메뉴 건너뛰기




Volumn 11, Issue 5, 2004, Pages 550-563

Cathepsin D links TNF-induced acid sphingomyelinase to Bid-mediated caspase-9 and -3 activation

Author keywords

A SMase; Bid; Caspases; Cathepsin D.; Ceramide; TNF

Indexed keywords

CASPASE 3; CASPASE 9; CATHEPSIN D; CERAMIDE; PROTEIN BCL 2; PROTEIN BID; RAB PROTEIN; SPHINGOMYELIN PHOSPHODIESTERASE; TUMOR NECROSIS FACTOR;

EID: 2442661614     PISSN: 13509047     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cdd.4401382     Document Type: Review
Times cited : (301)

References (51)
  • 2
    • 0032719378 scopus 로고    scopus 로고
    • Possible involvement of cytochrome c release and sequential activation of caspases in ceramide-induced apoptosis in SK-N-MC cells
    • Ito A, Uehara T, Tokumitsu A, Okuma Y and Nomura Y (1999) Possible involvement of cytochrome c release and sequential activation of caspases in ceramide-induced apoptosis in SK-N-MC cells. Biochim. Biophys. Acta 1452: 263-274
    • (1999) Biochim. Biophys. Acta , vol.1452 , pp. 263-274
    • Ito, A.1    Uehara, T.2    Tokumitsu, A.3    Okuma, Y.4    Nomura, Y.5
  • 4
    • 0032497837 scopus 로고    scopus 로고
    • The role of ceramide in cell signaling
    • Perry DK and Hannun YA (1998) The role of ceramide in cell signaling. Biochim. Biophys. Acta 1436: 233-243
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 233-243
    • Perry, D.K.1    Hannun, Y.A.2
  • 5
    • 0032489554 scopus 로고    scopus 로고
    • TNF receptor death domain-associated proteins TRADD and FADD signal activation of acid sphingomyelinase
    • Schwandner R, Wiegmann K, Bernado K, Kreder D and Krönke M (1998) TNF receptor death domain-associated proteins TRADD and FADD signal activation of acid sphingomyelinase. J. Biol. Chem. 273: 5916-5922
    • (1998) J. Biol. Chem. , vol.273 , pp. 5916-5922
    • Schwandner, R.1    Wiegmann, K.2    Bernado, K.3    Kreder, D.4    Krönke, M.5
  • 7
    • 0029782494 scopus 로고    scopus 로고
    • Cathepsin D protease mediates programmed cell death induced by interferon-γ, Fas/Apo-1 and TNF-α
    • Deiss LP, Galinka H, Berissi H, Cohen O and Kimchi A (1996) Cathepsin D protease mediates programmed cell death induced by interferon-γ, Fas/Apo-1 and TNF-α. EMBO J. 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
  • 8
    • 0033436344 scopus 로고    scopus 로고
    • Lysosomal release of cathepsin D precedes relocation of cytochrome c and loss of mitochondrial transmembrane potential during apoptosis by oxidative stress
    • Roberg K, Johansson U and Öllinger K (1999) Lysosomal release of cathepsin D precedes relocation of cytochrome c and loss of mitochondrial transmembrane potential during apoptosis by oxidative stress. Free Radic. Biol. Med. 27: 1228-1237
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 1228-1237
    • Roberg, K.1    Johansson, U.2    Öllinger, K.3
  • 9
    • 0034650786 scopus 로고    scopus 로고
    • Inhibition of cathepsin D prevents free-radical-induced apoptosis in rat cardiomyocytes
    • Öllinger K (2000) Inhibition of cathepsin D prevents free-radical-induced apoptosis in rat cardiomyocytes. Arch. Biochem. Biophys. 373: 346-351
    • (2000) Arch. Biochem. Biophys. , vol.373 , pp. 346-351
    • Öllinger, K.1
  • 10
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cystein proteases: More than scavengers
    • Turk B, Turk D and Turk V (2000) Lysosomal cystein proteases: more than scavengers. Biochem. Biophys. Acta 1477: 98-111
