메뉴 건너뛰기




Volumn 416, Issue 1, 2008, Pages 145-152

Effects of phosphatidylethanolamine glycation on lipid-protein interactions and membrane protein thermal stability

Author keywords

Membrane protein; Non enzymatic glycation; Phospholipid; Plasma membrane Ca2+ ATPase; Protein lipid interaction

Indexed keywords

DIFFERENT SIZES; GLYCATION; IN-VIVO; LIPID-PROTEIN INTERACTIONS; MEMBRANE LIPIDS; MEMBRANE PROTEIN; MEMBRANE PROTEINS; NON-ENZYMATIC; NON-ENZYMATIC GLYCATION; PATHOPHYSIOLOGY; PHOSPHATIDYLETHANOLAMINE; PLASMA MEMBRANE CA2+ - ATPASE; PROTEIN-LIPID INTERACTION; STRUCTURAL REARRANGEMENT; THERMAL DENATURATIONS; THERMAL UNFOLDING; TRANSMEMBRANE;

EID: 56049106110     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20080618     Document Type: Article
Times cited : (33)

References (42)
  • 1
    • 0000916315 scopus 로고
    • Action des acides aminés sur les sucres: Formation des melanoidines par voie methodique.
    • Maillard, L. C. (1912) Action des acides aminés sur les sucres: formation des melanoidines par voie methodique. Compt. Rend. Hebd. Seances Acad. Sci. 154, 66-68
    • (1912) Compt. Rend. Hebd. Seances Acad. Sci , vol.154 , pp. 66-68
    • Maillard, L.C.1
  • 2
    • 34347327190 scopus 로고    scopus 로고
    • The road to advanced glycation end products: A mechanistic perspective
    • Cho, S. J., Roman, G., Yeboah, F. and Konishi, Y. (2007) The road to advanced glycation end products: a mechanistic perspective. Curr. Med. Chem. 14, 1653-1671
    • (2007) Curr. Med. Chem , vol.14 , pp. 1653-1671
    • Cho, S.J.1    Roman, G.2    Yeboah, F.3    Konishi, Y.4
  • 3
    • 33646377677 scopus 로고    scopus 로고
    • Creating proteins with novel functionality via the Maillard reaction: A review
    • Oliver, C. M., Melton, L. D. and Stanley, R. A. (2006) Creating proteins with novel functionality via the Maillard reaction: A review. Crit. Rev. Food Sci. Nutr. 46, 337-350
    • (2006) Crit. Rev. Food Sci. Nutr , vol.46 , pp. 337-350
    • Oliver, C.M.1    Melton, L.D.2    Stanley, R.A.3
  • 4
    • 0035787070 scopus 로고    scopus 로고
    • Protein glycation, diabetes, and aging
    • Ulrich, P. and Cerami, A. (2001) Protein glycation, diabetes, and aging. Recent Prog. Horm. Res. 56, 1-21
    • (2001) Recent Prog. Horm. Res , vol.56 , pp. 1-21
    • Ulrich, P.1    Cerami, A.2
  • 6
    • 27444441208 scopus 로고    scopus 로고
    • Ion-trap tandem mass spectrometric analysis of Amadori-glycated phosphatidylethanolamine in human plasma with or without diabetes
    • Nakagawa, K., Oak, J. H., Higuchi, O., Tsuzuki, T., Oikawa, S., Otani, H., Mune, M., Cai, H. and Miyazawa, T. (2005) Ion-trap tandem mass spectrometric analysis of Amadori-glycated phosphatidylethanolamine in human plasma with or without diabetes. J. Lipid Res. 46, 2514-2524
    • (2005) J. Lipid Res , vol.46 , pp. 2514-2524
    • Nakagawa, K.1    Oak, J.H.2    Higuchi, O.3    Tsuzuki, T.4    Oikawa, S.5    Otani, H.6    Mune, M.7    Cai, H.8    Miyazawa, T.9
  • 7
    • 0034622668 scopus 로고    scopus 로고
    • Synthetically prepared Amadori-glycated phosphatidylethanolamine can trigger lipid peroxidation via free radical reactions
    • Oak, J., Nakagawa, K. and Miyazawa, T. (2000) Synthetically prepared Amadori-glycated phosphatidylethanolamine can trigger lipid peroxidation via free radical reactions. FEBS Lett. 481, 26-30
    • (2000) FEBS Lett , vol.481 , pp. 26-30
    • Oak, J.1    Nakagawa, K.2    Miyazawa, T.3
  • 8
    • 33646771683 scopus 로고    scopus 로고
