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Volumn 53, Issue 7, 2005, Pages 2670-2683

Casein proteins as molecular chaperones

Author keywords

s casein; casein; casein; Milk proteins; Molecular chaperones; Stability of milk proteins

Indexed keywords

ALPHA CRYSTALLIN; ALPHA LACTALBUMIN; BETA LACTOGLOBULIN; CASEIN; CHAPERONE; CLUSTERIN; HEAT SHOCK PROTEIN; INSULIN; MILK PROTEIN;

EID: 16344383300     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf048329h     Document Type: Article
Times cited : (141)

References (59)
  • 2
    • 0002772383 scopus 로고
    • Chemistry of the caseins
    • Proteins; Fox, P. R, Ed.; Elsevier: London
    • Swaisgood, H. E. Chemistry of the caseins. In Advanced Dairy Chemistry-1: Proteins; Fox, P. R, Ed.; Elsevier: London, 1992; p 63-110.
    • (1992) Advanced Dairy Chemistry-1 , pp. 63-110
    • Swaisgood, H.E.1
  • 4
    • 0042306605 scopus 로고    scopus 로고
    • Gelation mechanisms of milk as influenced by temperature and pH; studied by the use of transglutimase cross-linked casein micelles
    • Vasbinder, A. J.; Rollema, H. S.; Bot, A.; de Kruif, C. G. Gelation mechanisms of milk as influenced by temperature and pH; studied by the use of transglutimase cross-linked casein micelles. J. Dairy Sci. 2003, 86, 1556-1563.
    • (2003) J. Dairy Sci. , vol.86 , pp. 1556-1563
    • Vasbinder, A.J.1    Rollema, H.S.2    Bot, A.3    De Kruif, C.G.4
  • 5
    • 0032703108 scopus 로고    scopus 로고
    • s-Casein is required for efficient transport of β- and κ-casein from the endoplasmic reticulum to the Golgi apparatus of mammary epithelial cells
    • s-Casein is required for efficient transport of β- and κ-casein from the endoplasmic reticulum to the Golgi apparatus of mammary epithelial cells. J. Cell Sci. 1999, 112, 3399-3412.
    • (1999) J. Cell Sci. , vol.112 , pp. 3399-3412
    • Chanat, E.1    Martin, P.2    Bousquet, M.-O.3
  • 11
    • 0037596678 scopus 로고    scopus 로고
    • Intracellular protein unfolding and aggregation: The role of small heat-shock chaperone proteins
    • Treweek, T. M.; Morris, A. M.; Carver, J. A. Intracellular protein unfolding and aggregation: The role of small heat-shock chaperone proteins. Aust. J. Chem. 2003, 56, 357-367.
    • (2003) Aust. J. Chem. , vol.56 , pp. 357-367
    • Treweek, T.M.1    Morris, A.M.2    Carver, J.A.3
  • 12
    • 1642528843 scopus 로고    scopus 로고
    • Small heat shock proteins and clusterin: Intra- and extracellular molecular chaperones with a common mechanism of action and function?
    • Carver, J. A.; Rekas, A.; Thorn, D. C.; Wilson, M. R. Small heat shock proteins and clusterin: intra- and extracellular molecular chaperones with a common mechanism of action and function? IUBMB Life, 2003, 55, 661-668.
    • (2003) IUBMB Life , vol.55 , pp. 661-668
    • Carver, J.A.1    Rekas, A.2    Thorn, D.C.3    Wilson, M.R.4
  • 13
    • 0032077156 scopus 로고    scopus 로고
    • Genealogy of the alpha-crystallin-small heat-shock protein superfamily
    • de Jong, W. W.; Gaspers, G. J.; Leunissen, J. A. Genealogy of the alpha-crystallin-small heat-shock protein superfamily. Int. J. Biol. Macromol. 1998, 22, 151-62.
