메뉴 건너뛰기




Volumn 12, Issue 7, 2005, Pages 751-760

The voltage-dependent anion channel-1 modulates apoptotic cell death

Author keywords

Apoptosis; Hexokinase; Mitochondria; Ruthenium red; VDAC

Indexed keywords

ACRIDINE ORANGE; AMINO ACID; ANION CHANNEL; DICYCLOHEXYLCARBODIIMIDE; ETHIDIUM BROMIDE; GLUTAMIC ACID; HEXOKINASE; PROTEIN INHIBITOR; RUTHENIUM RED; VOLTAGE GATED CHANNEL FORMING PROTEIN;

EID: 21744441655     PISSN: 13509047     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cdd.4401599     Document Type: Article
Times cited : (262)

References (47)
  • 1
    • 0032531818 scopus 로고    scopus 로고
    • Calcium - A life and death signal
    • Berridge MJ, Bootman MD and Lipp P (1998) Calcium - a life and death signal. Nature 395: 645-648
    • (1998) Nature , vol.395 , pp. 645-648
    • Berridge, M.J.1    Bootman, M.D.2    Lipp, P.3
  • 5
    • 0032587982 scopus 로고    scopus 로고
    • Bcl-xL prevents cell death following growth factor withdrawal by facilitating mitochondrial ATP/ADP exchange
    • Vander Heiden MG, Chandel NS, Schumacker PT and Thompson CB (1999) Bcl-xL prevents cell death following growth factor withdrawal by facilitating mitochondrial ATP/ADP exchange. Mol. Cell 3: 159-167
    • (1999) Mol. Cell , vol.3 , pp. 159-167
    • Vander Heiden, M.G.1    Chandel, N.S.2    Schumacker, P.T.3    Thompson, C.B.4
  • 6
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti M and Szabo I (1995) The mitochondrial permeability transition. Biochim. Biophys. Acta 1241: 139-176
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabo, I.2
  • 7
    • 0035881510 scopus 로고    scopus 로고
    • Calcium binding and translocation by the voltage-dependent anion channel: A possible regulatory mechanism in mitochondrial function
    • Gincel D, Zaid H and Shoshan-Barmatz V (2001) Calcium binding and translocation by the voltage-dependent anion channel: a possible regulatory mechanism in mitochondrial function. Biochem. J. 358: 147-155
    • (2001) Biochem. J. , vol.358 , pp. 147-155
    • Gincel, D.1    Zaid, H.2    Shoshan-Barmatz, V.3
  • 8
    • 0032827410 scopus 로고    scopus 로고
    • Mitochondrial transport of cations: Channels, exchangers, and permeability transition
    • Bernardi P (1999) Mitochondrial transport of cations: channels, exchangers, and permeability transition. Physiol. Rev. 79: 1127-1155
    • (1999) Physiol. Rev. , vol.79 , pp. 1127-1155
    • Bernardi, P.1
  • 10
    • 0942297436 scopus 로고    scopus 로고
    • The voltage-dependent anion channel: Characterization, modulation, and role in mitochondrial function in cell life and death
    • Shoshan-Barmatz V and Gincel D (2003) The voltage-dependent anion channel: characterization, modulation, and role in mitochondrial function in cell life and death. Cell Biochem. Biophys. 39: 279-292
    • (2003) Cell Biochem. Biophys. , vol.39 , pp. 279-292
    • Shoshan-Barmatz, V.1    Gincel, D.2
  • 12
    • 0036287992 scopus 로고    scopus 로고
    • Retinal voltage-dependent anion channel: Characterization and cellular localization
    • Gincel D, Vardi N and Shoshan-Barmatz V (2002) Retinal voltage-dependent anion channel: characterization and cellular localization. Invest. Ophthalmol. Vis. Sci. 43: 2097-2104
    • (2002) Invest. Ophthalmol. Vis. Sci. , vol.43 , pp. 2097-2104
    • Gincel, D.1    Vardi, N.2    Shoshan-Barmatz, V.3
  • 14
    • 0028168454 scopus 로고
    • 2+ release channel (ryanodine receptor) of rabbit skeletal muscle sarcoplasmic reticulum
    • 2+ release channel (ryanodine receptor) of rabbit skeletal muscle sarcoplasmic reticulum. J. Biol. Chem. 269: 22698-22704
    • (1994) J. Biol. Chem. , vol.269 , pp. 22698-22704
    • Chen, S.R.1    MacLennan, D.H.2
  • 16
    • 0026793692 scopus 로고
