Protein-liposome Interactions and Their Relevance to the Structure and Function of Cell Membranes

Overview

Journal Mol Cell Biochem

Publisher Springer

Specialty Biochemistry

Date 1976 Feb 25

PMID 177856

Citations 19

Authors

H K Kimelberg

Affiliations

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Abstract

Recent studies on the interactions of soluble proteins, membrane proteins and enzymes with phospholipid model membranes are reviewed. Similarities between the properties of such systems and the behavior of biomembranes, such as alterations in the redox potential of cytochrome c after binding to membranes and effects of phospholipid fluidity on (Na+K) ATPase activity, are emphasized. The degree of correspondence between the behavior of model systems and natural membranes encourages the continuing use of model membranes in studies on protein-lipid interactions. However, some of the data on the increase of surface pressure of phospholipid monolayers by proteins and increases in the permeability of liposomes indicate that many soluble proteins also have a capability to interact hydrophobically with phospholipids. Thus a sharp distinction between both peripheral and integral membrane proteins and non-membrane proteins are not seen by these techniques. Cautious use of such studies, however, should lead to greater understanding of the molecular basis of cell membrane structure and function in normal and pathological states. Studies implicating protein-lipid interactions and (Na+K) ATPase activity in membrane alterations in disease states are also briefly discussed.

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References

Helenius A, Simons K . The binding of detergents to lipophilic and hydrophilic proteins. J Biol Chem. 1972; 247(11):3656-61. View

Smith M . Influence of temperature acclimatization on the temperature-dependence and ouabain-sensitizing of goldfish intestinal adenosine triphosphatase. Biochem J. 1967; 105(1):65-71. PMC: 1198274. DOI: 10.1042/bj1050065. View

de Gier J, Mandersloot J, Van Deenen L . Lipid composition and permeability of liposomes. Biochim Biophys Acta. 1968; 150(4):666-75. DOI: 10.1016/0005-2736(68)90056-4. View

Papahadjopoulos D, Miller N . Phospholipid model membranes. I. Structural characteristics of hydrated liquid crystals. Biochim Biophys Acta. 1967; 135(4):624-38. DOI: 10.1016/0005-2736(67)90094-6. View

Esfahani M, Limbrick A, Knutton S, Oka T, WAKIL S . The molecular organization of lipids in the membrane of Escherichia coli: phase transitions. Proc Natl Acad Sci U S A. 1971; 68(12):3180-4. PMC: 389617. DOI: 10.1073/pnas.68.12.3180. View

HOKIN L, Hexum T . Studies on the characterization of the sodium-potassium transport adenosine triphosphatase. Arch Biochem Biophys. 1972; 151(2):453-63. DOI: 10.1016/0003-9861(72)90521-8. View

WHEELER K, Whittam R . The involvement of phosphatidylserine in adenosine triphosphatase activity of the sodium pump. J Physiol. 1970; 207(2):303-28. PMC: 1348708. DOI: 10.1113/jphysiol.1970.sp009063. View

Ohnishi T, Kawamura H . [ROLE OF PHOSPHATIDES IN ADENOSINE TRIPHOSPHATASE SENSITIVE TO OUABAIN LOCALIZED IN ERYTHROCYTE MEMBRANES]. J Biochem. 1964; 56:377-8. DOI: 10.1093/oxfordjournals.jbchem.a128006. View

Overath P, Schairer H, STOFFEL W . Correlation of in vivo and in vitro phase transitions of membrane lipids in Escherichia coli. Proc Natl Acad Sci U S A. 1970; 67(2):606-12. PMC: 283249. DOI: 10.1073/pnas.67.2.606. View

10.

Marchesi V, Jackson R, Segrest J, Kahane I . Molecular features of the major glycoprotein of the human erythrocyte membrane. Fed Proc. 1973; 32(8):1833-7. View

11.

SECCHI G, Alessio L, CAMBIAGHI G . Na plus-K plus-ATPase activity of erythrocyte membranes: in urban populations not occupationally exposed to lead. Arch Environ Health. 1973; 27(6):399-400. DOI: 10.1080/00039896.1973.10666412. View

12.

Kimelberg H, Lee C . Binding and electron transfer to cytochrome c in artificial phospholipid membranes. Biochem Biophys Res Commun. 1969; 34(6):784-90. DOI: 10.1016/0006-291x(69)90248-4. View

13.

Fourcans B, Jain M . Role of phospholipids in transport and enzymic reactions. Adv Lipid Res. 1974; 12(0):147-226. DOI: 10.1016/b978-0-12-024912-1.50011-9. View

14.

Kleemann W, McConnell H . Lateral phase separations in Escherichia coli membranes. Biochim Biophys Acta. 1974; 345(2):220-30. DOI: 10.1016/0005-2736(74)90260-0. View

15.

Lim R, de la Torre J, Mullan S . Protein and enzyme alterations in experimental brain injury. Arch Neurol. 1972; 27(4):314-21. DOI: 10.1001/archneur.1972.00490160042006. View

16.

GOLDMAN S, Albers R . Sodium-potassium-activated adenosine triphosphatase. IX. The role of phospholipids. J Biol Chem. 1973; 248(3):867-74. View

17.

Letellier L, SHECHTER E . Correlations between structure and spectroscopic properties in membrane model system. Fluorescence and circular dichroism of the cytochrome c-cardiolipin system. Eur J Biochem. 1973; 40(2):507-12. DOI: 10.1111/j.1432-1033.1973.tb03220.x. View

18.

Claude A . FRACTIONATION OF MAMMALIAN LIVER CELLS BY DIFFERENTIAL CENTRIFUGATION : I. PROBLEMS, METHODS, AND PREPARATION OF EXTRACT. J Exp Med. 2009; 84(1):51-9. PMC: 2135638. View

19.

Lenaz G, SECHI A, Landi L, Bertoli E . Activation energies of different mitochondrial enzymes: breaks in Arrhenius plots of membrane-bound enzymes occur at different temperatures. Biochem Biophys Res Commun. 1972; 49(2):536-42. DOI: 10.1016/0006-291x(72)90444-5. View

20.

Dahl J, HOKIN L . The sodium-potassium adenosinetriphosphatase. Annu Rev Biochem. 1974; 43(0):327-56. DOI: 10.1146/annurev.bi.43.070174.001551. View