Development modulates the serum induced effect on the incorporation of [2-3H]mannose into chick optic lobe protein: The possible role of glia

Recently, we described that serum decreases tritiated mannose incorporation into protein in the chick optic lobe at 18 days of embryonic age (Rossi et al., 1990). In this paper, we found a strikingly different response of this serum effect according to age. The data obtained showed no serum induced...

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Autor principal: Rossi, S.
Otros Autores: Vargas, V.I, Carminatti, H.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1992
Acceso en línea:Registro en Scopus
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Registro en la Biblioteca Digital
Aporte de:Registro referencial: Solicitar el recurso aquí
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024 7 |2 cas  |a 2-deoxyglucose-6-phosphate, 3573-50-0; Culture Media; Glucosephosphates; Glycoproteins; Leucine, 61-90-5; Mannose, 31103-86-3; Nerve Tissue Proteins; Tritium, 10028-17-8 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a NEUID 
100 1 |a Rossi, S. 
245 1 0 |a Development modulates the serum induced effect on the incorporation of [2-3H]mannose into chick optic lobe protein: The possible role of glia 
260 |c 1992 
270 1 0 |m Carminatti, H.; Instituto de Investigaciones Bioquimicas Fundación Campomar, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos AiresArgentina 
506 |2 openaire  |e Política editorial 
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504 |a Brunk, Jones, James, Assay for nanogram quantities of DNA in cellular homogenates (1979) Analyt. Biochem., 92, pp. 497-500 
504 |a Catteral, The molecular basis of neuronal excitability (1984) Science, 23, pp. 653-661 
504 |a Cowan, Martin, Wenger, Mitotic patterns in the optic tectum of the chick during normal development and after early removal of the optic vesicle (1968) J. exp. Zool., 169, pp. 71-92 
504 |a Dodd, Jessel, Axon induced patterning of neural projection in invertebrates (1988) Science, 242, pp. 692-699 
504 |a Dubois, Gelles, Hamilton, Rebers, Smith, Colorimetric method for determination of sugars and related substances (1956) Analyt. Chem., 28, pp. 350-356 
504 |a Edelman, Cell adhesion molecules in the regulation of animal form and tissue pattern (1986) Ann. Rev. Cell Biol., 2, pp. 81-116 
504 |a Hamburger, Hamilton, A series of normal stages in the development of the chick embryo (1951) Journal of Morphology, 88, pp. 49-92 
504 |a Idoyaga-Vargas, Carminatti, Glycosylation of endogenous protein(s) of the rough and smooth microsomes by a lipid sugar intermediate (1977) Molecular and Cellular Biochemistry, 16, pp. 171-176 
504 |a Keilhauer, Faissner, Schachner, Differential inhibition of neurone-neurone, neurone-astrocyte and astrocyte-astrocyte adhesion by L1, L2 and N-CAM antibodies (1985) Nature (Lond.), 316, pp. 728-730 
504 |a La Vail, Cowan, The development of the chick optic tectum I. Normal morphology and cytoarchitectonic development (1971) Brain Res., 28, pp. 391-419 
504 |a La Vail, Cowan, Autoradiographic studies (1971) Brain Res., 28, pp. 421-441 
504 |a Lowry, Rosebrough, Farr, Randall, Protein measurement with the Folin phenol reagent (1951) J. biol. Chem., 193, pp. 265-275 
504 |a Margolis, Preti, Lai, Margolis, Developmental changes in brain glycoproteins (1976) Brain Res., 112, pp. 363-371 
504 |a McGraw, McLaughlin, Fine structural studies of synaptogenesis in the superficial layers of the chick optic tectum (1980) J. Neurocytol., 9, pp. 79-93 
504 |a Merlie, Sebbane, Gardener, Olson, Lindstrom, The regulation of acetylcholine receptor expression in mammalian muscle (1983) Cold Spring Harbor Symp. Quant. Biol. XLVIII, pp. 136-146 
504 |a Morris, Thy-1 in the developing nervous tissue (1985) Dev. Neurosci., 7, pp. 133-160 
504 |a Rossi, Idoyaga-Vargas, Carminatti, An improved micromethod of incubation for the study of glycoprotein biosynthesis in the central nervous system (1989) Analyt. Asoc. Quimica Argentina, 77, pp. 35-40 
