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Volumn 12, Issue 12, 2003, Pages 2794-2804

α-lactalbumin unfolding is not sufficient to cause apoptosis, but is required for the conversion to HAMLET (human α-lactalbumin made lethal to tumor cells)

Author keywords

Lactalbumin; Ca2+ binding site; HAMLET; Protein folding; Tumor cell death

Indexed keywords

ALPHA LACTALBUMIN; CALCIUM ION; SOLVENT;

EID: 10744223979     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0231003     Document Type: Article
Times cited : (118)

References (37)
  • 2
    • 0030828472 scopus 로고    scopus 로고
    • Functional identification of calcium binding residues in bovine α-lactalbumin
    • Anderson, P.J., Brooks, C.L., and Berliner, L.J. 1997. Functional identification of calcium binding residues in bovine α-lactalbumin. Biochemistry 36: 11648-11654.
    • (1997) Biochemistry , vol.36 , pp. 11648-11654
    • Anderson, P.J.1    Brooks, C.L.2    Berliner, L.J.3
  • 3
    • 0037096128 scopus 로고    scopus 로고
    • Measurement of Ca2+-binding constants of proteins and presentation of the CaLigator software
    • Andre, I. and Linse, S. 2002. Measurement of Ca2+-binding constants of proteins and presentation of the CaLigator software. Anal. Biochem. 305: 195-205.
    • (2002) Anal. Biochem. , vol.305 , pp. 195-205
    • Andre, I.1    Linse, S.2
  • 4
    • 0026694189 scopus 로고
    • Calcium-43 NMR studies of calcium-binding lysozymes and α-lactalbumins
    • Aramini, J.M., Drakenberg, T., Hiraoki, T., Ke, Y., Nitta, K., and Vogel, H.J. 1992. Calcium-43 NMR studies of calcium-binding lysozymes and α-lactalbumins. Biochemistry 31: 6761-6768.
    • (1992) Biochemistry , vol.31 , pp. 6761-6768
    • Aramini, J.M.1    Drakenberg, T.2    Hiraoki, T.3    Ke, Y.4    Nitta, K.5    Vogel, H.J.6
  • 6
    • 0021143705 scopus 로고
    • Metal ion binding to the N and A conformers of bovine α-lactalbumin
    • Bratcher, S.C. and Kronman, M.J. 1984. Metal ion binding to the N and A conformers of bovine α-lactalbumin. J. Biol. Chem. 259: 10875-10886.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10875-10886
    • Bratcher, S.C.1    Kronman, M.J.2
  • 7
    • 0034711229 scopus 로고    scopus 로고
    • Crystal structures of apo-and holo-bovine α-lactalbumin at 2.2 Å resolution reveal an effect of calcium on inter-lobe interactions
    • Chrysina. E.D., Brew. K., and Acharya, K.R. 2000. Crystal structures of apo-and holo-bovine α-lactalbumin at 2.2 Å resolution reveal an effect of calcium on inter-lobe interactions. J. Biol. Chem. 275: 37021-37029.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37021-37029
    • Chrysina, E.D.1    Brew, K.2    Acharya, K.R.3
  • 9
    • 0023127316 scopus 로고
    • Comparison of the binding of Na+ and Ca2+ to bovine α-lactalbumin
    • Desmet, J., Hanssens. I., and van Cauwelaert, F. 1987. Comparison of the binding of Na+ and Ca2+ to bovine α-lactalbumin. Biochim. Biophys. Acta 912: 211-219.
    • (1987) Biochim. Biophys. Acta , vol.912 , pp. 211-219
    • Desmet, J.1    Hanssens, I.2    Van Cauwelaert, F.3
  • 11
    • 0021771671 scopus 로고
    • Carbon-13 NMR studies of native and modified ovine submaxillary mucin
    • Gerken, T.A. and Dearborn, D.G. 1984. Carbon-13 NMR studies of native and modified ovine submaxillary mucin. Biochemistry 23: 1485-1497.
    • (1984) Biochemistry , vol.23 , pp. 1485-1497
    • Gerken, T.A.1    Dearborn, D.G.2
  • 12
    • 0033053602 scopus 로고    scopus 로고
    • Energetics of solvent and ligand-induced conformational changes in α-lactalbumin
