Morphology modifications in negatively charged lipid monolayers upon mitochondrial creatine kinase binding

References

• Wallimann T, Wyss M, Brdiczka D, Nicolay K, Eppenberger HM. Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands – the phosphocreatine circuit for cellular energy homeostasis. Biochem J 1992; 281: 21–40
   PubMed Web of Science ®Google Scholar
• Wallimann T, Dolder M, Schlattner U, Eder M, Hornemann T, Kraft T, Stolz M. Creatine kinase: an enzyme with a central role in cellular energy metabolism. Magma 1998; 6: 116–119
   PubMedGoogle Scholar
• Dolder M, Walzel B, Speer O, Schlattner U, Wallimann T. Inhibition of the mitochondrial permeability transition by creatine kinase substrates. Requirement for microcompartmentation. J Biol Chem 2003; 278: 17760–17766
   PubMed Web of Science ®Google Scholar
• Speer O, Back N, Buerklen T, Brdiczka D, Koretsky A, Wallimann T, Eriksson O. Octameric mitochondrial creatine kinase induces and stabilizes contact sites between the inner and outer membrane. Biochem J 2005; 385: 445–450
   PubMedGoogle Scholar
• Dolder M, Wendt S, Wallimann T. Mitochondrial creatine kinase in contact sites: interaction with porin and adenine nucleotide translocase, role in permeability transition and sensitivity to oxidative damage. Biol Signals Recept 2001; 10: 93–111
   PubMedGoogle Scholar
• Brdiczka D, Beutner G, Ruck A, Dolder M, Wallimann T. The molecular structure of mitochondrial contact sites. Their role in regulation of energy metabolism and permeability transition. Biofactors 1998; 8: 235–242
   PubMed Web of Science ®Google Scholar
• O'Gorman E, Beutner G, Dolder M, Koretsky AP, Brdiczka D, Wallimann T. The role of creatine kinase in inhibition of mitochondrial permeability transition. FEBS Lett 1997; 414: 253–257
   PubMed Web of Science ®Google Scholar
• Lenz H, Schmidt M, Welge V, Kueper T, Schlattner U, Wallimann T, Elsasser HP, Wittern KP, Wenck H, Staeb F, Blatt T. Inhibition of cytosolic and mitochondrial creatine kinase by siRNA in HaCaT- and HeLaS3-cells affects cell viability and mitochondrial morphology. Mol Cell Biochem 2007; 306: 153–162
   PubMed Web of Science ®Google Scholar
• Copley SD. Enzymes with extra talents: moonlighting functions and catalytic promiscuity. Curr Opin Chem Biol 2003; 7: 265–272
   PubMed Web of Science ®Google Scholar
• Schlame M, Augustin W. Association of creatine kinase with rat heart mitochondria: high and low affinity binding sites and the involvement of phospholipids. Biomed Biochim Acta 1985; 44: 1083–1088
   PubMedGoogle Scholar
• Schlattner U, Gehring F, Vernoux N, Tokarska-Schlattner M, Neumann D, Marcillat O, Vial C, Wallimann T. C-terminal lysines determine phospholipid interaction of sarcomeric mitochondrial creatine kinase. J Biol Chem 2004; 279: 24334–24342
   PubMed Web of Science ®Google Scholar
• Vacheron MJ, Clottes E, Chautard C, Vial C. Mitochondrial creatine kinase interaction with phospholipid vesicles. Arch Biochem Biophys 1997; 344: 316–324
   PubMed Web of Science ®Google Scholar
• Vernoux N, Maniti O, Besson F, Granjon T, Marcillat O, Vial C. Mitochondrial creatine kinase adsorption to biomimetic membranes: a Langmuir monolayer study. J Colloid Interface Sci 2007; 310: 436–445
   PubMed Web of Science ®Google Scholar
• Granjon T, Vacheron MJ, Vial C, Buchet R. Mitochondrial creatine kinase binding to phospholipids decreases fluidity of membranes and promotes new lipid-induced beta structures as monitored by red edge excitation shift, laurdan fluorescence, and FTIR. Biochemistry 2001; 40: 6016–6026
   PubMed Web of Science ®Google Scholar
• Marsh D. Lateral pressure in membranes. Biochim Biophys Acta 1996; 1286: 183–223
   PubMed Web of Science ®Google Scholar
• Marcillat O, Perraut C, Granjon T, Vial C, Vacheron MJ. Cloning, Escherichia coli expression, and phase-transition chromatography-based purification of recombinant rabbit heart mitochondrial creatine kinase. Prot Expr Purif 1999; 17: 163–168
   PubMed Web of Science ®Google Scholar
• Vernoux N, Granjon T, Marcillat O, Besson F, Vial C. Interfacial behavior of cytoplasmic and mitochondrial creatine kinase oligomeric states. Biopolymers 2006; 81: 270–281
   PubMed Web of Science ®Google Scholar
• Henon S, Meunier J. Microscope at the Brewster angle: direct observation of first-order phase transitions in monolayers. Rev Sci Instrum 1991; 62: 936–939
   Web of Science ®Google Scholar