    • (2000) Biochem. Biophys. Acta , vol.1477 , pp. 98-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 17
    • 0035180207 scopus 로고    scopus 로고
    • Cathepsin B knock out mice are resistant to tumor necrosis factor-α-mediated hepatocyte apoptosis and liver injury
    • Guicciardi ME, Miyoshi H, Bronk SF and Gores GJ (2001) Cathepsin B knock out mice are resistant to tumor necrosis factor-α-mediated hepatocyte apoptosis and liver injury. Am. J. Pathol. 159: 2045-2054
    • (2001) Am. J. Pathol. , vol.159 , pp. 2045-2054
    • Guicciardi, M.E.1    Miyoshi, H.2    Bronk, S.F.3    Gores, G.J.4
  • 19
    • 0035408169 scopus 로고    scopus 로고
    • The lysosomal protease cathepsin D mediates apoptosis induced by oxidative stress
    • Kargedal K, Johansson U and Öllinger K (2001) The lysosomal protease cathepsin D mediates apoptosis induced by oxidative stress. FASEB J. 15: 1592-1594
    • (2001) FASEB J. , vol.15 , pp. 1592-1594
    • Kargedal, K.1    Johansson, U.2    Öllinger, K.3
  • 20
    • 0032580334 scopus 로고    scopus 로고
    • Potential role for cathepsin D in p53-dependent tumor suppression and chemosensitivity
    • Wu GS, Saftig P, Peters C and El-Deiry WS (1998) Potential role for cathepsin D in p53-dependent tumor suppression and chemosensitivity. Oncogene 16: 2177-2183
    • (1998) Oncogene , vol.16 , pp. 2177-2183
    • Wu, G.S.1    Saftig, P.2    Peters, C.3    El-Deiry, W.S.4
  • 21
    • 0036310279 scopus 로고    scopus 로고
    • Microinjection of cathepsin D induces caspase-dependent apoptosis in fibroblasts
    • Roberg K, Kagedal K and Öllinger K (2002) Microinjection of cathepsin D induces caspase-dependent apoptosis in fibroblasts. Am. J. Pathol. 161: 89-96
    • (2002) Am. J. Pathol. , vol.161 , pp. 89-96
    • Roberg, K.1    Kagedal, K.2    Öllinger, K.3
  • 22
    • 0035164416 scopus 로고    scopus 로고
    • A lysosomal protease enters the death scene
    • Salvesen GS (2001) A lysosomal protease enters the death scene. J. Clin. Invest. 107: 21-22
    • (2001) J. Clin. Invest. , vol.107 , pp. 21-22
    • Salvesen, G.S.1
  • 23
    • 0033832629 scopus 로고    scopus 로고
    • Noncaspase proteases in apoptosis
    • Johnson DE (2000) Noncaspase proteases in apoptosis. Leukemia 14: 1695-1730
    • (2000) Leukemia , vol.14 , pp. 1695-1730
    • Johnson, D.E.1
  • 25
    • 0030757986 scopus 로고    scopus 로고
    • Photo-oxidative disruption of lysosomal membranes causes apoptosis of cultured human fibroblasts
    • Brunk UT, Dalen H, Roberg K and Hellquist HB (1997) Photo-oxidative disruption of lysosomal membranes causes apoptosis of cultured human fibroblasts. Free Radic. Biol. Med. 23: 616-626
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 616-626
    • Brunk, U.T.1    Dalen, H.2    Roberg, K.3    Hellquist, H.B.4
  • 26
    • 17344370810 scopus 로고    scopus 로고
    • Uptake of oxidative LDL by macrophages results in partial lysosomal enzyme inactivation and relocation
    • Li W, Yuan XM, Olsson AG and Brunk UT (1998) Uptake of oxidative LDL by macrophages results in partial lysosomal enzyme inactivation and relocation. Arterioscler. Thromb. Vasc. Biol. 18: 177-184
    • (1998) Arterioscler. Thromb. Vasc. Biol. , vol.18 , pp. 177-184
    • Li, W.1    Yuan, X.M.2    Olsson, A.G.3    Brunk, U.T.4
  • 27
    • 0031897739 scopus 로고    scopus 로고
    • Oxidative stress causes relocation of the lysosomal enzyme cathepsin D with ensuing apoptosis in neonatal rat cardiomyocytes
