메뉴 건너뛰기




Volumn 277, Issue 1, 2010, Pages 163-173

The oleic acid complexes of proteolytic fragments of α-lactalbumin display apoptotic activity

Author keywords

lactalbumin; Apoptosis; HAMLET; Oleic acid; Protein fragments

Indexed keywords

ALPHA LACTALBUMIN; BOVINE ALPHA LACTALBUMIN; FATTY ACID; HUMAN ALPHA LACTALBUMIN; OLEIC ACID; UNCLASSIFIED DRUG;

EID: 73649141377     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2009.07466.x     Document Type: Article
Times cited : (63)

References (61)
  • 1
    • 0016649099 scopus 로고
    • Lactose synthetase
    • Hill RL Brew K (1975) Lactose synthetase. Adv Enzymol 43, 411 490.
    • (1975) Adv Enzymol , vol.43 , pp. 411-490
    • Hill, R.L.1    Brew, K.2
  • 2
    • 0030059690 scopus 로고    scopus 로고
    • The molten globule state of α-lactalbumin
    • Kuwajima K (1996) The molten globule state of α-lactalbumin. FASEB J 10, 102 109.
    • (1996) FASEB J , vol.10 , pp. 102-109
    • Kuwajima, K.1
  • 3
    • 0029157429 scopus 로고
    • Compact intermediate states in protein folding
    • Fink AL (1995) Compact intermediate states in protein folding. Annu Rev Biophys Biomol Struct 24, 495 522.
    • (1995) Annu Rev Biophys Biomol Struct , vol.24 , pp. 495-522
    • Fink, A.L.1
  • 4
    • 0030585408 scopus 로고    scopus 로고
    • Crystal structures of guinea-pig, goat and bovine alpha-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase
    • Pike AC, Brew K Acharya KR (1996) Crystal structures of guinea-pig, goat and bovine alpha-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase. Structure 4, 691 703.
    • (1996) Structure , vol.4 , pp. 691-703
    • Pike, A.C.1    Brew, K.2    Acharya, K.R.3
  • 5
    • 0034685838 scopus 로고    scopus 로고
    • Alpha-lactalbumin: Structure and function
    • Permyakov EA Berliner LJ (2000) Alpha-lactalbumin: structure and function. FEBS Lett 473, 269 274.
    • (2000) FEBS Lett , vol.473 , pp. 269-274
    • Permyakov, E.A.1    Berliner, L.J.2
  • 7
    • 0027536094 scopus 로고
    • Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: A two-dimensional NMR study
    • Alexandrescu AT, Evans PA, Pitkeathly M, Baum J Dobson CM (1993) Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study. Biochemistry 32, 1707 1718.
    • (1993) Biochemistry , vol.32 , pp. 1707-1718
    • Alexandrescu, A.T.1    Evans, P.A.2    Pitkeathly, M.3    Baum, J.4    Dobson, C.M.5
  • 8
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn OB (1995) Molten globule and protein folding. Adv Protein Chem 47, 83 229.
    • (1995) Adv Protein Chem , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 10
    • 0029591840 scopus 로고
    • Binding of molten globule-like conformations to lipid bilayers. Structure of native and partially folded alpha-lactalbumin bound to model membranes
    • Bañuelos S Muga A (1995) Binding of molten globule-like conformations to lipid bilayers. Structure of native and partially folded alpha-lactalbumin bound to model membranes. J Biol Chem 270, 29910 29915.
    • (1995) J Biol Chem , vol.270 , pp. 29910-29915
    • Bañuelos, S.1    Muga, A.2
  • 11
    • 0030014802 scopus 로고    scopus 로고
    • Membrane-bound states of alpha-lactalbumin: Implications for the protein stability and conformation
    • Cawthern KM, Permyakov E Berliner LJ (1996) Membrane-bound states of alpha-lactalbumin: implications for the protein stability and conformation. Protein Sci 5, 1394 1405.
