Search results for: Christian Vial

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article

Acyl chain composition determines cardiolipin clustering induced by mitochondrial creatine kinase binding to monolayers

Ofelia Maniti, Mouhedine Cheniour, Marie-France Lecompte, Olivier Marcillat, more

BBA - Biomembranes > 2011 > 1808 > 4 > 1129-1139

It has been recently shown that mitochondrial creatine kinase (mtCK) organizes mitochondrial model membrane by modulating the state and fluidity of lipids and by promoting the formation of protein–cardiolipin clusters. This report shows, using Brewster angle microscopy, that such clustering is largely dependent on the acyl chain composition of phospholipids. Indeed, mtCK-cardiolipin domains were observed...

article

Male Phyllotreta striolata (F.) Produce an Aggregation Pheromone: Identification of Male-specific compounds and Interaction with Host Plant Volatiles

Franziska Beran, Inga Mewis, Ramasamy Srinivasan, Jiří Svoboda, more

Journal of Chemical Ecology > 2011 > 37 > 1 > 85-97

The chrysomelid beetle Phyllotreta striolata is an important pest of Brassicaceae in Southeast Asia and North America. Here, we identified the aggregation pheromone of a population of P. striolata from Taiwan, and host plant volatiles that interact with the pheromone. Volatiles emitted by feeding male P. striolata attracted males and females in the field. Headspace volatile analyses revealed that...

article

Mitochondrial creatine kinase interaction with cardiolipin-containing biomimetic membranes is a two-step process involving adsorption and insertion

Ofelia Maniti, Marie-France Lecompte, Olivier Marcillat, Christian Vial, more

European Biophysics Journal > 2010 > 39 > 12 > 1649-1655

Mitochondrial creatine kinase (mtCK) binding to the mitochondrial inner membrane largely determines its biological functions in cellular energy homeostasis, mitochondrial physiology, and dynamics. The membrane binding mechanism is, however, not completely understood. Recent data suggest that a hydrophobic component is involved in mtCK binding to cardiolipin at the outer face of the inner mitochondrial...

article

Mitochondrial creatine kinase interaction with heterogeneous monolayers: Effect on lipid lateral organization

Nathalie Vernoux, Ofelia Maniti, Olivier Marcillat, Christian Vial, more

Biochimie > 2009 > 91 > 6 > 752-764

Our study highlights the tight relationship between protein binding to monolayers and the phase-state of the phospholipids. Interaction of mitochondrial creatine kinase with phospholipidic membranes was analysed using a two-phase monolayer system containing anionic phospholipids under chain mismatch conditions. Monolayers were made up of mixtures of DMPC/DPPG or DPPC/DMPG containing 40% negatively...

article

Mitochondrial Creatine Kinase Binding to Phospholipid Monolayers Induces Cardiolipin Segregation

Ofelia Maniti, Marie-France Lecompte, Olivier Marcillat, Bernard Desbat, more

Biophysical Journal > 2009 > 96 > 6 > 2428-2438

It is well established that the octameric mitochondrial form of creatine kinase (mtCK) binds to the outer face of the inner mitochondrial membrane mainly via electrostatic interactions with cardiolipin (CL). However, little is known about the consequences of these interactions on membrane and protein levels. Brewster angle microscopy investigations provide, for the first time to our knowledge, images...

article

Structure Elucidation of a Pungent Compound in Black Cardamom: Amomum tsao-ko Crevost et Lemarié (Zingiberaceae)

Christian Starkenmann, Fabienne Mayenzet, Robert Brauchli, Laurent Wunsche, more

Journal of Agricultural and Food Chemistry > 2007 > 55 > 26 > 10902 - 10907

article

Mitochondrial creatine kinase adsorption to biomimetic membranes: A Langmuir monolayer study

Nathalie Vernoux, Ofelia Maniti, Françoise Besson, Thierry Granjon, more

Journal of Colloid And Interface Science > 2007 > 310 > 2 > 436-445

Interaction of mitochondrial creatine kinase (mtCK) with either synthetic or natural zwitterionic or acidic phospholipids was monitored by surface pressure measurements. Injection of mtCK beneath a monolayer at very low surface pressure results in a large increase in the apparent area per lipid molecule reflecting the intrinsic surface activity of the protein. This effect is particularly pronounced...

article

Despite its high similarity with monomeric arginine kinase, muscle creatine kinase is only enzymatically active as a dimer

