Jean Derancourt

Centre National de la Recherche Scientifique

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Ridha Kassab

Centre National de la Recherche Scientifique

Jean‐Paul Capony

Centre National de la Recherche Scientifique

Raoul Bertrand

Centre de Recherche en Biologie cellulaire de Montpellier

Jacques Haiech

Centre National de la Recherche Scientifique

Etienne Audemard

Université de Montréal

Jacques Demaille

Institut de Génétique Moléculaire de Montpellier

Patrick Chaussepied

Centre National de la Recherche Scientifique

J C Cavadore

Centre National de la Recherche Scientifique

Jean‐Claude Labbé

Université de Montréal

Dominique Mornet

Inserm

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Centre National de la Recherche Scientifique

177

Inserm

156

Université de Montpellier

Centre de Recherche en Biologie cellulaire de Montpellier

Université Paris Cité

Sorbonne Université

Weatherford College

Institut National de la Recherche Agronomique

Centre National pour la Recherche Scientifique et Technique (CNRST)

Heidelberg University

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A new large-scale purification procedure for muscular parvalbumins

Biochimie (1979)

Jacques Haiech Jean Derancourt Jean-François Péchère Jacques Demaille

Tropomyosin

10.1016/s0300-9084(79)80155-8

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Citations (49)

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Journal of Biological Chemistry (1994)

Grant Mason A Witte A. Wilhelmsson Lorenz Poellinger Jan Gustafsson

4555 Molecular events in close proximity to the membrane associated with the binding of

10.1016/s0021-9258(17)41833-3

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Citations (0)

Author Index

Journal of Biological Chemistry (1994)

Colin Gegg Marilynn Etzkr John Colllins Tants Kobayashi Terence Tao

Structure of the troponin complex. Implications of photocross-

10.1016/s0021-9258(17)37596-8

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Ontogenesis of rabbit liver cytochrome P450

European Journal of Biochemistry (1990)

Claude BONFINS Jean Combalbert Thierry Pineau Jacques ANGEVIN Christian Larroque

The liver hydroxylating system, mainly composed of cytochromes P 450, is not highly active during foetal life. If develops after birth and reaches the adult level several weeks post‐partum. We have studied the ontogenesis of rabbit cytochrome P 450 during the post‐natal period. Total P 450 as well as isozymes 2, 3b, 3c, 4 and 6 were measured. The evolution of these proteins with ageing, together with qualitative modification of an electrophoretic profile, produced evidence of an early developing P 450 prevailing from one week to three weeks after birth. We isolated and characterized a cytochrome, called P 450 2y, from two‐week liver microsomes. It is closely related to P450 450 3a, an adult form of rabbit P 450 induced by ethanol. They have similar molecular masses, the same λ max of CO‐reduced spectrum and exhibit immunological cross‐reactivity. However, we cannot conclude that the two proteins are identical from N‐terminal amino acid analysis or the two‐dimensional gel electrophoresis pattern. These results, as well as the recent evidence of two different genes coding for the P 450 3a family, strengthen the idea that P 450 2y and 3a are distinct proteins, P 450 2y seems to be an early developing form abundant soon after birth, while P 450 3a is a delayed form appearing like most P 450 isozymes during the fourth post‐natal week. Besides the quantitative development during perinatal life, there is an important qualitative modification of liver cytochrome P 450 content.

10.1111/j.1432-1033.1990.tb15387.x

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Citations (18)

Determination of cardiac and plasma drug levels during long‐term amiodarone therapy

European Journal of Clinical Investigation (1983)

Nadia Debbas C. Du Cailar A Sassine Jean Derancourt Jacques Demaille

Abstract. A study of plasma and cardiac concentrations of amiodarone during the course of long‐term oral therapy was made possible by the improvement of analytical high performance liquid chromatography of plasma and tissue extracts. The plasma level was found to increase linearly with the daily dose of the drug, above a threshold value of c. 1.9 mg kg ‐1 day ‐1 . Similarly, the cardiac content increased linearly with the daily dose, with no threshold, showing that the drug is taken up and accumulated in the cardiac tissue, with no obvious difference between atrial and ventricular samples ( P > 0.05). Both plasma and heart showed no saturation at high drug intake, a justification for increasing the oral intake in severe cases. The linear relationship between tissue and blood concentrations allows a prediction of the cardiac level from a simple and routine blood analysis.