504 |a Rossi, Idoyaga-Vargas, Carminatti, Novel effect of serum on the incorporation of [2-3H]mannose into dolichol-bound carbohydrates and proteins (1990) Neurochem. Int., 16, pp. 295-300 
504 |a Rothman, Lodish, Synchronized transmembrane insertion and glycosylation of a nascent membrane protein (1977) Nature, 269, pp. 775-778 
504 |a Sellinger, Azcurra, Johnson, Ohlsson, Lodin, Independence of protein synthesis and drug uptake in nerve cell bodies and glial cells isolated by a new technique (1971) Nature New Biol., 230, pp. 253-256 
504 |a Silverman, Amenta, Sources of error in estimating radioactivity in protein from cell cultures by liquid scintillation counting (1984) Analyt. Biochem., 141, pp. 538-544 
504 |a Sokoloff, Reivich, Kennedy, Des Rosiers, Patlak, Pettigrew, Sakurada, Shinokara, The [14C]deoxyglucose method for the measurement of local cerebral glucose utilization: theory, procedure and normal values in the conscious and anesthetized albino rat (1977) J. Neurochem., 28, pp. 897-916 
504 |a Tildon, Stevenson, Decreased oxidation of labeled glucose by dissociated brain cells in the presence of fetal bovine serum (1984) Science, 224, pp. 903-904 
504 |a Tildon, Stevenson, Roedes, Serum effects on substrate oxidation by dissociated brain cells: possible sites of action (1987) Brain Res., 403, pp. 127-135 
520 3 |a Recently, we described that serum decreases tritiated mannose incorporation into protein in the chick optic lobe at 18 days of embryonic age (Rossi et al., 1990). In this paper, we found a strikingly different response of this serum effect according to age. The data obtained showed no serum induced decrease in 6-10-day-old embryo. In addition, our results demonstrate that the differential response of the tissue to the serum is independent of the rate of sugar entry into nerve cells. Furthermore, we also report that the variation of mannose or leucine incorporation into protein coincides very closely with the pattern of protein and glycoprotein accumulation during chick optic lobe development. Finally, data were obtained to define glial cells as the cellular target of the serum induced effect. This finding may contribute to elucidate the mechanism of cellular pathogenesis of cerebral lesions that occur after the breakdown of the blood brain barrier, such as in some diseases or during bleeding after injuries. © 1992.  |l eng 
593 |a Instituto de Investigaciones Bioquimicas Fundación Campomar, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Argentina 
690 1 0 |a LEUCINE 
690 1 0 |a MANNOSE 
690 1 0 |a PROTEIN 
690 1 0 |a AMINO ACID TRANSPORT 
690 1 0 |a ANIMAL TISSUE 
690 1 0 |a ARTICLE 
690 1 0 |a BLOOD BRAIN BARRIER 
690 1 0 |a BRAIN INJURY 
690 1 0 |a EMBRYO 
690 1 0 |a EMBRYO DEVELOPMENT 
690 1 0 |a GESTATIONAL AGE 
690 1 0 |a GLIA CELL 
690 1 0 |a HATCHING 
690 1 0 |a NERVE CELL 
690 1 0 |a NEWBORN 
690 1 0 |a NONHUMAN 
690 1 0 |a OPTIC LOBE 
690 1 0 |a PATHOGENESIS 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a SERUM 
690 1 0 |a SUGAR TRANSPORT 
690 1 0 |a AGING 
690 1 0 |a ANIMAL 
690 1 0 |a BLOOD 
690 1 0 |a CELLS, CULTURED 
690 1 0 |a CHICK EMBRYO 
690 1 0 |a CHICKENS 
690 1 0 |a CULTURE MEDIA 
690 1 0 |a GLUCOSEPHOSPHATES 
690 1 0 |a GLYCOPROTEINS 
690 1 0 |a LEUCINE 
690 1 0 |a MANNOSE 
690 1 0 |a NERVE TISSUE PROTEINS 
690 1 0 |a NEUROGLIA 
690 1 0 |a NEURONS 
690 1 0 |a SUPERIOR COLLICULUS 
690 1 0 |a SUPPORT, NON-U.S. GOV'T 
690 1 0 |a TRITIUM 
690 1 0 |a ANIMALIA 
700 1 |a Vargas, V.I. 
700 1 |a Carminatti, H. 
773 0 |d 1992  |g v. 21  |h pp. 281-286  |k n. 2  |p Neurochem. Int.  |x 01970186  |w (AR-BaUEN)CENRE-6251  |t Neurochemistry International 
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856 4 0 |u https://doi.org/10.1016/0197-0186(92)90159-O  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_01970186_v21_n2_p281_Rossi  |y Handle 
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