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Biomedical subjects

Y Courtois

Publications and source records attributed to Y Courtois.

At least 235 records · Page 13Linked to original sources
PubMed1976

Surface labelling of senescent chick fibroblasts by lactoperoxidase-catalysed iodination.

Cell surface of chick fibroblasts were labelled by a short treatment with 125I in presence of lactoperoxidase. A glycoprotein (220,000 molec. wt) was iodinated and was present in a more exposed position or in greater amounts at the surface of old phase III cells compared to young phase II cells. The findings extend our previous observations on cell surface modifications in in vitro senescing fibroblasts.

Aging↗
PubMed1976

Age dependence of the biosynthesis of intercellular matrix macromolecules of rabbit aorta in organ culture and cell culture.

The age dependence of the relative rate of biosynthesis of intercellular matrix macromolecules was studied in organ culture and cell culture obtained from aortas of newborn, young and adult rabbits. In organ culture there was a strong decrease with age of the rate of incorporation of (14C)-lysine and (3H)-glucosamine in all macromolecular fractions. Neosynthesis of elastin could be demonstrated by the isolation of labelled demosine at all ages. In cell cultures derived from newborn and adult aortas, no decrease in total incorporation was noticed. The pattern of synthesis and secretion of glycosaminoglycans and glycoproteins did however change with age. These results suggest the existence of matrix-dependent and of a matrix-independent regulation of the relative rate of synthesis of matrix macromolecules.

Aging↗
PubMed1975

Lens glycoproteins: biosynthesis in cultured epithelial cells of bovine lens.

1. Radioactivity from [3H]glucosamine is rapidly incorporated into cellular fractions of lens epithelial cells cultured in vitro. The incorporated isotope appears largely in glycoproteins of the cell surface that are exposed to trypsin and are released into a soluble form by proteolysis of intact cells. Glycoproteins are also secreted by cultured cells and can be recovered in the culture fluids. Sodium dodecysulphate-polyacrylamide gell electrophoresis shows that a range of glycoproteins with apparent molecular weights from approximately 14000 to 120000 are present. The relationships of these glycoproteins to collagen and the non-collagenous glycoproteins of lens basement membranes are discussed. 2. A plasma membrane fraction obtained from non-trypsinised lens epithelial cells contains one major glycoprotein of apparent molecular weight 120000. A major non-glycosylated polypeptide of molecular weight about 38000 detectable by Bloemendal et al. (1972) in plasma membranes of differentiated lens fibre cells was not prominent in lens epithelial cell membranes. 3. Examination of lens basement membranes extracted in various ways failed to reveal major glycoproteins of low molecular weight. Higher molecular weight glycoproteins, some of them related to collagen, were present.

Animals↗
PubMed1975

[Biosynthesis of macromolecules of the intercellular matrix in aorta organ culture. Influence of the age of the animal].

Rabbit aorta organ cultures were used as a model for the study of the modifications of the rate of biosynthesis of intercellular matrix macromolecules with age. Aortas of new born (100 g), young (400 g) and adult (2 kg) rabbits were maintained in culture for several weeks. 14C-lysine is incorporated in all the macromolecular fractions of the aortas, even in polymeric elastin. The change with age of the distribution of proteins of the aorta-explants in successive extracts obtained by a "chemical dissection" procedure and the decrease of their specific radioactivity wtih age enabled us to characterise biochemically the "aging program" of the arterial wall.

Age Factors↗
PubMed1969

Interaction entre pigments et acides nucleiques Etude sur l'interaction de l'Actinomycine D avec les nucléosides par Dichroïsme Circulaire.

The interaction of Actinomycin C(1) (AM) with purine nucleosides was investigated by circular dichroism. While dG and dGMP show identical interactions, rG, rGMP and 8-aza-GMP show lower tendency for complex formation. ara-G shows no complex formation. 6-Thio-GMP shows the strongest affinity for AM in accordance with previous results. Substitution on N-7 (methylation, protonation) or C-8 (8-Br-rG, 8-SH-rG) eliminate completely the complexing capacity. Another type of weaker complexes is formed by dA, dAMP and rIMP, indicated by the appearance of a positive band at 440 nm. It is concluded that in these complexes both the electron donor capacity of the purine base as well as the steric flexibility of the sugar around the glycosidic linkage determine their complexing capacity.

Journal Article↗
PubMed1968

pH induced changes in optical activity of guanine nucleosides.

Optical rotatory dispersion and circular dichroism have been used to investigate the protonation of guanosine and some of its analogues. An inversion of the principal Cotton effect and the dichroic band is observed below the acid pK. It is suggested that a conformational change from the anti form above the pK to the syn form below the pK occurs. The reasons why this change should occur only in guanosine and not in adenosine are discussed.

Journal Article↗