Ayman M. Awama, Hortense Mazon, Christian Vial, Olivier Marcillat

Archives of Biochemistry and Biophysics > 2007 > 458 > 2 > 158-166

Although having highly similar primary to tertiary structures, the different guanidino kinases exhibit distinct quaternary structures: monomer, dimer or octamer. However, no evidence for communication between subunits has yet been provided, and reasons for these different levels of quaternary complexity that can be observed from invertebrate to mammalian guanidino kinases remain elusive. Muscle creatine...

article

Local dynamics measured by hydrogen/deuterium exchange and mass spectrometry of creatine kinase digested by two proteases

Hortense Mazon, Olivier Marcillat, Eric Forest, Christian Vial

Biochimie > 2005 > 87 > 12 > 1101-1110

Hydrogen/deuterium exchange coupled to mass spectrometry has been used to investigate the structure and dynamics of native dimeric cytosolic muscle creatine kinase. The protein was incubated in D ₂ O for various time. After H/D exchange and rapid quenching of the reaction, the partially deuterated protein was cleaved in parallel by two different proteases (pepsin or type XIII protease from...

article

Conformational Dynamics of the GdmHCl-Induced Molten Globule State of Creatine Kinase Monitored by Hydrogen Exchange and Mass Spectrometry

Hortense Mazon, Olivier Marcillat, Eric Forest, David L. Smith, more

Biochemistry > 2004 > 43 > 17 > 5045 - 5054

article

Changes in MM-CK Conformational Mobility upon Formation of the ADP−Mg ²⁺ −NO ₃ ^- −Creatine Transition State Analogue Complex As Detected by Hydrogen/Deuterium Exchange

Hortense Mazon, Olivier Marcillat, Eric Forest, Christian Vial

Biochemistry > 2003 > 42 > 46 > 13596 - 13604

article

Role of C-Terminal Sequences in the Folding of Muscle Creatine Kinase

Hortense Mazon, Olivier Marcillat, Christian Vial, Eric Clottes

Biochemistry > 2002 > 41 > 30 > 9646 - 9653

article

Mitochondrial Creatine Kinase Binding to Phospholipids Decreases Fluidity of Membranes and Promotes New Lipid-Induced β Structures As Monitored by Red Edge Excitation Shift, Laurdan Fluorescence, and FTIR ^†

Thierry Granjon, Marie-Jeanne Vacheron, Christian Vial, René Buchet

Biochemistry > 2001 > 40 > 20 > 6016 - 6026

article

Structural Changes of Mitochondrial Creatine Kinase upon Binding of ADP, ATP, or Pi, Observed by Reaction-Induced Infrared Difference Spectra ^†

Thierry Granjon, Marie-Jeanne Vacheron, Christian Vial, René Buchet

Biochemistry > 2001 > 40 > 9 > 2988 - 2994

article

Mitochondrial Creatine Kinase Binding to Liposomes and Vesicle Aggregation: Effect of Cleavage by Proteinase K

Thierry Granjon, Christian Vial, René Buchet, Marie-Jeanne Vacheron

The Protein Journal > 2001 > 20 > 8 > 593-599

Mitochondrial creatine kinase and its proteinase K nicked-derivative interaction with liposomes induced slight secondary structure changes evidenced by infrared spectra. In nondenaturing conditions, the N-terminal (K₁) and the C-terminal (K₂) fragments remained associated with each other and bound to liposomes. When the two fragments were separated by denaturation, K₂ was soluble, whereas most of...

article

Cloning, Escherichia coli Expression, and Phase-Transition Chromatography-Based Purification of Recombinant Rabbit Heart Mitochondrial Creatine Kinase

Olivier Marcillat, Catherine Perraut, Thierry Granjon, Christian Vial, more

Protein Expression and Purification > 1999 > 17 > 1 > 163-168

A cDNA clone of the mitochondrial sarcomeric creatine kinase cDNA was obtained by screening a rabbit heart library. This cDNA is characterized by a 1257-nucleotide open reading frame encoding a 419-amino-acid protein with a cleavable 39-amino-acid mitochondrial presequence (Accession No. AJ011334). This new member of the guanidino kinase family shows a high degree of sequence similarity with the other...

article

Mitochondrial Creatine Kinase Interaction with Phospholipid Vesicles

Marie-Jeanne Vacheron, Eric Clottes, Cécile Chautard, Christian Vial

Archives of Biochemistry and Biophysics > 1997 > 344 > 2 > 316-324

The characteristics of the interaction of mitochondrial creatine kinase (mt-CK) with phospholipid vesicles are determined. The presence of negatively charged phospholipids is required to obtain a significant binding of mt-CK. The interaction seems to be largely of an electrostatic nature: it increases with increasing amounts of anionic phospholipid in liposomes and decreases when the ionic strength...

