sphingomyelinase activity in intact cells. J. Neurochem. 63, 1060-1068 (Pubitemid 24266620)
    • (1994) Journal of Neurochemistry , vol.63 , Issue.3 , pp. 1060-1068
    • Graber, D.1    Salvayre, R.2    Levade, T.3
  • 37
    • 79851470428 scopus 로고    scopus 로고
    • Brain pathology in Niemann-Pick disease type A: Insights from the acid sphingomyelinase knockout mice
    • Ledesma, M. D., Prinetti, A., Sonnino, S., and Schuchman, E. H. (2011) Brain pathology in Niemann-Pick disease type A: insights from the acid sphingomyelinase knockout mice. J. Neurochem. 116, 779-788
    • (2011) J. Neurochem. , vol.116 , pp. 779-788
    • Ledesma, M.D.1    Prinetti, A.2    Sonnino, S.3    Schuchman, E.H.4
  • 38


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.