    • Roberg K and Öllinger K (1998) Oxidative stress causes relocation of the lysosomal enzyme cathepsin D with ensuing apoptosis in neonatal rat cardiomyocytes. Am J. Pathol. 152: 1151-1156
    • (1998) Am. J. Pathol. , vol.152 , pp. 1151-1156
    • Roberg, K.1    Öllinger, K.2
  • 29
    • 0020538837 scopus 로고
    • Biosynthesis and transport of cathepsin D in cultured human fibroblasts
    • Gieselmann V, Pohlmann R, Hasilik A and Von Figura K (1983) Biosynthesis and transport of cathepsin D in cultured human fibroblasts. J. Cell Biol. 97: 1-5
    • (1983) J. Cell Biol. , vol.97 , pp. 1-5
    • Gieselmann, V.1    Pohlmann, R.2    Hasilik, A.3    Von Figura, K.4
  • 30
    • 0026653849 scopus 로고
    • Identification of subcellular compartments involved in biosynthetic processing of cathepsin D
    • Rijnboutt S, Stoorvogel W, Geuze HJ and Strous GJ (1992) Identification of subcellular compartments involved in biosynthetic processing of cathepsin D. J. Biol. Chem. 267: 15665-15672
    • (1992) J. Biol. Chem. , vol.267 , pp. 15665-15672
    • Rijnboutt, S.1    Stoorvogel, W.2    Geuze, H.J.3    Strous, G.J.4
  • 31
    • 0033974782 scopus 로고    scopus 로고
    • Luberto C Ceramide in the eukaryotic stress response
    • Hannun YA and Luberto C (2000) Ceramide in the eukaryotic stress response. Trends Cell Biol. 10: 73-80
    • (2000) Trends Cell Biol. , vol.10 , pp. 73-80
    • Hannun, Y.A.1
  • 32
    • 0031919157 scopus 로고    scopus 로고
    • Regulation of ceramide production and apoptosis
    • Kolesnick RN and Krönke M (1998) Regulation of ceramide production and apoptosis. Annu. Rev. Physiol. 60: 643-665
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 643-665
    • Kolesnick, R.N.1    Krönke, M.2
  • 35
    • 0034282716 scopus 로고    scopus 로고
    • CD95-mediated apoptosis in vivo involves acid sphingomyelinase
    • Kolesnick R and Gulbins E (2000) CD95-mediated apoptosis in vivo involves acid sphingomyelinase. J. Biol. Chem. 275: 27316-27323
    • (2000) J. Biol. Chem. , vol.275 , pp. 27316-27323
    • Kolesnick, R.1    Gulbins, E.2
  • 42
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • Chinnaiyan AM, O'Rourke K, Tewari M and Dixit VM (1995) FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 81: 505-512
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 43
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NFkB activation
    • Hsu H, Xiong J and Goeddel DV (1995) The TNF receptor 1-associated protein TRADD signals cell death and NFkB activation. Cell 81: 495-504
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 44
    • 0035018235 scopus 로고    scopus 로고
    • Evidence of a lysosomal pathway for apoptosis induced by the synthetic retinoid CD437 in human leukemia HL-60 cells
    • Zang Y, Beard RL, Chandraratna RA and Kang JX (2001) Evidence of a lysosomal pathway for apoptosis induced by the synthetic retinoid CD437 in human leukemia HL-60 cells. Cell Death Differ. 8: 477-485
    • (2001) Cell Death Differ. , vol.8 , pp. 477-485
    • Zang, Y.1    Beard, R.L.2    Chandraratna, R.A.3    Kang, J.X.4
  • 45
    • 0037742249 scopus 로고    scopus 로고
    • Inhibition of PI-3 kinase sensitizes vascular endothelial cells to cytokine-initiated cathepsin-dependent apoptosis
    • Madge LA, Li JH, Choi J and Pober JS (2003) Inhibition of PI-3 kinase sensitizes vascular endothelial cells to cytokine-initiated cathepsin-dependent apoptosis. J. Biol. Chem. 278: 21295-21306