    • (1996) Protein Sci , vol.5 , pp. 1394-1405
    • Cawthern, K.M.1    Permyakov, E.2    Berliner, L.J.3
  • 14
    • 0037821763 scopus 로고    scopus 로고
    • The interaction of peripheral proteins and membranes studied with α-lactalbumin and phospholipid bilayers of various compositions
    • Agasøster AV, Halskau O, Fuglebakk E, Frøystein NA, Muga A, Holmsen H Martinez A (2003) The interaction of peripheral proteins and membranes studied with α-lactalbumin and phospholipid bilayers of various compositions. J Biol Chem 278, 21790 21797.
    • (2003) J Biol Chem , vol.278 , pp. 21790-21797
    • Agasøster, A.V.1    Halskau, O.2    Fuglebakk, E.3    Frøystein, N.A.4    Muga, A.5    Holmsen, H.6    Martinez, A.7
  • 19
    • 0344201898 scopus 로고    scopus 로고
    • Lipids as cofactors in protein folding: Stereo-specific lipid-protein interactions are required to form HAMLET (human alpha-lactalbumin made lethal to tumor cells)
    • Svensson M, Mossberg AK, Pettersson J, Linse S Svanborg C (2003) Lipids as cofactors in protein folding: stereo-specific lipid-protein interactions are required to form HAMLET (human alpha-lactalbumin made lethal to tumor cells). Protein Sci 12, 2805 2814.
    • (2003) Protein Sci , vol.12 , pp. 2805-2814
    • Svensson, M.1    Mossberg, A.K.2    Pettersson, J.3    Linse, S.4    Svanborg, C.5
  • 21
    • 10744223979 scopus 로고    scopus 로고
    • α-Lactalbumin unfolding is not sufficient to cause apoptosis, but is required for the conversion to HAMLET (human alpha-lactalbumin made lethal to tumor cells)
    • Svensson M, Fast J, Mossberg AK, Duringer C, Gustafsson L, Hallgren O, Brooks CL, Berliner L, Linse S Svanborg C (2003) α-Lactalbumin unfolding is not sufficient to cause apoptosis, but is required for the conversion to HAMLET (human alpha-lactalbumin made lethal to tumor cells). Protein Sci 12, 2794 2804.
    • (2003) Protein Sci , vol.12 , pp. 2794-2804
    • Svensson, M.1    Fast, J.2    Mossberg, A.K.3    Duringer, C.4    Gustafsson, L.5    Hallgren, O.6    Brooks, C.L.7    Berliner, L.8    Linse, S.9    Svanborg, C.10
  • 22
    • 0025356254 scopus 로고
    • The complete digestion of human milk triacylglycerol in vitro requires gastric lipase, pancreatic colipase-dependent lipase and bile salt-stimulated lipase
    • Bernback S, Blackberg L Hernell O (1990) The complete digestion of human milk triacylglycerol in vitro requires gastric lipase, pancreatic colipase-dependent lipase and bile salt-stimulated lipase. J Clin Invest 85, 1221 1226.
    • (1990) J Clin Invest , vol.85 , pp. 1221-1226
    • Bernback, S.1    Blackberg, L.2    Hernell, O.3
  • 23
    • 0026635385 scopus 로고
    • Human gastric lipase: Ontogeny and variations in children
    • Sarles J, Moreau H Verger R (1992) Human gastric lipase: ontogeny and variations in children. Acta Paediatr 81, 511 513.
    • (1992) Acta Paediatr , vol.81 , pp. 511-513
    • Sarles, J.1    Moreau, H.2    Verger, R.3
  • 24
    • 33646386189 scopus 로고    scopus 로고
    • α-Lactalbumin species variation, HAMLET formation and tumor cell death
    • Pettersson J, Mossberg AK Svanborg C (2006) α-Lactalbumin species variation, HAMLET formation and tumor cell death. Biochem Biophys Res Commun 345, 260 270.