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 151-162
    • De Jong, W.W.1    Gaspers, G.J.2    Leunissen, J.A.3
  • 15
    • 3242804263 scopus 로고    scopus 로고
    • Ability of αs-casein to suppress the heat aggregation of ovotransferrin
    • Matsudomi, N.; Kanda, Y.; Yoshika, Y.; Moriwaki, H. Ability of αs-casein to suppress the heat aggregation of ovotransferrin. J. Agric. Food Chem. 2004, 52, 4882-4886.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 4882-4886
    • Matsudomi, N.1    Kanda, Y.2    Yoshika, Y.3    Moriwaki, H.4
  • 16
    • 0001273048 scopus 로고
    • Colloque INSERM Series; Babney, C., et al., Eds.; John Libbey Eurotext: Montrouge, France
    • Johnson, D. E.; Austin, B. A.; Murphy, R. J. High Pressure and Biotechnology; Colloque INSERM Series; Babney, C., et al., Eds.; John Libbey Eurotext: Montrouge, France; 1992; Vol. 224, pp 243-247.
    • (1992) High Pressure and Biotechnology , vol.224 , pp. 243-247
    • Johnson, D.E.1    Austin, B.A.2    Murphy, R.J.3
  • 17
    • 0026483279 scopus 로고
    • α-crystallin can function as a molecular chaperone
    • Horwitz, J. α-Crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 10449-10453.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 18
    • 0030452980 scopus 로고    scopus 로고
    • Age-related changes in bovine alpha-crystallin and high-molecular-weight protein
    • Carver, J. A.; Nicholls, K. A.; Aquilina, J. A.; Truscott, R. J. W. Age-related changes in bovine alpha-crystallin and high-molecular-weight protein. Exp. Eye Res. 1996, 63, 639-647.
    • (1996) Exp. Eye Res. , vol.63 , pp. 639-647
    • Carver, J.A.1    Nicholls, K.A.2    Aquilina, J.A.3    Truscott, R.J.W.4
  • 21
    • 0027685785 scopus 로고
    • Review and update of casein chemistry
    • Swaisgood, H. E. Review and update of casein chemistry. J. Dairy Sci. 1993, 76, 3054-3061.
    • (1993) J. Dairy Sci. , vol.76 , pp. 3054-3061
    • Swaisgood, H.E.1
  • 24
    • 0036306093 scopus 로고    scopus 로고
    • The interaction of the molecular chaperone α-Crystallin with unfolding α-lactalbumin: A structural and kinetic spectroscopic study
    • Carver, J. A.; Lindner, R. A.; Lyon, C.; Canet, D.; Hernandez, H.; Dobson, C. M.; Redfield, C. The interaction of the molecular chaperone α-Crystallin with unfolding α-lactalbumin: A structural and kinetic spectroscopic study. J. Mol. Biol. 2002, 318, 815-827.
    • (2002) J. Mol. Biol. , vol.318 , pp. 815-827
    • Carver, J.A.1    Lindner, R.A.2    Lyon, C.3    Canet, D.4    Hernandez, H.5    Dobson, C.M.6    Redfield, C.7
  • 26
    • 0023642620 scopus 로고
    • An early intermediate of refolding α-lactalbumin forms within 20 ms
    • Gilmanshin, R. I.; Ptitsyn, O. B. An early intermediate of refolding α-lactalbumin forms within 20 ms. FEBS Lett. 1987, 223, 327-329.
    • (1987) FEBS Lett. , vol.223 , pp. 327-329
    • Gilmanshin, R.I.1    Ptitsyn, O.B.2
  • 27
    • 0024533979 scopus 로고
    • Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea pig α-lactalbumin
    • Baum, J.; Dobson, C. M.; Evans, M. C.; Hanley, C. Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig α-lactalbumin. Biochemistry, 1989, 25, 7-13.
    • (1989) Biochemistry , vol.25 , pp. 7-13
    • Baum, J.1    Dobson, C.M.2    Evans, M.C.3    Hanley, C.4
  • 28
    • 0026774938 scopus 로고
    • Increased exposure of hydrophobic surfaces in molten globule state of á-lactalbumin
    • Lala, A. K.; Kaul, P. Increased exposure of hydrophobic surfaces in molten globule state of á-lactalbumin. J. BM. Chem. 1992, 267, 19914-19918.