    • (2003) J. Biol. Chem. , vol.278 , pp. 21295-21306
    • Madge, L.A.1    Li, J.H.2    Choi, J.3    Pober, J.S.4
  • 46
    • 0035887215 scopus 로고    scopus 로고
    • Sphingosine-induced apoptosis is dependent on lysosomal proteases
    • Kargedal K, Zhao MSvensson I and Brunk UT (2001) Sphingosine-induced apoptosis is dependent on lysosomal proteases. Biochem. J. 359: 335-343
    • (2001) Biochem. J. , vol.359 , pp. 335-343
    • Kargedal, K.1    Zhao, M.2    Svensson, I.3    Brunk, U.T.4
  • 47
    • 0030048987 scopus 로고    scopus 로고
    • Apoptosis induced in Jurkat cells by several agents is preceded by intracellular acidification
    • Gottlieb RA, Nordberg J, Skowronski E and Babior BM (1996) Apoptosis induced in Jurkat cells by several agents is preceded by intracellular acidification. Proc. Natl. Acad. Sci. USA 93: 654-658
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 654-658
    • Gottlieb, R.A.1    Nordberg, J.2    Skowronski, E.3    Babior, B.M.4
  • 48
    • 0033776271 scopus 로고    scopus 로고
    • Changes in intramitochondrial and cytosolic pH: Early events that modulate caspase activation during apoptosis
    • Matsuyama S, Llopis J, Deveraux QL, Tsien RY and Reed JC (2000) Changes in intramitochondrial and cytosolic pH: early events that modulate caspase activation during apoptosis. Nat. Cell Biol. 2: 318-325
    • (2000) Nat. Cell Biol. , vol.2 , pp. 318-325
    • Matsuyama, S.1    Llopis, J.2    Deveraux, Q.L.3    Tsien, R.Y.4    Reed, J.C.5
  • 49
    • 0034737646 scopus 로고    scopus 로고
    • Caspase-8-mediated intracellular acidification precedes mitochondrial dysfunction in somatostatin-induced apoptosis
    • Liu D, Martino G, Thangaraju M, Sharma M, Halwani F, Shen SH, Patel YC and Srikant CB (2000) Caspase-8-mediated intracellular acidification precedes mitochondrial dysfunction in somatostatin-induced apoptosis. J. Biol. Chem. 275: 9244-9250
    • (2000) J. Biol. Chem. , vol.275 , pp. 9244-9250
    • Liu, D.1    Martino, G.2    Thangaraju, M.3    Sharma, M.4    Halwani, F.5    Shen, S.H.6    Patel, Y.C.7    Srikant, C.B.8
  • 50
    • 0029083689 scopus 로고
    • Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atropy of the intestinal mucosa and profound destruction of lymphoid cells
    • Saftig P, Hetman M, Schmahl W, Weber K, Heine L, Mossmann H, Köster A, Hess B, Evers M, von Figura K and Peters C (1995) Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atropy of the intestinal mucosa and profound destruction of lymphoid cells. EMBO J. 14: 3599-3608
    • (1995) EMBO J. , vol.14 , pp. 3599-3608
    • Saftig, P.1    Hetman, M.2    Schmahl, W.3    Weber, K.4    Heine, L.5    Mossmann, H.6    Köster, A.7    Hess, B.8    Evers, M.9    von Figura, K.10    Peters, C.11
  • 51
    • 0037155788 scopus 로고    scopus 로고
    • Cytochrome c release upon Fas receptor activation depends on translocation of full length Bid and the induction of the mitochondrial permeability transition
    • Tafani M, Karpinich NO, Hurster K, Pastorino JG, Schneider T, Russo MA and Farber JL (2002) Cytochrome c release upon Fas receptor activation depends on translocation of full length Bid and the induction of the mitochondrial permeability transition. J. Biol. Chem. 277: 10073-10082
    • (2002) J. Biol. Chem. , vol.277 , pp. 10073-10082
    • Tafani, M.1    Karpinich, N.O.2    Hurster, K.3    Pastorino, J.G.4    Schneider, T.5    Russo, M.A.6    Farber, J.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.