    • (2006) Biochem Biophys Res Commun , vol.345 , pp. 260-270
    • Pettersson, J.1    Mossberg, A.K.2    Svanborg, C.3
  • 29
    • 2442575245 scopus 로고    scopus 로고
    • No need to be HAMLET or BAMLET to interact with histones: Binding of monomeric alpha-lactalbumin to histones and basic poly-amino acids
    • Permyakov SE, Pershikova IV, Khokhlova TI, Uversky VN Permyakov EA. (2004) No need to be HAMLET or BAMLET to interact with histones: binding of monomeric alpha-lactalbumin to histones and basic poly-amino acids. Biochemistry 43, 5575 5582.
    • (2004) Biochemistry , vol.43 , pp. 5575-5582
    • Permyakov, S.E.1    Pershikova, I.V.2    Khokhlova, T.I.3    Uversky, V.N.4    Permyakov, E.A.5
  • 30
    • 17444365482 scopus 로고    scopus 로고
    • Conversion of human alpha-lactalbumin to an apo-like state in the complexes with basic poly-amino acids: Toward understanding of the molecular mechanism of antitumor action of HAMLET
    • Permyakov SE, Pershikova IV, Zhadan AP, Goers J, Bakunts AG, Uversky VN, Berliner LJ Permyakov EA (2005) Conversion of human alpha-lactalbumin to an apo-like state in the complexes with basic poly-amino acids: toward understanding of the molecular mechanism of antitumor action of HAMLET. J Proteome Res 4, 564 569.
    • (2005) J Proteome Res , vol.4 , pp. 564-569
    • Permyakov, S.E.1    Pershikova, I.V.2    Zhadan, A.P.3    Goers, J.4    Bakunts, A.G.5    Uversky, V.N.6    Berliner, L.J.7    Permyakov, E.A.8
  • 32
    • 0034826545 scopus 로고    scopus 로고
    • Stepwise proteolytic removal of the β-subdomain in α-lactalbumin: The protein remains folded and can form the molten globule in acid solution
    • Polverino de Laureto P, Vinante D, Scaramella E, Frare E Fontana A (2001) Stepwise proteolytic removal of the β-subdomain in α-lactalbumin: the protein remains folded and can form the molten globule in acid solution. Eur J Biochem 286, 4324 4333.
    • (2001) Eur J Biochem , vol.286 , pp. 4324-4333
    • Polverino De Laureto, P.1    Vinante, D.2    Scaramella, E.3    Frare, E.4    Fontana, A.5
  • 33
    • 4243164468 scopus 로고    scopus 로고
    • Comparative toxicity of oleic acid and linoleic acid on Jurkat cells
    • Cury-Boaventura MF, Pompéia C Curi R (2004) Comparative toxicity of oleic acid and linoleic acid on Jurkat cells. Clin Nutr 23, 721 732.
    • (2004) Clin Nutr , vol.23 , pp. 721-732
    • Cury-Boaventura, M.F.1    Pompéia, C.2    Curi, R.3
  • 34
    • 13244274907 scopus 로고    scopus 로고
    • Stability of HAMLET - A kinetically trapped alpha-lactalbumin oleic acid complex
    • Fast J, Mossberg AK, Svanborg C Linse S (2005) Stability of HAMLET - a kinetically trapped alpha-lactalbumin oleic acid complex. Protein Sci 14, 329 340.
    • (2005) Protein Sci , vol.14 , pp. 329-340
    • Fast, J.1    Mossberg, A.K.2    Svanborg, C.3    Linse, S.4
  • 35
    • 0037110569 scopus 로고    scopus 로고
    • Molten globule of bovine α-lactalbumin at neutral pH induced by heat, trifluoroethanol and oleic acid: A comparative analysis by circular dichroism spectroscopy and limited proteolysis
    • Polverino de Laureto P, Frare E, Gottardo R Fontana A (2002) Molten globule of bovine α-lactalbumin at neutral pH induced by heat, trifluoroethanol and oleic acid: a comparative analysis by circular dichroism spectroscopy and limited proteolysis. Proteins 49, 385 397.