    • Aminophospholipid glycation and its inhibitor screening system: A new role of pyridoxal 5′-phosphate as the inhibitor
    • Higuchi, O., Nakagawa, K., Tsuzuki, T., Suzuki, T., Oikawa, S. and Miyazawa, T. (2006) Aminophospholipid glycation and its inhibitor screening system: a new role of pyridoxal 5′-phosphate as the inhibitor. J. Lipid Res. 47, 964-974
    • (2006) J. Lipid Res , vol.47 , pp. 964-974
    • Higuchi, O.1    Nakagawa, K.2    Tsuzuki, T.3    Suzuki, T.4    Oikawa, S.5    Miyazawa, T.6
  • 9
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer, S. J. and Nicolson, G. L. (1972) The fluid mosaic model of the structure of cell membranes. Science 175, 720-731
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 10
    • 33749046710 scopus 로고    scopus 로고
    • To see or not to see: Lateral organization of biological membranes and fluorescence microscopy
    • Bagatolli, L. A. (2006) To see or not to see: lateral organization of biological membranes and fluorescence microscopy. Biochim. Biophys. Acta 1758, 1541-1556
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1541-1556
    • Bagatolli, L.A.1
  • 11
    • 28444437064 scopus 로고    scopus 로고
    • Membranes are more mosaic than fluid
    • Engelman, D. M. (2005) Membranes are more mosaic than fluid. Nature 438, 578-580
    • (2005) Nature , vol.438 , pp. 578-580
    • Engelman, D.M.1
  • 13
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White, S. H. and Wimley, W. C. (1999) Membrane protein folding and stability: physical principles. Annu. Rev. Biophys. Biomol. Struct. 28, 319-365
    • (1999) Annu. Rev. Biophys. Biomol. Struct , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 14
    • 45449105164 scopus 로고    scopus 로고
    • Protein modulation of lipids, and vice-versa, in membranes
    • Marsh, D. (2008) Protein modulation of lipids, and vice-versa, in membranes. Biochim. Biophys. Acta 1778, 1545-1575
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1545-1575
    • Marsh, D.1
  • 16
    • 0034142076 scopus 로고    scopus 로고
    • Thermal stability of the plasma membrane calcium pump. Quantitative analysis of its dependence on lipid-protein interactions
    • Levi, V., Rossi, J. P., Echarte, M. M., Castello, P. R. and González Flecha, F. L. (2000) Thermal stability of the plasma membrane calcium pump. Quantitative analysis of its dependence on lipid-protein interactions. J. Membr. Biol. 173, 215-225
    • (2000) J. Membr. Biol , vol.173 , pp. 215-225
    • Levi, V.1    Rossi, J.P.2    Echarte, M.M.3    Castello, P.R.4    González Flecha, F.L.5
  • 18
    • 0027325597 scopus 로고
    • The erythrocyte calcium pump is inhibited by non-enzymic glycation: Studies in situ and with the purified enzyme
    • González Flecha, F. L., Castello, P. R., Caride, A. J., Gagliardino, J. J. and Rossi, J. P. (1993) The erythrocyte calcium pump is inhibited by non-enzymic glycation: studies in situ and with the purified enzyme. Biochem. J. 293, 369-375
    • (1993) Biochem. J , vol.293 , pp. 369-375
    • González Flecha, F.L.1    Castello, P.R.2    Caride, A.J.3    Gagliardino, J.J.4    Rossi, J.P.5
  • 20
    • 0025270741 scopus 로고
    • Peptide sequence analysis and molecular cloning reveal two calcium pump isoforms in the human erythrocyte membrane
    • Strehler, E. E., James, P., Fischer, R., Heim, R., Vorherr, T., Filoteo, A. G., Penniston, J. T. and Carafoli, E. (1990) Peptide sequence analysis and molecular cloning reveal two calcium pump isoforms in the human erythrocyte membrane. J. Biol. Chem. 265, 2835-2842