    • Griko, Y.V. and Remeta, D.P. 1999. Energetics of solvent and ligand-induced conformational changes in α-lactalbumin. Protein Sci. 8: 554-561.
    • (1999) Protein Sci. , vol.8 , pp. 554-561
    • Griko, Y.V.1    Remeta, D.P.2
  • 14
    • 0037584357 scopus 로고    scopus 로고
    • Multimeric α-lactalbumin from human milk induces apoptosis through a direct effect on cell nuclei
    • Hakansson, A., Andreasson, J., Zhivotovsky, B., Karpman, D., Orrenius, S., and Svanborg, C. 1999. Multimeric α-lactalbumin from human milk induces apoptosis through a direct effect on cell nuclei. Exp. Cell Res. 246: 451-460.
    • (1999) Exp. Cell Res. , vol.246 , pp. 451-460
    • Hakansson, A.1    Andreasson, J.2    Zhivotovsky, B.3    Karpman, D.4    Orrenius, S.5    Svanborg, C.6
  • 15
    • 0033605892 scopus 로고    scopus 로고
    • Crystallographic evaluation of internal motion of human α-lactalbumin refined by full-matrix least-squares method
    • Harata, K., Abe, Y., and Muraki, M. 1999. Crystallographic evaluation of internal motion of human α-lactalbumin refined by full-matrix least-squares method. J. Mol. Biol. 287: 347-358.
    • (1999) J. Mol. Biol. , vol.287 , pp. 347-358
    • Harata, K.1    Abe, Y.2    Muraki, M.3
  • 16
    • 0033961193 scopus 로고    scopus 로고
    • A calorimetric study of the influence of calcium on the stability of bovine α-lactalbumin
    • Hendrix, T., Griko, Y.V., and Privalov, P.L. 2000. A calorimetric study of the influence of calcium on the stability of bovine α-lactalbumin. Biophys. Chem. 84: 27-34.
    • (2000) Biophys. Chem. , vol.84 , pp. 27-34
    • Hendrix, T.1    Griko, Y.V.2    Privalov, P.L.3
  • 18
    • 0035160316 scopus 로고    scopus 로고
    • A folding variant of human α-lactalbumin induces mitochondrial permeability transition in isolated mitochondria
    • Kohler, C., Gogvadze, V., Hakansson, A., Svanborg, C., Orrenius, S., and Zhivotovsky, B. 2001. A folding variant of human α-lactalbumin induces mitochondrial permeability transition in isolated mitochondria. Eur. J. Biochem. 268: 186-191.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 186-191
    • Kohler, C.1    Gogvadze, V.2    Hakansson, A.3    Svanborg, C.4    Orrenius, S.5    Zhivotovsky, B.6
  • 19
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wuthrich, K. 1996. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph. 14: 51-56.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-56
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 20
    • 0024796120 scopus 로고
    • Metal-ion binding and the molecular conformational properties of α lactalbumin
    • Kronman, M.J. 1989. Metal-ion binding and the molecular conformational properties of α lactalbumin. Crit. Rev. Biochem. Mol. Biol. 24: 565-667.
    • (1989) Crit. Rev. Biochem. Mol. Biol. , vol.24 , pp. 565-667
    • Kronman, M.J.1
  • 21
    • 0019888355 scopus 로고
    • Characteristics of the binding of Ca2+ and other divalent metal ions to bovine α-lactalbumin
    • Kronman, M.J., Sinha, S.K., and Brew, K. 1981. Characteristics of the binding of Ca2+ and other divalent metal ions to bovine α-lactalbumin. J. Biol. Chem. 256: 8582-8587.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8582-8587
    • Kronman, M.J.1    Sinha, S.K.2    Brew, K.3
  • 22
    • 0036365845 scopus 로고    scopus 로고
    • Calcium binding to proteins studied via competition with chromophoric chelators
    • Linse, S. 2002. Calcium binding to proteins studied via competition with chromophoric chelators. Methods Mol. Biol. 173: 15-24.
    • (2002) Methods Mol. Biol. , vol.173 , pp. 15-24
    • Linse, S.1
  • 23
    • 0025823438 scopus 로고
    • Calcium binding to calmodulin and its globular domains
