Publications by authors named "Mallet B"

Whatever the profession of caregivers, their activity involves supporting patients and families who are suffering. Doctors and nurses, in particular, talk of the strong emotions which they feel but which they find difficult to express. Being aware of them is essential for being able to accept them and limit their consequences.

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Objective: Physical activity (PA) prescriptions provided by family physicians can promote PA participation among patients, but few physicians regularly write PA prescriptions. The objective of this study was to describe family physicians' experiences of trying to implement written PA prescriptions into their practice.

Design: Longitudinal qualitative study where participants were interviewed four times during a 12-month period.

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Backgrounds And Aims: Theory predicts that the long-term persistence of plant populations exposed to size reduction can be threatened by a loss of genetic diversity and increased inbreeding. However, several life-history and ecological traits can influence the response to population size reduction. The reproductive patterns, levels of genetic diversity and magnitude of inbreeding depression of the rare and fragmented Jumellea fragrans and of its widespread congener J.

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In CKD, uremic solutes may induce endothelial dysfunction, inflammation, and oxidative stress, leading to increased cardiovascular risk. We investigated whether the uremic solute indole-3 acetic acid (IAA) predicts clinical outcomes in patients with CKD and has prooxidant and proinflammatory effects. We studied 120 patients with CKD.

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Identifying factors that promote population differentiation is of interest for understanding the early stages of speciation. Gene flow among populations inhabiting different environments can be reduced by geographical distance (isolation-by-distance) or by divergent selection resulting from local adaptation (isolation-by-ecology). Few studies have investigated the influence of these factors in small oceanic islands where the influence of geographic distance is expected to be null but where habitat diversity could have a strong effect on population differentiation.

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We report on the use of zeolites to limit the effects of reactive oxygen species (ROS) on human albumin under in vitro conditions. Zeolites of different structure type, channel size, channel polarity, and charge-compensating cation were screened for the elimination of ROS, notably HO(·), resulting from the Fenton reaction. A test based on ischemia-modified albumin (IMA) was used as a marker to monitor the activity of HO(·) after co-exposure of human serum to these zeolites.

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Adenosine is a modulator of nociceptive pathways, both at the spinal and supraspinal levels. Adenosine A(1) and A(2A) receptors (A(1)R, A(2A)R) are expressed in the basal ganglia where they are the target of caffeine, the most widely use psychoactive drug which acts as an antagonist to both types of receptors. Given the controversial role of A(2A)R versus A(1)R in modulating pain in brain areas, mice received intracerebroventricular injection of Adonis, an agonist-like monoclonal antibody with high specificity for the A(2A)R and were subjected to behavioral tests investigating nociceptive thresholds.

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The second extracellular loop of the A(2A) receptor (A(2A)R) of adenosine was used to immunize mice for production of Adonis, an IgM monoclonal antibody. Adonis bound to the immunogen peptide and the native receptor in ELISA with K(D) values in 6.51-12.

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Myocardial damage is a frequent complication of cardiac surgery by direct mechanical trauma during the surgical procedure and by myocardial ischemia, which occurs during the cardiopulmonary bypass (CBP). Because the concentrations of biomarkers in the blood collected from the coronary sinus are the best witness of the myocardial damages, we measured the levels of specific cardiac troponin I (c-TnI) and nonspecific (adenosine, myoglobin) markers of left ventricular damages in the coronary sinus of patients during cardiac surgery. Thirty patients who underwent aortic valve replacement for aortic stenosis were included.

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Proteasome activity takes place in the cytosolic compartment and acts to degrade several proteins translated and unfolded. In transfected CHO cells expressing thyroid peroxidase (TPO), just-translated TPO undergoes proteasome activity, and then a second proteolytic system degrades more mature forms of TPO. A plasminogen-like (Pl-like) protease is found in microsomal liver membranes and in the thyroid.

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Plasminogen (Pl), a circulating protease synthesized in the liver, is also present in several tissues. In the thyroid gland a Pl-like protease was found in the apical lumen where it is involved, through its proteolytic activity, in luminal degradation of thyroglobulin (Tg). Here, we showed for the first time that the Pl-like protease apically secreted by epithelial thyroid cells is sulfated, both on tyrosine residue(s) and on oligosaccharide side chains.

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Dysfunction of copper metabolism leading to its excess or deficiency results in severe ailments. Recently, neurodegenerative disorders such as Alzheimer's disease have been associated with copper metabolism. Compounds having the ability to reduce copper levels in brain or to affect its distribution could have neuroprotective effects, mainly through a downregulation of the transcription of amyloid peptide precursor (APP).

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The prothyroid hormone, thyroglobulin (Tg), is stored at high concentrations in the thyroid follicular lumen as a soluble 19S homo-dimer and as heavier soluble (27S and 37S) and insoluble (Tgm) forms. Follicular degradation of Tg may contribute to maintaining Tg concentrations compatible with follicle integrity. Here, we report on the presence of a plasminogen-like protein in the follicular lumen of normal human thyroids and its synthesis and apical secretion by cultured epithelial thyroid cells.