    • (2002) Proteins , vol.49 , pp. 385-397
    • Polverino De Laureto, P.1    Frare, E.2    Gottardo, R.3    Fontana, A.4
  • 36
    • 33747773827 scopus 로고    scopus 로고
    • Structural changes of α-lactalbumin induced by low pH and oleic acid
    • Yang F Jr., Zhang M, Chen J Liang Y (2006) Structural changes of α-lactalbumin induced by low pH and oleic acid. Biochim Biophys Acta 1764, 1389 1396.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1389-1396
    • Yang Jr., F.1    Zhang, M.2    Chen, J.3    Liang, Y.4
  • 37
    • 67349213968 scopus 로고    scopus 로고
    • Cytotoxic aggregates of alpha-lactalbumin induced by unsaturated fatty acid induce apoptosis in tumor cells
    • Zhang M, Yang F Jr., Yang F, Chen J, Zheng CY Liang Y (2009) Cytotoxic aggregates of alpha-lactalbumin induced by unsaturated fatty acid induce apoptosis in tumor cells. Chem Biol Interact 180, 131 142.
    • (2009) Chem Biol Interact , vol.180 , pp. 131-142
    • Zhang, M.1    Yang Jr., F.2    Yang, F.3    Chen, J.4    Zheng, C.Y.5    Liang, Y.6
  • 38
    • 0028959773 scopus 로고
    • Circular dichroism
    • Woody RW (1995) Circular dichroism. Methods Enzymol 246, 34 71.
    • (1995) Methods Enzymol , vol.246 , pp. 34-71
    • Woody, R.W.1
  • 39
    • 0024294298 scopus 로고
    • Ionization and phase behavior of fatty acids in water: Application of Gibbs phase rule
    • Cistola DP, Hamilton J, Jackson D Small D (1988) Ionization and phase behavior of fatty acids in water: application of Gibbs phase rule. Biochemistry 27, 1881 1888.
    • (1988) Biochemistry , vol.27 , pp. 1881-1888
    • Cistola, D.P.1    Hamilton, J.2    Jackson, D.3    Small, D.4
  • 40
    • 0000984395 scopus 로고
    • Aggregate structure in dilute aqueous dispersions of oleic acid/sodium oleate and oleic acid/sodium oleate/egg phosphatidylcholine
    • Edwards K, Silvander M Karlsson G (1995) Aggregate structure in dilute aqueous dispersions of oleic acid/sodium oleate and oleic acid/sodium oleate/egg phosphatidylcholine. Langmuir 11, 2429 2434.
    • (1995) Langmuir , vol.11 , pp. 2429-2434
    • Edwards, K.1    Silvander, M.2    Karlsson, G.3
  • 41
    • 33644631179 scopus 로고    scopus 로고
    • Kinetic studies of the interaction of fatty acids with phosphatidylcholine vesicles (liposomes)
    • Rogerson ML, Robinson BH, Bucak S Walde P (2006) Kinetic studies of the interaction of fatty acids with phosphatidylcholine vesicles (liposomes). Colloids Surf B Biointerfaces 48, 24 34.
    • (2006) Colloids Surf B Biointerfaces , vol.48 , pp. 24-34
    • Rogerson, M.L.1    Robinson, B.H.2    Bucak, S.3    Walde, P.4
  • 43
    • 0026688017 scopus 로고
    • Critical micellar concentrations of palmitoyl dihydroxyacetone phosphate and 1-palmitoyl-rac-glycerol 3-phosphate
    • Das AK Hajra AK (1992) Critical micellar concentrations of palmitoyl dihydroxyacetone phosphate and 1-palmitoyl-rac-glycerol 3-phosphate. J Biol Chem 267, 9731 9737.