    • Ruthenium red inhibits the binding of calcium to calmodulin required for enzyme activation
    • Sasaki T, Naka M, Nakamura F and Tanaka T (1992) Ruthenium red inhibits the binding of calcium to calmodulin required for enzyme activation. J. Biol. Chem. 267: 21518-21523
    • (1992) J. Biol. Chem. , vol.267 , pp. 21518-21523
    • Sasaki, T.1    Naka, M.2    Nakamura, F.3    Tanaka, T.4
  • 18
    • 0019409829 scopus 로고
    • The effect of ruthenium red on the assembly and disassembly of microtubules and on rapid axonal transport
    • Deinum J, Wallin M, Kanje M and Lagercrantz C (1981) The effect of ruthenium red on the assembly and disassembly of microtubules and on rapid axonal transport. Biochim. Biophys. Acta 675: 209-213
    • (1981) Biochim. Biophys. Acta , vol.675 , pp. 209-213
    • Deinum, J.1    Wallin, M.2    Kanje, M.3    Lagercrantz, C.4
  • 19
    • 0025783891 scopus 로고
    • Inhibition of mitochondrial calcium ion transport by an oxo-bridged dinuclear ruthenium ammine complex
    • Ying WL, Emerson J, Clarke MJ and Sanadi DR (1991) Inhibition of mitochondrial calcium ion transport by an oxo-bridged dinuclear ruthenium ammine complex. Biochemistry 30: 4949-4952
    • (1991) Biochemistry , vol.30 , pp. 4949-4952
    • Ying, W.L.1    Emerson, J.2    Clarke, M.J.3    Sanadi, D.R.4
  • 22
    • 0034801483 scopus 로고    scopus 로고
    • 2+ in microcystin-induced mitochondrial permeability transition in rat hepatocytes
    • 2+ in microcystin-induced mitochondrial permeability transition in rat hepatocytes. Biochem. Biophys. Res. Commun. 285: 1155-1161
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , pp. 1155-1161
    • Ding, W.X.1    Shen, H.M.2    Ong, C.N.3
  • 23
    • 0037192787 scopus 로고    scopus 로고
    • Increased hexokinase activity, of either ectopic or endogenous origin, protects renal epithelial cells against acute oxidant-induced cell death
    • Bryson JM, Coy PE, Gottlob K, Hay N and Robey RB (2002) Increased hexokinase activity, of either ectopic or endogenous origin, protects renal epithelial cells against acute oxidant-induced cell death. J. Biol. Chem. 277: 11392-11400
    • (2002) J. Biol. Chem. , vol.277 , pp. 11392-11400
    • Bryson, J.M.1    Coy, P.E.2    Gottlob, K.3    Hay, N.4    Robey, R.B.5
  • 24
    • 0036510541 scopus 로고    scopus 로고
    • Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis
    • Pastorino JG, Shulga N and Hoek JB (2002) Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis. J. Biol. Chem. 277: 7610-7618
    • (2002) J. Biol. Chem. , vol.277 , pp. 7610-7618
    • Pastorino, J.G.1    Shulga, N.2    Hoek, J.B.3
  • 25
    • 0942290437 scopus 로고    scopus 로고
    • In self-defence: Hexokinase promotes voltage-dependent anion channel closure and prevents mitochondria-mediated apoptotic cell death
    • Azoulay-Zohar H, Israelson A, Abu-Hamad S and Shoshan-Barmatz V (2004) In self-defence: hexokinase promotes voltage-dependent anion channel closure and prevents mitochondria-mediated apoptotic cell death. Biochem. J. 377: 347-355
    • (2004) Biochem. J. , vol.377 , pp. 347-355
    • Azoulay-Zohar, H.1    Israelson, A.2    Abu-Hamad, S.3    Shoshan-Barmatz, V.4
  • 26
    • 0029018094 scopus 로고
    • Further evidence for multitopological localization of mammalian porin (VDAC) in the plasmalemma forming part of a chloride channel complex affected in cystic fibrosis and encephalomyopathy
    • Reymann S, Florke H, Heiden M, Jakob C, Stadtmuller U, Steinacker P, Lalk VE, Pardowitz I and Thinnes FP (1995) Further evidence for multitopological localization of mammalian porin (VDAC) in the plasmalemma forming part of a chloride channel complex affected in cystic fibrosis and encephalomyopathy. Biochem. Mol. Med. 54: 75-87