• Hönig D, Möbius D. Direct visualization of monolayers at the air-water interface by Brewster angle microscopy. J Phys Chem 1991; 95: 4590–4592
   Web of Science ®Google Scholar
• Rodriguez Patino JM, Sanchez CC, Rodriguez Nino MR. Structural and morphological characteristics of [beta]-casein monolayers at the air-water interface. Food Hydrocolloids 1999; 13: 401–408
   Web of Science ®Google Scholar
• Rodriguez Patino JM, Carrera Sanchez C, Rodriguez Nino MR. Morphological and structural characteristics of monoglyceride monolayers at the air-water interface observed by brewster angle microscopy. Langmuir 1999; 15: 2484–2492
   Google Scholar
• Ducharme D, Max JJ, Salesse C, Leblanc RM. Ellipsometric study of the physical states of phosphatidylchoilnes at the air-water interface. J Phys Chem 1990; 94: 1925–1932
   Web of Science ®Google Scholar
• Sacre MM, Tocanne JF. Importance of glycerol and fatty acid residues on the ionic properties of phosphatidylglycerols at the air-water interface. Chem Phys Lipids 1977; 18: 334–354
   Google Scholar
• Garidel P, Blume A. 1,2-Dimyristoyl-sn-glycero-3-phosphoglycerol (DMPG) monolayers: influence of temperature, pH, ionic strength and binding of alkaline earth cations. Chem Phys Lipids 2005; 138: 50–59
   Google Scholar
• Davies J, Rideal E. Interfacial phenomena2nd ed. Academic Press, New York 1963; 265
   Google Scholar
• Minones J, Jr, Dynarowicz-Latka P, Minones J, Rodriguez Patino JM, Iribarnegaray E. Orientational changes in dipalmitoyl phosphatidyl glycerol Langmuir monolayers. J Colloid Interface Sci 2003; 265: 380–385
   Google Scholar
• Koppenol S, Yu H, Zografi G. Mixing of saturated and unsaturated phosphatidylcholines and phosphatidylglycerols in monolayers at the air/water interface. J Colloid Interface Sci 1997; 189: 158–166
   Google Scholar
• Etienne F, Roche Y, Peretti P, Bernard S. Cardiolipin packing ability studied by grazing incidence X-ray diffraction. Chem Phys Lipids 2008; 152: 13–23
   Google Scholar
• Vollhardt D, Fainerman VB, Siegel S. Thermodynamic and textural characterization of DPPG phospholipid monolayers. J Phys Chem B 2000; 104: 4115–4121
   Google Scholar
• Takamoto DY, Lipp MM, von Nahmen A, Lee KY, Waring AJ, Zasadzinski JA. Interaction of lung surfactant proteins with anionic phospholipids. Biophys J 2001; 81: 153–169
   PubMed Web of Science ®Google Scholar
• Vollhardt D, Fainerman VB. Progress in characterization of Langmuir monolayers by consideration of compressibility. Adv Colloid Interface Sci 2006; 127: 83–97
   Google Scholar
• Krol S, Ross M, Sieber M, Kunneke S, Galla HJ, Janshoff A. Formation of three-dimensional protein-lipid aggregates in monolayer films induced by surfactant protein B. Biophys J 2000; 79: 904–918
   PubMed Web of Science ®Google Scholar
• Bourdos N, Kollmer F, Benninghoven A, Ross M, Sieber M, Galla HJ. Analysis of lung surfactant model systems with time-of-flight secondary ion mass spectrometry. Biophys J 2000; 79: 357–369
   PubMed Web of Science ®Google Scholar
• Kruger P, Schalke M, Wang Z, Notter RH, Dluhy RA, Losche M. Effect of hydrophobic surfactant peptides SP-B and SP-C on binary phospholipid monolayers. I. Fluorescence and dark-field microscopy. Biophys J 1999; 77: 903–914
   Google Scholar
• Lewis RN, Zweytick D, Pabst G, Lohner K, McElhaney RN. Calorimetric, x-ray diffraction, and spectroscopic studies of the thermotropic phase behavior and organization of tetramyristoyl cardiolipin membranes. Biophys J 2007; 92: 3166–3177
   PubMed Web of Science ®Google Scholar
• Bagatolli LA. To see or not to see: lateral organization of biological membranes and fluorescence microscopy. Biochim Biophys Acta 2006; 1758: 1541–1556
   PubMed Web of Science ®Google Scholar
• Barth PG, Scholte HR, Berden JA, Van der Klei-Van Moorsel JM, Luyt-Houwen IE, Van ‘t Veer-Korthof ET, Van der Harten JJ, Sobotka-Plojhar MA. An X-linked mitochondrial disease affecting cardiac muscle, skeletal muscle and neutrophil leucocytes. J Neurol Sci 1983; 62: 327–355
   PubMed Web of Science ®Google Scholar
• Barth PG, Wanders RJ, Vreken P. X-linked cardioskeletal myopathy and neutropenia (Barth syndrome). J Pediatr 1999; 135: 273–276
   Google Scholar
• Vreken P, Valianpour F, Nijtmans LG, Grivell LA, Plecko B, Wanders RJ, Barth PG. Defective remodeling of cardiolipin and phosphatidylglycerol in Barth syndrome. Biochem Biophys Res Commun 2000; 279: 378–382
   PubMedGoogle Scholar