    • (1992) J Biol Chem , vol.267 , pp. 9731-9737
    • Das, A.K.1    Hajra, A.K.2
  • 44
    • 22444442888 scopus 로고    scopus 로고
    • From decanoate micelles to decanoic acid/dodecylbenzenesulfonate vesicles
    • Namani T Walde P (2005) From decanoate micelles to decanoic acid/dodecylbenzenesulfonate vesicles. Langmuir 21, 6210 6219.
    • (2005) Langmuir , vol.21 , pp. 6210-6219
    • Namani, T.1    Walde, P.2
  • 45
    • 0032872786 scopus 로고    scopus 로고
    • Amphitropic proteins: Regulation by reversible membrane interactions
    • Johnson JE Cornell RB (1999) Amphitropic proteins: regulation by reversible membrane interactions. Mol Membr Biol 16, 217 235.
    • (1999) Mol Membr Biol , vol.16 , pp. 217-235
    • Johnson, J.E.1    Cornell, R.B.2
  • 46
    • 33845350971 scopus 로고    scopus 로고
    • Amphipathic helices as mediators of the membrane interaction of amphitropic proteins, and as modulators of bilayer physical properties
    • Cornell RB Taneva SG (2006) Amphipathic helices as mediators of the membrane interaction of amphitropic proteins, and as modulators of bilayer physical properties. Curr Protein Pept Sci 7, 539 552.
    • (2006) Curr Protein Pept Sci , vol.7 , pp. 539-552
    • Cornell, R.B.1    Taneva, S.G.2
  • 47
    • 26644444070 scopus 로고    scopus 로고
    • How lipids and proteins interact in a membrane: A molecular approach
    • Lee GA (2005) How lipids and proteins interact in a membrane: a molecular approach. Mol Biosyst 1, 203 212.
    • (2005) Mol Biosyst , vol.1 , pp. 203-212
    • Lee, G.A.1
  • 48
    • 0345306656 scopus 로고    scopus 로고
    • Rapid Anionic Micelle-mediated α-Synuclein Fibrillization in Vitro
    • DOI 10.1074/jbc.M308231200
    • Necula M, Chirita CN Kuret J (2003) Rapid anionic micelle-mediated alpha-synuclein fibrillization in vitro. J Biol Chem 278, 46674 46680. (Pubitemid 37452245)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 46674-46680
    • Necula, M.1    Chirita, C.N.2    Kuret, J.3
  • 49
    • 0038152836 scopus 로고    scopus 로고
    • Anionic micelles and vesicles induce tau fibrillization in vitro
    • Chirita C, Necula M Kuret J (2003) Anionic micelles and vesicles induce tau fibrillization in vitro. J Biol Chem 278, 25644 25650.
    • (2003) J Biol Chem , vol.278 , pp. 25644-25650
    • Chirita, C.1    Necula, M.2    Kuret, J.3
  • 50
    • 33744982084 scopus 로고    scopus 로고
    • Lysozyme effect on oleic acid/oleate vesicles
    • Ruiz-Mirazo K, Stano P Luisi PL (2006) Lysozyme effect on oleic acid/oleate vesicles. J Liposome Res 16, 143 154.
    • (2006) J Liposome Res , vol.16 , pp. 143-154
    • Ruiz-Mirazo, K.1    Stano, P.2    Luisi, P.L.3
  • 51
    • 0035970302 scopus 로고    scopus 로고
    • Comparison of the structural and dynamical properties of holo and apo bovine alpha-lactalbumin by NMR spectroscopy
    • Wijesinha-Bettoni R, Dobson CM Redfield C (2001) Comparison of the structural and dynamical properties of holo and apo bovine alpha-lactalbumin by NMR spectroscopy. J Mol Biol 307, 885 898.