    • (1995) Biochem. Mol. Med. , vol.54 , pp. 75-87
    • Reymann, S.1    Florke, H.2    Heiden, M.3    Jakob, C.4    Stadtmuller, U.5    Steinacker, P.6    Lalk, V.E.7    Pardowitz, I.8    Thinnes, F.P.9
  • 27
    • 0029914605 scopus 로고    scopus 로고
    • Indications of a common folding pattern for VDAC channels from all sources
    • Song J and Colombini M (1996) Indications of a common folding pattern for VDAC channels from all sources. J. Bioenerg. Biomembr. 28: 153-161
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 153-161
    • Song, J.1    Colombini, M.2
  • 28
    • 0030873947 scopus 로고    scopus 로고
    • Multicopy suppressors of phenotypes resulting from the absence of yeast VDAC encode a VDAC-like protein
    • Blachly-Dyson E, Song J, Wolfgang WJ, Colombini M and Forte M (1997) Multicopy suppressors of phenotypes resulting from the absence of yeast VDAC encode a VDAC-like protein. Mol. Cell. Biol. 17: 5727-5738
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5727-5738
    • Blachly-Dyson, E.1    Song, J.2    Wolfgang, W.J.3    Colombini, M.4    Forte, M.5
  • 29
    • 0027242022 scopus 로고
    • Location of the dicyclohexylcarbodiimide-reactive glutamate residue in the bovine heart mitochondrial porin
    • De Pinto V, al Jamal JA and Palmieri F (1993) Location of the dicyclohexylcarbodiimide-reactive glutamate residue in the bovine heart mitochondrial porin. J. Biol. Chem. 268: 12977-12982
    • (1993) J. Biol. Chem. , vol.268 , pp. 12977-12982
    • De Pinto, V.1    al Jamal, J.A.2    Palmieri, F.3
  • 30
    • 0032080218 scopus 로고    scopus 로고
    • Dicyclohexylcarbodiimide interaction with the voltage-dependent anion channel from sarcoplasmic reticulum
    • Shafir I, Feng W and Shoshan-Barmatz V (1998) Dicyclohexylcarbodiimide interaction with the voltage-dependent anion channel from sarcoplasmic reticulum. Eur. J. Biochem. 253: 627-636
    • (1998) Eur. J. Biochem. , vol.253 , pp. 627-636
    • Shafir, I.1    Feng, W.2    Shoshan-Barmatz, V.3
  • 32
    • 0022595453 scopus 로고
    • Hexokinase receptor complex in hepatoma mitochondria: Evidence from N, N′-dicyclohexylcarbodiimide-labeling studies for the involvement of the pore-forming protein VDAC
    • Nakashima RA, Mangan PS, Colombini M and Pedersen PL (1986) Hexokinase receptor complex in hepatoma mitochondria: evidence from N, N′-dicyclohexylcarbodiimide-labeling studies for the involvement of the pore-forming protein VDAC. Biochemistry 25: 1015-1021
    • (1986) Biochemistry , vol.25 , pp. 1015-1021
    • Nakashima, R.A.1    Mangan, P.S.2    Colombini, M.3    Pedersen, P.L.4
  • 33
    • 0242285732 scopus 로고    scopus 로고
    • VDAC is a conserved element of death pathways in plant and animal systems
    • Godbole A, Varghese J, Sarin A and Mathew MK (2003) VDAC is a conserved element of death pathways in plant and animal systems. Biochim. Biophys. Acta 1642: 87-96
    • (2003) Biochim. Biophys. Acta , vol.1642 , pp. 87-96
    • Godbole, A.1    Varghese, J.2    Sarin, A.3    Mathew, M.K.4
  • 34
    • 0036479011 scopus 로고    scopus 로고
    • The voltage-dependent anion channel: An essential player in apoptosis
    • Tsujimoto Y and Shimizu S (2002) The voltage-dependent anion channel: an essential player in apoptosis. Biochimie 84: 187-193
    • (2002) Biochimie , vol.84 , pp. 187-193
    • Tsujimoto, Y.1    Shimizu, S.2
  • 35
    • 14244269224 scopus 로고    scopus 로고
    • Oligomeric states of the voltage-dependent anion channel and cytochrome c release from mitochondria
    • Zalk R, Israelson A, Garty E, Azoulay-Zohar H and Shoshan-Barmatz V (2005) Oligomeric states of the voltage-dependent anion channel and cytochrome c release from mitochondria. Biochem. J. 386: 73-83