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Urinary iodine is largely measured in microtiter plates by a colorimetic ceric-arsenic assay based on the Sandell-Kolthoff reaction. However, a preliminary digestion step is necessary and requires a particular care not only to transform all the iodo-compounds into iodide but also to prevent the formation of substances liable to the disturb of the subsequent redox reaction. In the present study we tested three types of digestion processes, among them two conventional methods (ammonium persulfate and chloric acid) and a new one using combined nitric acid/hydrochloric acid.

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Thyroglobulin (Tg) is cleaved into several peptides during thyroid hormone synthesis, an oxidative process. P40, an iodinated C-terminal peptide from human Tg, has a molecular weight of about 40 kDa and contains two hormonogenic sites. P40 is the smallest peptide that is still recognized by monoclonal antibodies from mice immunized with human Tg directed against its immunodominant region.

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The process of thyroid hormone synthesis, which occurs in the lumen of the thyroid follicles, results from an oxidative reaction leading, as side effects, to the multimerization of thyroglobulin (TG), the prothyroid hormone. Although hormone synthesis is a continuous process, the amount of Tg multimers is relatively constant. Here, we investigated the role of two molecular chaperones, protein disulfide isomerase (PDI) and immunoglobulin heavy chain-binding protein (BiP), present in the follicular lumen, on the multimerization process due to oxidation using both native Tg and its N-terminal domain (NTD).

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Here, we studied the fragmentation of the prothyroid hormone, thyroglobulin (Tg), which occurs during thyroid hormone synthesis, a process which involves iodide, thyroperoxidase, and the H2O2-generating system, consisting of glucose and glucose oxidase. Various peptides were found to be immunoreactive to autoantibodies to Tg from patients and monoclonal antibodies directed against the immunodominant region of Tg. The smallest peptide (40 kDa) bore thyroid hormones and was identified at the C-terminal end of the Tg molecule, which shows homologies with acetylcholinesterase.

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Reactive oxygen species (ROS) are involved in many pathological processes through modifications of structure and activity of proteins. ROS also participate in physiological pathways such as thyroid hormone biosynthesis, which proceeds through oxidation of the prothyroid hormone (thyroglobulin, Tg) and iodide. Regarding the colloidal insoluble multimerized Tg (m-Tg), which bears dityrosine bridges and is present in the follicular lumen, a mild oxidative system generated different soluble forms of Tg, more or less compacted by hydrophobic associations, and linked with Grp78 and Grp94.

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Thyroglobulin (Tg), the prothyroid hormone, is stored in the lumen of the thyroid follicles as soluble dimers and tetramers and insoluble multimers, Soluble Tg is well characterized with regards to structure and role, but insoluble Tg (i-Tg) is not. Here we show that i-Tg, multimerized through formation of disulfide and dityrosine bonds, has a higher iodine content than soluble Tg and no thyroid hormones. Furthermore, the size and the resistance of i-Tg to proteolytic enzymes implied a new mechanism by which thyrocytes may degrade this form of Tg.

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We describe a new method for quantification of iodoamino acids after enzymatic hydrolysis of thyroglobulin. The procedure involves separation of monoiodotyrosine (MIT), di-iodotyrosine, tri-iodothyronine and thyroxine by reverse phase HPLC with a Vydac C18 stationary phase and a mobile phase of water-acetonitrile-acetic acid. The separation is monitored by sensitive spectrophotometric detection through a 96-well microplate system based on the catalytic Sandell-Kolthoff reaction of iodide on the oxidation of arsenic(III) by cerium(IV).

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Formation of dityrosine bridges is a ubiquitous process mainly attributed to oxidative stress leading to protein degradation and cellular damages. Here we show that dityrosine formation is involved in a physiological process, thyroid hormone synthesis, and is strictly dependent on structural characteristics, namely N-glycans, presented by the protein acting as the prothyroid hormone. We used two isoforms of the N-terminal thyroid hormone forming domain (NTD) of human thyroglobulin: one without N-glycan (19 kDa isoform) and the other with high mannose type structures (25 kDa isoform).

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This report describes the results of the third part of the collaborative study organized by a working group sponsored by the Community Bureau of Reference of the European Community Commission. The aim of the present work was to establish the link between immunoreactivity and biological activity of human LH, thus allowing to determine the antigenic domains of the molecule involved in the induction of the biological effect. The relationship between immunoreactivity and electric charge of hLH was also studied.

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Thyroglobulin (Tg) is the substrate for thyroid hormone biosynthesis, which requires tyrosine iodination and iodotyrosine coupling and occurs at the apical membrane of the thyrocytes. Tg glycoconjugates have been shown to play a major role in Tg routing through cellular compartments and recycling after endocytosis. Here we show that glycoconjugates also play a direct role in hormonosynthesis.

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