    • (1992) J. BM. Chem. , vol.267 , pp. 19914-19918
    • Lala, A.K.1    Kaul, P.2
  • 29
    • 0027536094 scopus 로고
    • Structure and dynamics of the acid-denatured molten globule state of α-lactalbumin: A two-dimensional NMR study
    • Alexandrescu, A. T.; Evans, M. C.; Pitkeathly, M.; Baum, J.; Dobson, C. M. Structure and dynamics of the acid-denatured molten globule state of α-lactalbumin: A two-dimensional NMR study. Biochemistry, 1993, 32, 1707-1718.
    • (1993) Biochemistry , vol.32 , pp. 1707-1718
    • Alexandrescu, A.T.1    Evans, M.C.2    Pitkeathly, M.3    Baum, J.4    Dobson, C.M.5
  • 30
    • 0027280472 scopus 로고
    • Structure and stability of the molten globule state of guineapig α-lactalbumin: A hydrogen exchange study
    • Chyan, C.-L.; Wormald, C.; Dobson, C. M.; Evans, M. C.; Baum, J. Structure and stability of the molten globule state of guineapig α-lactalbumin: A hydrogen exchange study. Biochemistry, 1993, 32, 5681-5691.
    • (1993) Biochemistry , vol.32 , pp. 5681-5691
    • Chyan, C.-L.1    Wormald, C.2    Dobson, C.M.3    Evans, M.C.4    Baum, J.5
  • 31
    • 0028466243 scopus 로고
    • Protein folding. Solid evidence for molten globules
    • Dobson, C. M. Protein folding. Solid evidence for molten globules. Curr. Biol. 1994, 4, 636-640.
    • (1994) Curr. Biol. , vol.4 , pp. 636-640
    • Dobson, C.M.1
  • 32
    • 0030059690 scopus 로고    scopus 로고
    • The molten globule state of α-lactalbumin
    • Kuwajima, K. The molten globule state of α-lactalbumin. FASEB J. 1996, 10, 102-109.
    • (1996) FASEB J. , vol.10 , pp. 102-109
    • Kuwajima, K.1
  • 33
    • 0030783517 scopus 로고    scopus 로고
    • The interaction of the molecular chaperone, α-Crystallin, with molten globule states of bovine α-lactalbumin
    • Lindner, R. A.; Kapur, A.; Carver, J. A. The interaction of the molecular chaperone, α-Crystallin, with molten globule states of bovine α-lactalbumin. J. Biol. Chem. 1997, 272, 27722-27729.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27722-27729
    • Lindner, R.A.1    Kapur, A.2    Carver, J.A.3
  • 34
    • 0032479440 scopus 로고    scopus 로고
    • A specific hydrophobic core in the α-lactalbumin molten globule
    • Wu, L. C.; Kim, P. S. A specific hydrophobic core in the α-lactalbumin molten globule. J. Mol. Biol., 1998, 280, 175-182.
    • (1998) J. Mol. Biol. , vol.280 , pp. 175-182
    • Wu, L.C.1    Kim, P.S.2
  • 35
    • 0032986520 scopus 로고    scopus 로고
    • α-crystallin as a molecular chaperone
    • Derham, B. K.; Harding, J. J. α-Crystallin as a Molecular Chaperone. Prog. Ret. Eye Res. 1999, 18, 463-509.
    • (1999) Prog. Ret. Eye Res. , vol.18 , pp. 463-509
    • Derham, B.K.1    Harding, J.J.2
  • 36
    • 0029124685 scopus 로고
    • Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin
    • Das, B. K.; Surewicz, W. K. Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin. FEBS Lett. 1995, 369, 321-5.