Plasma levels

10.1111/j.1365-2362.1983.tb00076.x

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Citations (33)

In Vitro Creation of Amyloid Fibrils from Native and Arg124Cys Mutated βIGH3(110–131) Peptides, and Its Relevance for Lattice Corneal Amyloid Dystrophy Type I

Biochemical and Biophysical Research Communications (2000)

Clair‐Florent Schmitt‐Bernard Alain Chavanieu Jean Derancourt Bernard Arnaud Jacques Demaille

Amyloid (mycology)

10.1006/bbrc.2000.2955

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Citations (29)

Biochemical evidence for the presence of an unconventional actin protein in a prokaryotic organism

Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology (1996)

Jean-Pierre Labbé Marie-Cécile Harricane Mireille Boyer Jean Derancourt Claude Roustan

10.1016/0305-0491(96)00034-x

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Citations (7)

Abstracts of the XVIII European Conference on Muscle and Motility

Journal of Muscle Research and Cell Motility (1990)

В. П. Нестеров U. Peiper J. Hiller B. Krienke K Schüttler

10.1007/bf01833326

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Purification and Cloning of Type A/B hnRNP Proteins Involved in Transcriptional Activation from the Rat spi 2 Gene GAGA Box

Biological Chemistry (2000)

Sabrina Leverrier Elisa Cinato C. Paul Jean Derancourt Mats Bemark

The GAGA box of the rat serine protease inhibitor 2 (spi 2) genes not only acts as a basal promoter element, but also mediates transcriptional activation by growth hormone and interleukin-6. The GAGA box is separated from the TATA box by only 12 bp, and this close association is required for efficient transcription. Hence, the GAGA box may influence transcription efficiency through interactions between GAGA box binding proteins and some components of the RNA polymerase II complex. Here we report the cloning of two GAGA box-binding proteins termed p38 and p40, that belong to the type A/B heterogeneous nuclear ribonucleoprotein subgroup. GAGA box mutations that diminish the affinity for p38 and p40 decrease basal and GH-induced reporter gene expression. Furthermore, nuclear extracts depleted of p38 and p40 can no longer support GAGA box-dependent in vitro transcription. Therefore, two polypeptides previously assigned to a family of RNA processing proteins also act as DNA-binding, promoter-specific transcription factors.

TATA box

Transcription

CAAT box

RNA polymerase II

General transcription factor

Heterogeneous ribonucleoprotein particle

E-box

10.1515/bc.2000.127

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Citations (25)

Mapping of the functional domains in the amino-terminal region of calponin.

Journal of Biological Chemistry (1992)

Mohamed Mezgueldi Abdellatif Fattoum Jean Derancourt Ridha Kassab

Three chymotryptic fragments accounting for almost the entire amino acid sequence of gizzard calponin (Takahashi, K., and Nadal-Ginard, B. (1991) J. Biol. Chem. 266, 13284-13288) were isolated and characterized. They encompass the segments of residues 7-144 (NH2-terminal 13-kDa peptide), 7-182 (NH2-terminal 22-kDa peptide), and 183-292 (COOH-terminal 13-kDa peptide). They arise from the sequential hydrolysis of the peptide bonds at Tyr182-Gly183 and Tyr144-Ala145 which were protected by the binding of F-actin to calponin. Only the NH2-terminal 13- and 22-kDa fragments were retained by immobilized Ca(2+)-calmodulin, but only the larger 22 kDa entity cosedimented with F-actin and inhibited, in the absence of Ca(2+)-calmodulin, the skeletal actomyosin subfragment-1 ATPase activity as the intact calponin. Since the latter peptide differs from the NH2-terminal 13-kDa fragment by a COOH-terminal 38-residue extension, this difference segment appears to contain the actin-binding domain of calponin. Zero-length cross-linked complexes of F-actin and either calponin or its 22-kDa peptide were produced. The total CNBr digest of the F-actin-calponin conjugate was fractionated over immobilized calmodulin. The EGTA-eluted pair of cross-linked actin-calponin peptides was composed of the COOH-terminal actin segment of residues 326-355 joined to the NH2-terminal calponin region of residues 52-168 which seems to contain the major determinants for F-actin and Ca(2+)-calmodulin binding.

Calponin

EGTA

10.1016/s0021-9258(19)49625-7

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Citations (91)