메뉴 건너뛰기




Volumn 442, Issue 2, 2008, Pages 96-99

Bcl-xL inhibits Bax-induced alterations in mitochondrial respiration and calcium release

Author keywords

ADP; Apoptosis; ATP; Bax; Bcl xL; Calcium; Cell death; Mitochondria; Respiratory chain

Indexed keywords

PROTEIN BAX; PROTEIN BCL XL; RECOMBINANT PROTEIN;

EID: 48149114659     PISSN: 03043940     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neulet.2008.06.073     Document Type: Article
Times cited : (9)

References (29)
  • 1
    • 0037147239 scopus 로고    scopus 로고
    • Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature
    • Basañes G., Sharpe J.C., Galanis J., Brandt T.B., Hardwick J.M., and Zimmerberg J. Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature. J. Biol. Chem. 277 (2002) 49360-49365
    • (2002) J. Biol. Chem. , vol.277 , pp. 49360-49365
    • Basañes, G.1    Sharpe, J.C.2    Galanis, J.3    Brandt, T.B.4    Hardwick, J.M.5    Zimmerberg, J.6
  • 2
    • 0344825875 scopus 로고    scopus 로고
    • Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis
    • Boehning D., Patterson R.L., Sedaghat L., Glebova N.O., Kurosaki T., and Snyder S. Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis. Nat. Cell Biol. 5 (2003) 1051-1061
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1051-1061
    • Boehning, D.1    Patterson, R.L.2    Sedaghat, L.3    Glebova, N.O.4    Kurosaki, T.5    Snyder, S.6
  • 4
    • 0034786019 scopus 로고    scopus 로고
    • BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis
    • Cheng E.H., Wei M.C., Weiler S., Flavel R.A., Mak T.W., Lindsten T., and Korsmeyer S.J. BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. Mol. Cell. 8 (2001) 705-711
    • (2001) Mol. Cell. , vol.8 , pp. 705-711
    • Cheng, E.H.1    Wei, M.C.2    Weiler, S.3    Flavel, R.A.4    Mak, T.W.5    Lindsten, T.6    Korsmeyer, S.J.7
  • 5
    • 0037418861 scopus 로고    scopus 로고
    • Apoptosis-the calcium connection
    • Demaurex N., and Distelhorst C. Apoptosis-the calcium connection. Science 300 (2003) 65-67
    • (2003) Science , vol.300 , pp. 65-67
    • Demaurex, N.1    Distelhorst, C.2
  • 7
    • 0036291021 scopus 로고    scopus 로고
    • Bcl-X(L) and calyculin A prevent translocation of Bax to mitochondria during apoptosis
    • Ganju N., and Eastman A. Bcl-X(L) and calyculin A prevent translocation of Bax to mitochondria during apoptosis. Biochem. Biophys. Res. Commun. 291 (2002) 1258-1264
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 1258-1264
    • Ganju, N.1    Eastman, A.2
  • 8
    • 0033781027 scopus 로고    scopus 로고
    • The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant
    • Goldstein J.C., Waterhouse N.J., Juin P., Evan G.I., and Green D.R. The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant. Nat. Cell Biol. 2 (2000) 156-162
    • (2000) Nat. Cell Biol. , vol.2 , pp. 156-162
    • Goldstein, J.C.1    Waterhouse, N.J.2    Juin, P.3    Evan, G.I.4    Green, D.R.5
  • 10
    • 0032528118 scopus 로고    scopus 로고
    • Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis
    • Gross A., Jockel J., Wei M.C., and Korsmeyer S.J. Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis. EMBO J. 17 (1998) 3878-3885
    • (1998) EMBO J. , vol.17 , pp. 3878-3885
    • Gross, A.1    Jockel, J.2    Wei, M.C.3    Korsmeyer, S.J.4
  • 12
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis
    • Hsu Y.T., Wolter K.G., and Youle R.J. Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis. Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 3668-3672
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 3668-3672
    • Hsu, Y.T.1    Wolter, K.G.2    Youle, R.J.3
  • 13
    • 0032562796 scopus 로고    scopus 로고
    • Nonionic detergents induce dimerization among members of the Bcl-2 family
    • Hsu Y.T., and Youle R.J. Nonionic detergents induce dimerization among members of the Bcl-2 family. J. Biol. Chem. 273 (1998) 10777-10783
    • (1998) J. Biol. Chem. , vol.273 , pp. 10777-10783
    • Hsu, Y.T.1    Youle, R.J.2
  • 14
    • 34247506768 scopus 로고    scopus 로고
    • A tale of two mitochondrial channels, MAC and PTP, in apoptosis
    • Kinnally K., and Antonson B. A tale of two mitochondrial channels, MAC and PTP, in apoptosis. Apoptosis 12 (2007) 857-868
    • (2007) Apoptosis , vol.12 , pp. 857-868
    • Kinnally, K.1    Antonson, B.2
  • 15
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer G., Galluzzi L., and Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol. Rev. 87 (2007) 99-163
    • (2007) Physiol. Rev. , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 20
    • 0032571294 scopus 로고    scopus 로고
    • The overexpression of Bax produces cell death upon induction of the mitochondrial permeability transition
    • Pastorino J.G., Chen S.T., Tafani M., Snyder J.W., and Farber J.L. The overexpression of Bax produces cell death upon induction of the mitochondrial permeability transition. J. Biol. Chem. 273 (1998) 7770-7775
    • (1998) J. Biol. Chem. , vol.273 , pp. 7770-7775
    • Pastorino, J.G.1    Chen, S.T.2    Tafani, M.3    Snyder, J.W.4    Farber, J.L.5
  • 22
    • 0034866507 scopus 로고    scopus 로고
    • Bax translocation to mitochondria subsequent to a rapid loss of mitochondrial membrane potential
    • Smaili S.S., Hsu Y.-T., Sanders K., Russell J.T., and Youle R.J. Bax translocation to mitochondria subsequent to a rapid loss of mitochondrial membrane potential. Cell Death Differ. 8 (2001) 909-920
    • (2001) Cell Death Differ. , vol.8 , pp. 909-920
    • Smaili, S.S.1    Hsu, Y.-T.2    Sanders, K.3    Russell, J.T.4    Youle, R.J.5
  • 23
    • 0033570890 scopus 로고    scopus 로고
    • Apoptosis driven by IP(3)-linked mitochondrial calcium signals
    • Szalai G., Krishnamurthy R., and Hajnóczky G. Apoptosis driven by IP(3)-linked mitochondrial calcium signals. EMBO J. 18 (1999) 6349-6361
    • (1999) EMBO J. , vol.18 , pp. 6349-6361
    • Szalai, G.1    Krishnamurthy, R.2    Hajnóczky, G.3
  • 25
  • 26
    • 0035380462 scopus 로고    scopus 로고
    • L promotes the open configuration of the voltage-dependent anion channel and metabolite passage through the outer mitochondrial membrane
    • L promotes the open configuration of the voltage-dependent anion channel and metabolite passage through the outer mitochondrial membrane. J. Biol. Chem. 276 (2001) 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
  • 29
    • 35848929088 scopus 로고    scopus 로고
    • Complete activation of Bax by a single site mutation
    • Zhou H., Hou Q., Hansen J.L., and Hsu Y.T. Complete activation of Bax by a single site mutation. Oncogene 26 (2007) 7092-7102
    • (2007) Oncogene , vol.26 , pp. 7092-7102
    • Zhou, H.1    Hou, Q.2    Hansen, J.L.3    Hsu, Y.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.