    • (1995) FEBS Lett. , vol.369 , pp. 321-325
    • Das, B.K.1    Surewicz, W.K.2
  • 37
    • 0028811494 scopus 로고
    • Membrane-protein interaction and the molten globule state: Interaction of alpha-lactalbumin with membranes
    • Lala, A. K.; Kaul, P.; Ratnam, P. B. Membrane-protein interaction and the molten globule state: interaction of alpha-lactalbumin with membranes. J. Protein Chem. 1995, 14, 601-609.
    • (1995) J. Protein Chem. , vol.14 , pp. 601-609
    • Lala, A.K.1    Kaul, P.2    Ratnam, P.B.3
  • 38
    • 0032575656 scopus 로고    scopus 로고
    • The chaperone-like a-crystallin forms a complex only with the aggregation-prone molten globule state of α-lactalbumin
    • Rajaraman, K.; Raman, B.; Ramakrishna, T.; Rao, C. M. The chaperone-like a-crystallin forms a complex only with the aggregation-prone molten globule state of α-lactalbumin. Biochem. Biophys. Res. Comm. 1998, 249, 917-921.
    • (1998) Biochem. Biophys. Res. Comm. , vol.249 , pp. 917-921
    • Rajaraman, K.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 39
    • 0036516861 scopus 로고    scopus 로고
    • Molten globule structures in milk proteins: Implications for potential new structure-function relationships
    • Farrell, J. H. M.; Qi, P. X.; Brown, E. M.; Cooke, P. H.; Tunick, M. H.; Wickham, E. D.; Unruh, J. J. Molten globule structures in milk proteins: implications for potential new structure-function relationships. J Dairy Sci 2002, 85, 459-471.
    • (2002) J. Dairy Sci. , vol.85 , pp. 459-471
    • Farrell, J.H.M.1    Qi, P.X.2    Brown, E.M.3    Cooke, P.H.4    Tunick, M.H.5    Wickham, E.D.6    Unruh, J.J.7
  • 40
    • 0029034730 scopus 로고
    • Temperature dependent chaperone-like activity of alpha-crystallin
    • Raman, B.; Ramakrishna, T.; Rao, C. M. Temperature dependent chaperone-like activity of alpha-crystallin. FEBS Lett. 1995, 365, 133-136.
    • (1995) FEBS Lett. , vol.365 , pp. 133-136
    • Raman, B.1    Ramakrishna, T.2    Rao, C.M.3
  • 41
    • 0027973129 scopus 로고
    • Chaperone-like activity and quaternary structure of alpha-crystallin
    • Raman, B.; Rao, C. M. Chaperone-like activity and quaternary structure of alpha-crystallin. J. Biol. Chem. 1994, 269, 27264-27268.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27264-27268
    • Raman, B.1    Rao, C.M.2
  • 42
    • 0027008444 scopus 로고
    • 1H NMR assignments and local environments of aromatic residues in bovine, human and guinea pig variants of alpha-lactalbumin
    • Alexandrescu, A. T.; Broadhurst, R. W.; Wormald, C.; Chyan, C.-L.; Baum, J.; Dobson, C. M. 1H NMR assignments and local environments of aromatic residues in bovine, human and guinea pig variants of alpha-lactalbumin. Eur. J. Biochem. 1992, 210, 699-709.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 699-709
    • Alexandrescu, A.T.1    Broadhurst, R.W.2    Wormald, C.3    Chyan, C.-L.4    Baum, J.5    Dobson, C.M.6
  • 43
    • 78651138927 scopus 로고
    • The interaction between polysaccharides and other macromolecules 5: The solubility of proteins in the presence of dextran
    • Laurent, T. C. The interaction between polysaccharides and other macromolecules 5: The solubility of proteins in the presence of dextran. Biochem. J. 1963, 59, 253-257.
