Publications by authors named "Gachon A"

Pregnancy-specific glycoproteins (PSGs) are major placental proteins essential for the maintenance of normal gestation. However, little is known about their gene expression regulation during placentation. It was previously demonstrated that the human core promoter binding protein recently renamed Krüppel-like factor (KLF) 6 binds to a highly conserved sequence within the PSG promoters and is mainly expressed in human term placenta.

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An increase in homocysteine, a sulphur amino acid, is nowdays considered as a risk factor for cardiovascular diseases, and is independent of other risk factors. Reference range for total plasma homocysteine level in adults is usually 5-15 mmol/l. Hyperhomocysteinemia is defined as a fasting total plasma homocysteine level > 15 mmol/l.

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Lipocalins are carrier proteins for hydrophobic molecules in many biological fluids. In the oral sphere (nasal mucus, saliva, tears), they have an environmental biosensor function and are involved in the detection of odours and pheromones. Herein, we report the first identification of human lipocalins involved in odorant binding.

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Background: Relationship between plasma leptin and adiposity and gender has been reported in adults. Effects of age on plasma leptin is unclear and regulation of leptin production by white adipose tissue is still poorly understood.

Objectives: To study if age and parameters of lipolysis are related to plasma leptin concentrations.

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Objective: To address whether: (1) bioelectrical impedance analysis (BIA) can provide precise and accurate estimates of total body water (TBW) and extracellular water (ECW) in healthy elderly subjects, that display age-induced changes in body composition, (2) BIA models are improved by introducing variables related to geometrical body-shape and osmolarity.

Design: Cross-validation of available BIA models and models developed in the study.

Subjects: 58 healthy elderly subjects (31 women, 27 men, 66.

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LCN1 gene encodes the tear lipocalin; the lipocalins are a large and growing family of proteins characterized by their ability to bind small hydrophobic molecules. We report here the location of a dinucleotide repeat microsatellite marker (D9S1826) close to LCN1 gene. Using the CEPH reference families, the position of LCN1 is located within the 9q34 genetic map between D9S23 and D9S158.

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The eyes are protected by the mechanical action of blinking and the washing action of tears; besides maintaining comfort and serving as the optical surface, the tear film forms the first line of defence. This role is mainly due to specific action of secretory immunoglobulins and continuous presence of unspecific proteins such as lysozyme, lactoferrin and tear lipocalin.

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One-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (1D-SDS PAGE) of the non-denatured low molecular weight (MW) tear proteins (dilution in phosphate buffered saline or in the non-ionic detergent Triton X100) revealed no protein G but a strongly marked 23-kD related to a tear specific prealbumin (TSP) subunit coming with the known 15, 17, 18 and 20-kD TSP subunits. Under mild denaturating conditions of sample preparation with SDS dilution just before electrophoresis, 23-kD protein decreased and a faint 32-kD protein G appeared. Under stronger denaturing conditions of sample preparation with SDS treatment (boiling or freeze-thaw cycles), 23-kD protein disappeared and two main protein G forms (32 and 34-kD) and additional bands (29, 36, 39, 42, 57 and 60-kD) appeared depending on the sample treatment.

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A rapid two-dimensional electrophoretic system for evaluating the penetration of proteins into hydrogels (used as contact lenses) is presented. The proteins are sieved through the hydrogel under conditions which produce minimum deformity of pores. In another step, the proteins migrating through the pores are identified.

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The rabbit defense system has a number of specific features: no lactoferrin and lysozyme are detectable and peroxidase activity is only demonstrated in the cubic epithelial cells of the ducts. Experiments carried out with radioactive amino acid, demonstrate the absence of secreted proteins with molecular weights corresponding to those of albumin and transferrin, indicating that these proteins are not synthesized by the lacrimal gland tissue. Rabbit tear pattern presents a set of acidic proteins secreted by the lacrimal gland tissue, with small molecular weight and acidic pI's.

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