article

Physico-chemical characterization of the monomeric species

Fabienne Couthon, Eric Clottes, Christian Vial

Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology > 1997 > 1339 > 2 > 277-288

Incubation of dimeric MM-creatine kinase (MM-CK) with high NaCl or LiCl concentrations results in dissociation of the subunits and complete enzyme inactivation. In NaCl, this process, which depends on protein concentration, may be described according to a two-state model where the dimer can be reversibly converted into compact folded monomers (D↔2M). At LiCl concentrations higher than 2–2.5 M, MM-CK...

article

Proteinase K Processing of Rabbit Muscle Creatine Kinase

Chantal Leydier, Jens S. Andersen, Fabienne Couthon, Eric Forest, more

The Protein Journal > 1997 > 16 > 1 > 67-74

Proteinase K cleaves selectively both cytosolic and mitochondrial isoforms of creatine kinase leading to the appearance of two fragments, a large N-terminal one (K1) and a small C-terminal peptide (K2) which remain associated together. The loss of enzymatic activity correlates with the extent of monomer cleavage. N-terminal sequencing of the K2 fragments from rabbit cytosolic and pig mitochondrial...

article

Refolding of SDS- and Thermally Denatured MM-Creatine Kinase Using Cyclodextrins

Fabienne Couthon, Eric Clottes, Christian Vial

Biochemical and Biophysical Research Communications > 1996 > 227 > 3 > 854-860

We have tried to refold thermally-denatured MM-CK using detergent and cyclodextrins as protein folding assistants. This procedure, named artificial chaperone-assisted refolding, has been extensively tested to refold carbonic anhydrase B. Here, we describe a study which shows that this procedure can be applied to refold a dimeric multidomain protein : MM-creatine kinase. The pair SDS/hydroxy-propyl...

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Search results for: Christian Vial

Acyl chain composition determines cardiolipin clustering induced by mitochondrial creatine kinase binding to monolayers

Male Phyllotreta striolata (F.) Produce an Aggregation Pheromone: Identification of Male-specific compounds and Interaction with Host Plant Volatiles

Mitochondrial creatine kinase interaction with cardiolipin-containing biomimetic membranes is a two-step process involving adsorption and insertion

Mitochondrial creatine kinase interaction with heterogeneous monolayers: Effect on lipid lateral organization

Mitochondrial Creatine Kinase Binding to Phospholipid Monolayers Induces Cardiolipin Segregation

Structure Elucidation of a Pungent Compound in Black Cardamom: Amomum tsao-ko Crevost et Lemarié (Zingiberaceae)

Mitochondrial creatine kinase adsorption to biomimetic membranes: A Langmuir monolayer study

Despite its high similarity with monomeric arginine kinase, muscle creatine kinase is only enzymatically active as a dimer

Local dynamics measured by hydrogen/deuterium exchange and mass spectrometry of creatine kinase digested by two proteases

Conformational Dynamics of the GdmHCl-Induced Molten Globule State of Creatine Kinase Monitored by Hydrogen Exchange and Mass Spectrometry

Changes in MM-CK Conformational Mobility upon Formation of the ADP−Mg ²⁺ −NO ₃ ^- −Creatine Transition State Analogue Complex As Detected by Hydrogen/Deuterium Exchange

Role of C-Terminal Sequences in the Folding of Muscle Creatine Kinase

Mitochondrial Creatine Kinase Binding to Phospholipids Decreases Fluidity of Membranes and Promotes New Lipid-Induced β Structures As Monitored by Red Edge Excitation Shift, Laurdan Fluorescence, and FTIR ^†

Structural Changes of Mitochondrial Creatine Kinase upon Binding of ADP, ATP, or Pi, Observed by Reaction-Induced Infrared Difference Spectra ^†

Mitochondrial Creatine Kinase Binding to Liposomes and Vesicle Aggregation: Effect of Cleavage by Proteinase K

Cloning, Escherichia coli Expression, and Phase-Transition Chromatography-Based Purification of Recombinant Rabbit Heart Mitochondrial Creatine Kinase

Mitochondrial Creatine Kinase Interaction with Phospholipid Vesicles

Physico-chemical characterization of the monomeric species

Proteinase K Processing of Rabbit Muscle Creatine Kinase

Refolding of SDS- and Thermally Denatured MM-Creatine Kinase Using Cyclodextrins

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