    • (2005) Biochem. J. , vol.386 , pp. 73-83
    • Zalk, R.1    Israelson, A.2    Garty, E.3    Azoulay-Zohar, H.4    Shoshan-Barmatz, V.5
  • 36
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu S, Narita M and Tsujimoto Y (1999) Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 399: 483-487
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 37
    • 0034724190 scopus 로고    scopus 로고
    • BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death
    • Shimizu S, Konishi A, Kodama T and Tsujimoto Y (2000) BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death. Proc. Natl. Acad. Sci. USA 97: 3100-3105
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3100-3105
    • Shimizu, S.1    Konishi, A.2    Kodama, T.3    Tsujimoto, Y.4
  • 38
    • 0035380462 scopus 로고    scopus 로고
    • Bcl-xL promotes the open configuration of the voltage-dependent anion channel and metabolite passage through the outer mitochondrial membrane
    • Vander Heiden MG, Li XX, Gottleib E, Hill RB, Thompson CB and Colombini M (2001) Bcl-xL promotes the open configuration of the voltage-dependent anion channel and metabolite passage through the outer mitochondrial membrane. J. Biol. Chem. 276: 19414-19419
    • (2001) J. Biol. Chem. , vol.276 , pp. 19414-19419
    • Vander Heiden, M.G.1    Li, X.X.2    Gottleib, E.3    Hill, R.B.4    Thompson, C.B.5    Colombini, M.6
  • 39
    • 0003097634 scopus 로고    scopus 로고
    • Protein degradation in mitochondria: Implications for oxidative stress, aging and disease: A novel etiological classification of mitochondrial proteolytic disorders
    • Bota AD and Davies KJA (2001) Protein degradation in mitochondria: implications for oxidative stress, aging and disease: a novel etiological classification of mitochondrial proteolytic disorders. Mitochondrion 1: 33-49
    • (2001) Mitochondrion , vol.1 , pp. 33-49
    • Bota, A.D.1    Davies, K.J.A.2
  • 40
    • 1442327526 scopus 로고    scopus 로고
    • Essential role of the voltage-dependent anion channel (VDAC) in mitochondrial permeability transition pore opening and cytochrome c release induced by arsenic trioxide
    • Zheng Y, Shi Y, Tian C, Jiang C, Jin H, Chen J, Almasan A, Tang H and Chen Q (2004) Essential role of the voltage-dependent anion channel (VDAC) in mitochondrial permeability transition pore opening and cytochrome c release induced by arsenic trioxide. Oncogene 23: 1239-1247
    • (2004) Oncogene , vol.23 , pp. 1239-1247
    • Zheng, Y.1    Shi, Y.2    Tian, C.3    Jiang, C.4    Jin, H.5    Chen, J.6    Almasan, A.7    Tang, H.8    Chen, Q.9
  • 41
    • 15644371838 scopus 로고    scopus 로고
    • The role of yeast VDAC genes on the permeability of the mitochondrial outer membrane
    • Lee AC, Xu X, Blachly-Dyson E, Forte M and Colombini M (1998) The role of yeast VDAC genes on the permeability of the mitochondrial outer membrane. J. Membr. Biol. 161: 173-181
    • (1998) J. Membr. Biol. , vol.161 , pp. 173-181
    • Lee, A.C.1    Xu, X.2    Blachly-Dyson, E.3    Forte, M.4    Colombini, M.5
  • 43
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the Biuret reaction
    • Gornall AG, Bardawill CJ and David MM (1949) Determination of serum proteins by means of the Biuret reaction. J. Biol. Chem. 177: 751-766
    • (1949) J. Biol. Chem. , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 44
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 45
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 46
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staelhelin T and Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76: 4350-4354
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staelhelin, T.2    Gordon, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.