    • (2001) J Mol Biol , vol.307 , pp. 885-898
    • Wijesinha-Bettoni, R.1    Dobson, C.M.2    Redfield, C.3
  • 52
    • 0034711229 scopus 로고    scopus 로고
    • Crystal structures of apo- and holo-bovine alpha-lactalbumin at 2.2-Å resolution reveal an effect of calcium on inter-lobe interactions
    • Chrysina ED, Brew K Acharya KR (2000) Crystal structures of apo- and holo-bovine alpha-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
  • 54
    • 0033022708 scopus 로고    scopus 로고
    • Isolation and identification of three bactericidal domains in the bovine alpha-lactalbumin molecule
    • Pellegrini A, Thomas U, Bramaz N, Hunziker P von Fellenberg R (1999) Isolation and identification of three bactericidal domains in the bovine alpha-lactalbumin molecule. Biochim Biophys Acta 1426, 439 448.
    • (1999) Biochim Biophys Acta , vol.1426 , pp. 439-448
    • Pellegrini, A.1    Thomas, U.2    Bramaz, N.3    Hunziker, P.4    Von Fellenberg, R.5
  • 55
    • 70450224072 scopus 로고    scopus 로고
    • Alpha-Lactalbumin, engineered to be nonnative and inactive, kills tumor cells when in complex with oleic acid: A new biological function resulting from partial unfolding
    • doi
    • Pettersson-Kastberg J, Mossberg AK, Trulsson M, Yong YJ, Min S, Lim Y, O'Brien JE, Svanborg C Mok KH (2009) Alpha-Lactalbumin, engineered to be nonnative and inactive, kills tumor cells when in complex with oleic acid: a new biological function resulting from partial unfolding. J Mol Biol doi
    • (2009) J Mol Biol
    • Pettersson-Kastberg, J.1    Mossberg, A.K.2    Trulsson, M.3    Yong, Y.J.4    Min, S.5    Lim, Y.6    O'Brien, J.E.7    Svanborg, C.8    Mok, K.H.9
  • 58
    • 0035701464 scopus 로고    scopus 로고
    • Growth rates of a human colon adenocarcinoma cell line are regulated by the milk protein alpha-lactalbumin
    • Sternhagen LG Allen JC (2001) Growth rates of a human colon adenocarcinoma cell line are regulated by the milk protein alpha-lactalbumin. Adv Exp Med Biol 501, 115 120.
    • (2001) Adv Exp Med Biol , vol.501 , pp. 115-120
    • Sternhagen, L.G.1    Allen, J.C.2
  • 59
    • 22444439370 scopus 로고    scopus 로고
    • IEC-6 intestinal cell death induced by bovine milk alpha-lactalbumin
    • Xu M, Sugiura Y, Nagaoka S Kanamaru Y (2005) IEC-6 intestinal cell death induced by bovine milk alpha-lactalbumin. Biosci Biotechnol Biochem 69, 1082 1089.
    • (2005) Biosci Biotechnol Biochem , vol.69 , pp. 1082-1089
    • Xu, M.1    Sugiura, Y.2    Nagaoka, S.3    Kanamaru, Y.4
  • 60
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SG von Hippel PH (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182, 319 326.
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.G.1    Von Hippel, P.H.2
  • 61
    • 15444343013 scopus 로고
    • A comparison between 8-anilinonaphthalene-1-sulfonate and 2-p-toluidinylnaphthalene-6-sulfonate as fluorescent indicators of the critical micelle concentration of sodium dodecyl sulfate
    • Horowitz P (1977) A comparison between 8-anilinonaphthalene-1-sulfonate and 2-p-toluidinylnaphthalene-6-sulfonate as fluorescent indicators of the critical micelle concentration of sodium dodecyl sulfate. J Colloid Interface Sci 61, 197 198.
    • (1977) J Colloid Interface Sci , vol.61 , pp. 197-198
    • Horowitz, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.