    • (1990) J. Biol. Chem , vol.265 , pp. 2835-2842
    • Strehler, E.E.1    James, P.2    Fischer, R.3    Heim, R.4    Vorherr, T.5    Filoteo, A.G.6    Penniston, J.T.7    Carafoli, E.8
  • 22
    • 0034693172 scopus 로고    scopus 로고
    • Oligomerization of the plasma membrane calcium pump involves two regions with different thermal stability
    • Levi, V., Rossi, J. P., Castello, P. R. and González Flecha, F. L. (2000) Oligomerization of the plasma membrane calcium pump involves two regions with different thermal stability. FEBS Lett. 483, 99-103
    • (2000) FEBS Lett , vol.483 , pp. 99-103
    • Levi, V.1    Rossi, J.P.2    Castello, P.R.3    González Flecha, F.L.4
  • 23
    • 0036219942 scopus 로고    scopus 로고
    • Structural significance of the plasma membrane calcium pump oligomerization
    • Levi, V., Rossi, J. P., Castello, P. R. and González Flecha, F. L. (2002) Structural significance of the plasma membrane calcium pump oligomerization. Biophys. J. 82, 437-446
    • (2002) Biophys. J , vol.82 , pp. 437-446
    • Levi, V.1    Rossi, J.P.2    Castello, P.R.3    González Flecha, F.L.4
  • 24
    • 4244120872 scopus 로고
    • Microdetermination of phosphorus
    • Chen, P. S., Toribara, T. Y. and Warner, H. (1956) Microdetermination of phosphorus. Anal. Chem. 28, 1756-1758
    • (1956) Anal. Chem , vol.28 , pp. 1756-1758
    • Chen, P.S.1    Toribara, T.Y.2    Warner, H.3
  • 25
    • 0021210752 scopus 로고
    • Binding of sodium and potassium to the sodium pump of pig kidney evaluated from nucleotide-binding behaviour
    • Jensen, J., Norby, J. G. and Ottolenghi, P. (1984) Binding of sodium and potassium to the sodium pump of pig kidney evaluated from nucleotide-binding behaviour. J. Physiol. 346, 219-241
    • (1984) J. Physiol , vol.346 , pp. 219-241
    • Jensen, J.1    Norby, J.G.2    Ottolenghi, P.3
  • 26
    • 0024443728 scopus 로고
    • Purification and characterization of band 3 protein
    • Casey, J. R., Lieberman, D. M. and Reithmeier, R. A. (1989) Purification and characterization of band 3 protein. Methods Enzymol. 173, 494-512
    • (1989) Methods Enzymol , vol.173 , pp. 494-512
    • Casey, J.R.1    Lieberman, D.M.2    Reithmeier, R.A.3
  • 27
    • 0028856379 scopus 로고
    • Preparation and characterization of glucosylated aminoglycerophospholipids
    • Ravandi, A., Kuksis, A., Marai, L. and Myher, J. J. (1995) Preparation and characterization of glucosylated aminoglycerophospholipids. Lipids 30, 885-891
    • (1995) Lipids , vol.30 , pp. 885-891
    • Ravandi, A.1    Kuksis, A.2    Marai, L.3    Myher, J.J.4
  • 28
    • 0032062824 scopus 로고    scopus 로고
    • Identification of deoxy-D-fructosyl phosphatidylethanolamine as a non-enzymic glycation product of phosphatidylethanolamine and its occurrence in human blood plasma and red blood cells
    • Lertsiri, S., Shiraishi, M. and Miyazawa, T. (1998) Identification of deoxy-D-fructosyl phosphatidylethanolamine as a non-enzymic glycation product of phosphatidylethanolamine and its occurrence in human blood plasma and red blood cells. Biosci. Biotechnol. Biochem. 62, 893-901
    • (1998) Biosci. Biotechnol. Biochem , vol.62 , pp. 893-901
    • Lertsiri, S.1    Shiraishi, M.2    Miyazawa, T.3
  • 29
    • 0037591275 scopus 로고    scopus 로고
    • 2+-ATPase by ATP and acidic phospholipids
    • 2+-ATPase by ATP and acidic phospholipids. J. Biol. Chem. 278, 22265-22271