    • (1963) Biochem. J. , vol.59 , pp. 253-257
    • Laurent, T.C.1
  • 44
    • 0000295322 scopus 로고    scopus 로고
    • Kinetics of heat-induced aggregation of β-lactoglobulin
    • Verheul, M.; Roefs, S. P. F. M.; de Kruif, K. G. Kinetics of heat-induced aggregation of β-lactoglobulin. J. Agric. Food Chem. 1998, 46, 896-903.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 896-903
    • Verheul, M.1    Roefs, S.P.F.M.2    De Kruif, K.G.3
  • 46
    • 0034719136 scopus 로고    scopus 로고
    • Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state
    • Poon, S.; Easterbrook-Smith, S. B.; Rybchyn, M. S.; Carver, J. A.; Wilson, M. R. Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state. Biochemistry, 2000, 39, 15953-15960.
    • (2000) Biochemistry , vol.39 , pp. 15953-15960
    • Poon, S.1    Easterbrook-Smith, S.B.2    Rybchyn, M.S.3    Carver, J.A.4    Wilson, M.R.5
  • 47
    • 0000008542 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin: Role of the free thiol group and disulfide bonds
    • Hoffmann, M. A. M.; van Mil, P. J. J. M. Heat-induced aggregation of β-lactoglobulin: Role of the free thiol group and disulfide bonds. J. Agric. Food Chem. 1997, 45, 2942-2948.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 2942-2948
    • Hoffmann, M.A.M.1    Van Mil, P.J.J.M.2
  • 48
    • 0037181142 scopus 로고    scopus 로고
    • Clusterin is an extracellular chaperone that specifically interacts with slowly aggregating proteins on their off-folding pathway
    • Poon, S.; Treweek, T. M.; Wilson, M. R.; Easterbrook-Smith, S. B.; Carver, J. A. Clusterin is an extracellular chaperone that specifically interacts with slowly aggregating proteins on their off-folding pathway. FEBS Lett. 2002, 513, 259-266.
    • (2002) FEBS Lett. , vol.513 , pp. 259-266
    • Poon, S.1    Treweek, T.M.2    Wilson, M.R.3    Easterbrook-Smith, S.B.4    Carver, J.A.5
  • 51
    • 0032078725 scopus 로고    scopus 로고
    • Environmental factors influencing the chaperone-like activity of alpha-crystallin
    • Koretz, J. F.; Doss, E. W.; LaButti, J. N. Environmental factors influencing the chaperone-like activity of alpha-crystallin. Int. J. Biol. Macromol. 1998, 22, 283-294.
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 283-294
    • Koretz, J.F.1    Doss, E.W.2    LaButti, J.N.3
  • 53
    • 1542467586 scopus 로고    scopus 로고
    • The selective inhibition of serpin aggregation by the molecular chaperone, α-Crystallin, indicates a nucleation-dependent specificity
    • Devlin, G. L.; Carver, J. A.; Bottomley, S. P. The selective inhibition of serpin aggregation by the molecular chaperone, α-Crystallin, indicates a nucleation-dependent specificity. J. Biol. Chem. 2003, 278, 48644-48650.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48644-48650
    • Devlin, G.L.1    Carver, J.A.2    Bottomley, S.P.3
  • 54
    • 0035865589 scopus 로고    scopus 로고
    • The molecular chaperone alpha-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin
    • Lindner, R. A.; Treweek, T. M.; Carver, J. A. The molecular chaperone alpha-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin. Biochem. J. 2001, 354, 79-87.
    • (2001) Biochem. J. , vol.354 , pp. 79-87
    • Lindner, R.A.1    Treweek, T.M.2    Carver, J.A.3
  • 56
    • 0036402632 scopus 로고    scopus 로고
    • C-terminal lysine truncation increases thermostability and enhances chaperone-like function of porcine αB-Crystallin
    • Liao, J.-H.; Lee, J.-S.; Chiou, S.-H. C-terminal lysine truncation increases thermostability and enhances chaperone-like function of porcine αB-Crystallin. Biochem. Biophys. Res. Comm. 2002, 297, 309-316.
    • (2002) Biochem. Biophys. Res. Comm. , vol.297 , pp. 309-316
    • Liao, J.-H.1    Lee, J.-S.2    Chiou, S.-H.3


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