    • Linse, S., Helmersson, A., and Forsen, S. 1991a. Calcium binding to calmodulin and its globular domains. J. Biol. Chem. 266: 8050-8054.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8050-8054
    • Linse, S.1    Helmersson, A.2    Forsen, S.3
  • 26
    • 0019880942 scopus 로고
    • Calcium binding to α-lactalbumin: Structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changes
    • Permyakov, E.A., Yarmolenko, V.V., Kalinichenko, L.P., Morozova, L.A., and Burstein, E.A. 1981. Calcium binding to α-lactalbumin: Structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changes. Biochem. Biophys. Res. Commun. 100: 191-197.
    • (1981) Biochem. Biophys. Res. Commun. , vol.100 , pp. 191-197
    • Permyakov, E.A.1    Yarmolenko, V.V.2    Kalinichenko, L.P.3    Morozova, L.A.4    Burstein, E.A.5
  • 28
    • 0035664406 scopus 로고    scopus 로고
    • Mutating aspartate in the calcium-binding site of α-lactalbumin: Effects on the protein stability and cation binding
    • -. 2001b. Mutating aspartate in the calcium-binding site of α-lactalbumin: Effects on the protein stability and cation binding. Protein Eng. 14: 785-789.
    • (2001) Protein Eng. , vol.14 , pp. 785-789
  • 29
    • 0022214652 scopus 로고
    • Thermodynamics of the binding of calcium and strontium to bovine α-lactalbumin
    • Schaer, J.J., Milos, M., and Cox, J.A. 1985. Thermodynamics of the binding of calcium and strontium to bovine α-lactalbumin. FEBS Lett. 190: 77-80.
    • (1985) FEBS Lett. , vol.190 , pp. 77-80
    • Schaer, J.J.1    Milos, M.2    Cox, J.A.3
  • 30
    • 0020757935 scopus 로고
    • Interactions of divalent metal ions with bovine, human, and goat α-lactalbumins
    • Segawa, T. and Sugai, S. 1983. Interactions of divalent metal ions with bovine, human, and goat α-lactalbumins. J. Biochem. (Tokyo) 93: 1321-1328.
    • (1983) J. Biochem. (Tokyo) , vol.93 , pp. 1321-1328
    • Segawa, T.1    Sugai, S.2
  • 35
    • 0344201898 scopus 로고    scopus 로고
    • Lipids as cofactors in protein folding: Stereo-specific lipid-protein interactions are required to form HAMLET (human α-lactalbumin made lethal to tumor cells
    • this issue
    • Svensson, M., Mossberg, A., Pettersson, J., Linse, S., and Svanborg, C. 2003. Lipids as cofactors in protein folding: Stereo-specific lipid-protein interactions are required to form HAMLET (human α-lactalbumin made lethal to tumor cells. Protein Sci. (this issue).
    • (2003) Protein Sci.
    • Svensson, M.1    Mossberg, A.2    Pettersson, J.3    Linse, S.4    Svanborg, C.5
  • 36
    • 0036219540 scopus 로고    scopus 로고
    • Structural basis for difference in heat capacity increments for Ca(2+) binding to two α-lactalbumins
    • Vanhooren, A., Vanhee, K., Noyelle, K., Majer, Z., Joniau, M., and Hanssens, I. 2002. Structural basis for difference in heat capacity increments for Ca(2+) binding to two α-lactalbumins. Biophys. J. 82: 407- 417.
    • (2002) Biophys. J. , vol.82 , pp. 407-417
    • Vanhooren, A.1    Vanhee, K.2    Noyelle, K.3    Majer, Z.4    Joniau, M.5    Hanssens, I.6
  • 37
    • 0035823118 scopus 로고    scopus 로고
    • Comparison of the denaturant-induced unfolding of the bovine and human α-lactalbumin molten globules
    • Wijesinha-Bettoni, R., Dobson, C.M., and Redfield, C. 2001. Comparison of the denaturant-induced unfolding of the bovine and human α-lactalbumin molten globules. J. Mol. Biol. 312: 261-273.
    • (2001) J. Mol. Biol. , vol.312 , pp. 261-273
    • Wijesinha-Bettoni, R.1    Dobson, C.M.2    Redfield, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.