    • (2003) J. Biol. Chem , vol.278 , pp. 22265-22271
    • Filomatori, C.V.1    Rega, A.F.2
  • 30
    • 0012043902 scopus 로고
    • Spectrophotometric studies of the oxidation of fats. VI. Oxygen absorption and chromophore production in fatty esters
    • Holman, R. T. and Burr, G. O. (1946) Spectrophotometric studies of the oxidation of fats. VI. Oxygen absorption and chromophore production in fatty esters. J. Am. Chem. Soc. 68, 562-566
    • (1946) J. Am. Chem. Soc , vol.68 , pp. 562-566
    • Holman, R.T.1    Burr, G.O.2
  • 31
    • 0014937306 scopus 로고
    • The detection of oxidation in liposome preparations
    • Klein, R. A. (1970) The detection of oxidation in liposome preparations. Biochim. Biophys. Acta 210, 486-489
    • (1970) Biochim. Biophys. Acta , vol.210 , pp. 486-489
    • Klein, R.A.1
  • 32
    • 0037958570 scopus 로고    scopus 로고
    • Quantitative analysis of interactions between membrane proteins and amphiphiles using resonance energy transfer
    • Levi, V., Rossi, J. P., Castello, P. R. and González Flecha, F. L. (2003) Quantitative analysis of interactions between membrane proteins and amphiphiles using resonance energy transfer. Anal. Biochem. 317, 171-179
    • (2003) Anal. Biochem , vol.317 , pp. 171-179
    • Levi, V.1    Rossi, J.P.2    Castello, P.R.3    González Flecha, F.L.4
  • 34
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau, W. M., Wimley, W. C., Gawrisch, K. and White, S. H. (1998) The preference of tryptophan for membrane interfaces. Biochemistry 37, 14713-14718
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 38
    • 0022348630 scopus 로고    scopus 로고
    • Characterization of the solubilization of lipid bilayers by surfactants
    • Lichtenberg, D. (1998) Characterization of the solubilization of lipid bilayers by surfactants. Biochim. Biophys. Acta 821, 470-478
    • (1998) Biochim. Biophys. Acta , vol.821 , pp. 470-478
    • Lichtenberg, D.1
  • 39
    • 0031352721 scopus 로고    scopus 로고
    • Molecular composition of soybean phospholipids
    • Mukhamedova, Kh. S. and Glushenkova, A. I. (1997) Molecular composition of soybean phospholipids. Chem. Nat. Comp. 33, 693-694
    • (1997) Chem. Nat. Comp , vol.33 , pp. 693-694
    • Mukhamedova, K.S.1    Glushenkova, A.I.2
  • 40
    • 0015236352 scopus 로고
    • Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane
    • Fairbanks, G., Steck, T. L. and Wallach, D. F. (1971) Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 10, 2606-2617
    • (1971) Biochemistry , vol.10 , pp. 2606-2617
    • Fairbanks, G.1    Steck, T.L.2    Wallach, D.F.3
  • 41
    • 0035423934 scopus 로고    scopus 로고
    • Stabilizing membrane proteins
    • Bowie, J. U. (2001) Stabilizing membrane proteins. Curr. Opin. Struct. Biol. 11, 397-402
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 397-402
    • Bowie, J.U.1
  • 42
    • 37349040730 scopus 로고    scopus 로고
    • Purification of the human α2 isoform of Na,K-ATPase expressed in Pichia pastoris. Stabilization by lipids and FXYD1
    • Lifshitz, Y., Petrovich, E., Haviv, H., Goldshleger, R., Tal, D. M., Garty, H. and Karlish, S. J. (2007) Purification of the human α2 isoform of Na,K-ATPase expressed in Pichia pastoris. Stabilization by lipids and FXYD1. Biochemistry 46, 14937-14950
    • (2007) Biochemistry , vol.46 , pp. 14937-14950
    • Lifshitz, Y.1    Petrovich, E.2    Haviv, H.3    Goldshleger, R.4    Tal, D.M.5    Garty, H.6    Karlish, S.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.