Navegar

Colección

Datos Estadísticas

Artículo

La versión final de este artículo es de uso interno de la institución.
Consulte el artículo en la página del editor
Consulte la política de Acceso Abierto del editor

Abstract:

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.

Registro:

Documento: Artículo
Título:Development modulates the serum induced effect on the incorporation of [2-3H]mannose into chick optic lobe protein: The possible role of glia
Autor:Rossi, S.; Vargas, V.I.; Carminatti, H.
Filiación:Instituto de Investigaciones Bioquimicas Fundación Campomar, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Argentina
Palabras clave:leucine; mannose; protein; amino acid transport; animal tissue; article; blood brain barrier; brain injury; embryo; embryo development; gestational age; glia cell; hatching; nerve cell; newborn; nonhuman; optic lobe; pathogenesis; priority journal; serum; sugar transport; Aging; Animal; Blood; Cells, Cultured; Chick Embryo; Chickens; Culture Media; Glucosephosphates; Glycoproteins; Leucine; Mannose; Nerve Tissue Proteins; Neuroglia; Neurons; Superior Colliculus; Support, Non-U.S. Gov't; Tritium; Animalia
Año:1992
Volumen:21
Número:2
Página de inicio:281
Página de fin:286
DOI: http://dx.doi.org/10.1016/0197-0186(92)90159-O
Título revista:Neurochemistry International
Título revista abreviado:Neurochem. Int.
ISSN:01970186
CODEN:NEUID
CAS: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
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01970186_v21_n2_p281_Rossi

Referencias:

  • Alperin, Idoyaga-Vargas, Carminatti, Rate of protein glycosylation in rat cerebral cortex (1986) J. Neurochem., 47, pp. 355-362
  • Brunk, Jones, James, Assay for nanogram quantities of DNA in cellular homogenates (1979) Analyt. Biochem., 92, pp. 497-500
  • Catteral, The molecular basis of neuronal excitability (1984) Science, 23, pp. 653-661
  • 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
  • Dodd, Jessel, Axon induced patterning of neural projection in invertebrates (1988) Science, 242, pp. 692-699
  • Dubois, Gelles, Hamilton, Rebers, Smith, Colorimetric method for determination of sugars and related substances (1956) Analyt. Chem., 28, pp. 350-356
  • Edelman, Cell adhesion molecules in the regulation of animal form and tissue pattern (1986) Ann. Rev. Cell Biol., 2, pp. 81-116
  • Hamburger, Hamilton, A series of normal stages in the development of the chick embryo (1951) Journal of Morphology, 88, pp. 49-92
  • 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
  • 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
  • La Vail, Cowan, The development of the chick optic tectum I. Normal morphology and cytoarchitectonic development (1971) Brain Res., 28, pp. 391-419
  • La Vail, Cowan, Autoradiographic studies (1971) Brain Res., 28, pp. 421-441
  • Lowry, Rosebrough, Farr, Randall, Protein measurement with the Folin phenol reagent (1951) J. biol. Chem., 193, pp. 265-275
  • Margolis, Preti, Lai, Margolis, Developmental changes in brain glycoproteins (1976) Brain Res., 112, pp. 363-371
  • McGraw, McLaughlin, Fine structural studies of synaptogenesis in the superficial layers of the chick optic tectum (1980) J. Neurocytol., 9, pp. 79-93
  • 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
  • Morris, Thy-1 in the developing nervous tissue (1985) Dev. Neurosci., 7, pp. 133-160
  • 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
  • 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
  • Rothman, Lodish, Synchronized transmembrane insertion and glycosylation of a nascent membrane protein (1977) Nature, 269, pp. 775-778
  • 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
  • Silverman, Amenta, Sources of error in estimating radioactivity in protein from cell cultures by liquid scintillation counting (1984) Analyt. Biochem., 141, pp. 538-544
  • 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
  • Tildon, Stevenson, Decreased oxidation of labeled glucose by dissociated brain cells in the presence of fetal bovine serum (1984) Science, 224, pp. 903-904
  • Tildon, Stevenson, Roedes, Serum effects on substrate oxidation by dissociated brain cells: possible sites of action (1987) Brain Res., 403, pp. 127-135

Citas:

---------- APA ----------
Rossi, S., Vargas, V.I. & Carminatti, H. (1992) . Development modulates the serum induced effect on the incorporation of [2-3H]mannose into chick optic lobe protein: The possible role of glia. Neurochemistry International, 21(2), 281-286.
http://dx.doi.org/10.1016/0197-0186(92)90159-O
---------- CHICAGO ----------
Rossi, S., Vargas, V.I., Carminatti, H. "Development modulates the serum induced effect on the incorporation of [2-3H]mannose into chick optic lobe protein: The possible role of glia" . Neurochemistry International 21, no. 2 (1992) : 281-286.
http://dx.doi.org/10.1016/0197-0186(92)90159-O
---------- MLA ----------
Rossi, S., