Search PubMed⌕ Search

Biomedical subjects

G Vincendon

Publications and source records attributed to G Vincendon.

At least 91 records · Page 5Linked to original sources
PubMed1982

High affinity binding sites for gamma-hydroxybutyric acid in rat brain.

The existence of a specific synthesizing enzyme for gamma-hydroxybutyric acid in rat brain has recently been reported. Here, for the first time, we demonstrate the presence of a high affinity, apparently specific binding site for this compound in the same tissue. This binding does not require Na+ and takes place optimally at pH 5.5. The bound gamma-hydroxybutyric acid is not displacable by GABA or baclofen. We report here on some structurally related compounds of GHB with a similar or better binding capacity than GHB itself. The number of binding sites increases with age up to adulthood and differs depending on the brain region. In primary tissue cultures of pure chicken neurones and glia, gamma-hydroxybutyric acid binding occurs exclusively in the neuronal preparations.

Animals↗
PubMed1982

Immunocytochemical evidence for the existence of GABAergic neurons in the nucleus raphe dorsalis. Possible existence of neurons containing serotonin and GABA.

It has been established that nerve cell bodies of the nucleus raphe dorsalis (NRD) belong to ascending 5-hydroxytryptamine systems. These neurons could be modulated by GABAergic interneurons or interposed GABA neurons. A high glutamate decarboxylase (GAD) activity in the NRD and a specific high-affinity uptake mechanism for GABA suggest the presence of GABA synthesizing elements in the NRD. Anti-GAD antibodies were used by an immunocytochemical procedure to demonstrate the presence of GABAergic elements. Anti-GAD antibodies were previously tested in the cerebellum and substantia nigra. Large amounts of GAD-positive reaction product were observed in the cytoplasm of some neurons (fusiform, ovoid or multipolar) or appeared as punctate deposits apposed to dendrites, soma and dispersed in the neuropil of the NRD. At the electron microscopic level, GAD-positive reaction product was observed within the cytoplasm of numerous somata in sections from colchicine-treated rats. GAD-positive staining was observed in numerous fibers or axonal terminals and two types of morphologically different fibers could be distinguished. The first displays small clear vesicles and few large granular vesicles (LGV) (80-100 nm), the second displays only clear round vesicles (40-60 nm). After 5,7-dihydroxytryptamine treatment (a neurotoxic for 5-HT terminals), the immunocytochemical labeling is much decreased. Some reactive neurons are still dispersed in the nucleus but the fibers containing LGV are no longer observed. These results strongly suggest that some neuronal elements in the NRD are morphologically, pharmacologically and anatomically similar to 5-HT neurons described at this level. Such cell elements could possess a double GABA and 5-HT potentiality. If this is not the case, a population of GABA neurons could be sensitive to 5,7-DHT and so have the capacity to take up 5-HT. The other reactive elements, insensitive to 5,7-DHT, could represent the GABAergic interneurons postulated at this level. Numerous GAD positive fibers or axon terminals were observed in synaptic contact with dendrites, axons or soma of other neurons. The chemical nature of the neuronal postsynaptic elements remains unknown. These findings strongly support the hypothesis for GABA-mediated inhibition in the NRD.

Animals↗
PubMed1982

The importance of cell contact for the proliferation of neuroblasts in culture and its stimulation by meningeal extract.

The influence of cell density and cell contacts on the proliferation of neuroblasts in culture and its stimulation by meningeal extract were investigated. Dissociated brain cells from 6-day-old chick embryos were cultured under 3 different culture conditions to obtain dense or sparse brain cell cultures, as well as cultures of isolated neuronal cell. The proliferation fo neuroblasts, shown by morphological observations, cell counts, determinations of DNA content and measurements of [3H]thymidine incorporation, was found to be the highest in cultures where cell density and cellular contacts were greatest. The addition of meningeal extract stimulated the multiplication of neuroblasts only in cultures where the cells were in closer with each other. The results suggested, therefore, that cell density and cell-cell interactions are of importance and favored neuroblast proliferation.

Animals↗
PubMed1982

Immunoelectron microscopy of alpha 2-glycoprotein. An astrocyte-specific antigen.

The cellular and fine structural localization of the soluble brain-specific acidic alpha 2-glycoprotein was investigated using the indirect immunohistochemical method. The electron microscope was used to unambiguously identify cells containing the antigen. A single type of cell, the astrocyte, was found to be labelled with specific antisera directed against alpha 2-glycoprotein. Immunoperoxidase reaction product was found in astrocyte perikarya, their processes and perivascular end feet. It was found to be apparently associated with the cytoplasmic surface of mitochondria, reticular membranes and the plasma membrane. No specific labelling of neurones, oligodendrocytes, myelin or capillary endothelial cells was observed. The data is discussed in relation to the immunological properties of alpha 2-glycoprotein already reported.

Animals↗
PubMed1982

Cellular localization of the brain specific alpha 2-glycoprotein in rat cerebellum: an immunohistological study.

The cellular localization of the brain-specific, soluble, acidic alpha 2-glycoprotein was studied in rat cerebellum by using the immunoperoxidase technique at the light-and electron-microscopy levels with monospecific immune serum directed against this glycoprotein. Only astrocytes, their processes, and their end feet (subpial or perivascular) contained heavy immunoperoxidase reaction product. Cerebellar neurones, oligodendrocytes, myelin and blood vessel endothelia did not stain. Thus it appears that alpha 2-glycoprotein is an astrocyte marker.

Animals↗
PubMed1982

L-glutamate and L-glutamine uptake in adult rat cerebellum: an autoradiographic study.

The compartmentation of L-glutamate in the central nervous system has been extensively studied and L-glutamine is believed to be the precursor of the neuronal releasable pool of the L-glutamate. In order to localize the sites of uptake of both L-glutamate and L-glutamine, autoradiography was used in tissue slices of adult rat cerebellum, where granule cells are considered to be glutamatergic. Incubation of the tissue with low concentrations of [3H]L-glutamate or [3H]L-glutamine produces in both cases a heavy labelling of the molecular layer. [3H]L-glutamate uptake seems to be essentially glial (Golgi epithelial cells and Bergmann fibres) while [3H]L-glutamine is more diffusely distributed over the molecular layer. Although no conclusions can be drawn on the nature of L-glutamine uptake, these results are in agreement with the model which considers L-glutamate uptake by glial cells to be the inactivating process of glutamatergic synapses.

Animals↗
PubMed1982

Rat brain alpha-mannosidase: purification, properties, and interaction with its antibodies.

Alpha-D-Mannosidase (EC 3.2.1.24.) was purified to homogeneity from adult rat brain. The enzyme, of apparent molecular weight 397,000, appears to be formed of subunits of molecular weight 120,000 made of two protomers (62,000) bound by disulfide bridges. Isoelectric focusing gives two bands, of pI 5.40 and 5.15. Both isoenzymes seem to have the same pH curve (a small peak of activity at pH 4.5 and a maximum of activity around pH 6.0). These two isoenzymes are immunologically related.

Animals↗
PubMed1981

Isolation and immunohistochemical localization of a "Purkinje cell specific glycoprotein subunit from rat cerebellum.

The indirect immunohistochemical method has been used to determine the cellular localization of a Con A-binding glycoprotein subunit insoluble in Triton X-100, isolated from a rat cerebellar membrane pellet by Con A-Sepharose affinity chromatography and preparative PAGE electrophoresis in the presence of sodium dodecyl sulfate. This glycoprotein subunit (N-terminal amino acid Ala; MW 24,000 daltons) contains 24% carbohydrate (w/w) mainly mannose but also N-acetylglucosamine, galactose and sialic acid. At the optical level, the antiserum raised against this glycoprotein stains the whole Purkinje cell (dendrite, cell body and even the axon) but not the other cerebellar neurons. This staining is not eliminated when the antiserum is absorbed by rat forebrain or brain stem homogenates but is, in contrast, completely abolished by absorption with rat cerebellum homogenates. Thus, this antigen appears to be in the central nervous system exclusive to the cerebellum, and in the cerebellum specific for Purkinje cells. This antigen is present throughout the postnatal development of the rat cerebellum and the staining is already very strong at the fifth postnatal day.

Amino Acids↗
PubMed1981

Glycoproteins from adult rat brain synaptic vesicles. Fractionation on four immobilized lectins.

Glycoproteins obtained from large amounts of highly purified synaptic vesicles isolated from adult rat brain were fractionated by sequential affinity chromatography in the presence of SDS on four different immobilized lectins: concanavalin A, Ulex europeus lectin, Ricinus sanguinis lectin and wheat germ agglutinin. 83% of the total protein-bound sugar of synaptic vesicles can be adsorbed on the lectins and separated from the bulk of carbohydrate free proteins. Nine fractions containing only glycoproteins and differing by their terminal sugars were separated by analysed for their carbohydrate composition and electrophoretic profiles. A considerable heterogeneity of the glycoprotein population was observed which cannot be explained solely by the microheterogeneity of the glycans of the synaptic vesicle glycoproteins.

Animals↗
PubMed1981

Purification and properties of the membrane-bound acetylcholinesterase from adult rat brain.

The membrane-bound acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7) from adult rat brain has been purified to homogeneity using sequential affinity chromatography on Con A-Sepharose and on dimethyl-aminoethylbenzoic acid-Sepharose 4B followed by DEAE-cellulose chromatography. The yield of the purified enzyme (specific activity: 3068 U/mg protein) is higher than 50%. Polyacrylamide gel electrophoresis in the presence of Triton X-100 gives only one band with acetylcholinesterase activity. With the exception of electrofocusing and pore gradient electrophoresis, where a multiple band pattern was detected (which seems to be artefactual), the enzyme appears to be homogeneous. Gel filtration and sucrose density gradient centrifugation in the presence of Triton X-100 give only one symmetrical peak, with a calculated molecular weight of 328 000. Since polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS) and mercaptoethanol gives only one band with a molecular weight of 74 500, a tetrameric structure can be postulated for the membrane-bound acetylcholinesterase from rat brain.

Acetylcholinesterase↗
PubMed1981

Heterogeneity of rat brain acetylcholinesterase: a study by gel filtration and gradient centrifugation.

According to their solubilization properties, two classes of acetylcholinesterases (AChE) can be detected in the adult rat brain: a "soluble" species (easily solubilized without detergent), and a membrane-bound species (solubilized only in the presence of detergent). The latter was found to be homogeneous by gel filtration (Stokes radius 8.05 +/- 0.35 nm) and sucrose gradient centrifugation (9.75 +/- 0.2 S) in the presence of Triton X-100. The "soluble" AChE gives three stable species in the presence of the same detergent with Stokes radii and sedimentation constants of 10.9 +/- 0.5 nm and 16 +/- 2S; 6.75 +/- 0.30 nm, and 10.7 +/- 0.4 S; 5.37 +/- 0.35 nm and 4.37 +/- 0.1 S. Co-chromatography and co-sedimentation or the reduction and alkylation of disulfide bridges show that all the soluble species are different from the membrane-bound AChE. The possibility that soluble and membrane-bound AChE are completely different molecules is discussed.

Acetylcholinesterase↗