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Biomedical subjects

M Bellemare

Publications and source records attributed to M Bellemare.

11 recordsLinked to original sources
PubMed2006

Participatory ergonomic processes to reduce musculoskeletal disorders: summary of a Québec experience.

This article critically reviews 11 participatory ergonomic interventions carried out in Québec by the Occupational Health and Safety Research Institute (IRSST). In the introduction, the characteristics of the approach used are situated in relation to the literature on this subject. Based on the "Ergo team" formula, the approach aims to provide company personnel with the skills to analyze and correct hazardous workstations in relation to musculoskeletal disorders (MSD), using an analysis process that the researchers developed. Although isolated workstations were corrected, the process aims for more general impacts on the company. In the 11 interventions, 40 work situations were analyzed, and in 31 cases, changes were implemented to reduce MSD risks. The most common changes dealt with the tools/equipment (77.4% and physical layouts (84%); changes involving work methods (29% and work organization (12.9%) were less common. The difficulties encountered in the interventions are summarized, and the possible impacts of the interventions on the organization and psychosocial factors are discussed. The authors then address the limitations of the paper and the factors that should be considered in evaluating such a participatory process. The authors conclude that the participatory process was successful in implementing changes in companies and that other studies are necessary for a better understanding of the process and its impacts.

Ergonomics↗
PubMed1995

Radioimmunoassay for hexarelin, a peptidic growth hormone secretagogue, and its pharmacokinetic studies.

A radioimmunoassay (RIA) method for hexarelin, a peptidic growth hormone secretagogue, has been developed and applied to pharmacokinetic studies in dogs following an IV dose of 1 microgram/kg, and three SC doses of 1, 10, and 100 micrograms/kg. The sensitivity of the assay was determined to be 1.34 fmol/assay. Cross-reactivity of the antiserum with nine hexarelin analogues was less than 1% upon modification of positions 3, 4, or 5 of the peptide. No apparent cross-reaction with endogenous hexarelin metabolites were observed. Intra- and interassay coefficients of variation were less than 3% and 4%, respectively. Intravenous bolus pharmacokinetics of hexarelin displayed a high terminal half-life of 120 min, a fractional plasma clearance of 4.28 ml/min/kg, and a volume of distribution at steady state of 387.7 ml/kg. Following SC administration of hexarelin, despite the increase in dose administered, both clearance (3.93-5.17 ml/min/kg) and volume of distribution (316-544 ml/kg) parameters remained constant over the dose range studied.

Amino Acid Sequence↗
PubMed1991

A competitive enzyme immunoassay for albuterol: its application for the drug screening in urine.

A competitive enzyme immunoassay using purified monoclonal IgG1 and an alkaline phosphatase-albuterol derivative has been developed for the quantification of albuterol in urine. The calibration curve obtained in optimal incubation conditions is characterized by a minimum detectable level of 26 fmol/well and a working range from 52 fmol to 4,2 pmol/well. This method allows the precise and accurate quantification of albuterol in horse urine without any clean up or extraction step. Moreover the definition of its specificity shows a cross-reactivity of the antibody with the glucurono-/sulfo-conjugates of albuterol. This property is particularly interesting for the screening of urinary albuterol residues in meat producing animals.

Albuterol↗
PubMed1990

Radioimmunoassay for albuterol using a monoclonal antibody: application for direct quantification in horse urine.

A monoclonal antibody was synthesized in mouse against the O-(3-carboxypropionyl) derivative of albuterol linked to bovine serum albumin. Isotyping of this material revealed the IgG1 class characterized by an affinity constant of 1.03 nM-1 and a density of sites of 0.55 nM. This antibody was found specific as its cross-reactivity to structurally related molecules was less than 1% except for clenbuterol (75%). A radioimmunoassay was set up with culture supernatant (final dilution 1/1000) and [3H] albuterol. The calibration curve was characterized by a maximum binding of 28%, an ED50 of 1.15 pmol per tube, the detection limit was 28.8 fmol/tube and the linearity of the response was up to 39.8 pmol/tube. This RIA method has been used for direct quantitation of albuterol in horse urine without any clean-up or extraction step.

Albuterol↗
PubMed1989

Analysis of albuterol in human plasma based on immunoaffinity chromatographic clean-up combined with high-performance liquid chromatography with fluorimetric detection.

A method combining immunoaffinity chromatography with high-performance liquid chromatography was developed for the determination of albuterol in human plasma. The immunoaffinity chromatography, based on the specific interaction of albuterol with the immobilized antibody raised against it, was used as a clean-up step. Albuterol eluted from this immunochemical solid-phase clean-up step was analysed by reversed-phase high-performance liquid chromatography with fluorimetric detection. The performance of the assay was validated on six normal volunteers after a 4-mg oral dose of albuterol, which gave a peak plasma concentration in the range 6.67-15.31 ng/ml at 3-4 h after the dose. Plasma levels (0.79-1.56 ng/ml) of albuterol could be detected up to 24 h after the dose.

Albuterol↗
PubMedDate not supplied

The effect of LSD on the histology and ultrastructure of the neuroepithelium of young chick embryos: a stereological study.

Five control chick embryos and fifteen exposed to LSD at concentrations of 2.5, 12.5 and 50 mug/ml were examined. The morphometric analysis performed at the light microscope level shows that (1) the section area of the neural tube increases with the two highest doses of lysergic acid diethylamide (LDS) employed, (2) the volume fraction of the intercellular spaces decreases with the two highest doses of LSD, (3) the volume fraction of the nuclei in the neural tube is not modified with any concentrations of LSD employed, (4) the volume fraction of the cytoplasm in the neural tube increases with all three concentrations, and (5) the nucleo-cytoplasmic ratio decreases with all three doses employed. Moreover, at the ultrastructural level, it was found that (1) the volume fraction of mitochondria in the cytoplasm decreases at doses of 12.5 and 50 mug/ml (2) the surface to volume ratio of the mitochondria is unchanged with any of the concentrations of LSD employed and (3) the surface density of the endoplasmic reticulum in the cytoplasm increases only with a dose of 2.5 mug/ml of LSD.

Animals↗
PubMedDate not supplied

Role of the endopeptidase 24.11 in the disposition and metabolism of endogenous atrial natriuretic factor in the rabbit.

The neutral endopeptidase 24.11 (NEP) has been shown to inactivate the atrial natriuretic factor (ANF) by opening the ring structure. To document the role of NEP in the metabolic fate of ANF in vivo, the effects of an infusion of thiorphan (25 micrograms/min/kg), a specific NEP inhibitor, on the kinetics and metabolism of endogenous ANF were studied in conscious rabbits. A bolus of [125I]ANF(99-126) was injected 50 min after the beginning of the infusion of thiorphan. Plasma samples containing the radioactive peptides were separated by reverse-phase HPLC. The parent compound could be separated from at least two other minor metabolites, corresponding to the elution position of [125I]ANF(99-105/106-126), the inactive ring-opened metabolite, and of [125I]ANF(103-126), an N-truncated analog. The generation of the N-truncated metabolite was increased by thiorphan. Thiorphan also induced an increase in plasma ANF (29%) that was closely associated with a 32% reduction in the systemic clearance of [125I]ANF(99-126), whereas no modification in the estimated secretion rate was detected. These results support a role for NEP in the regulation of endogenous ANF plasma levels. These results also suggest that specific inhibition of NEP may result in an increase in the apparent activity of alternative metabolic pathways.

Animals↗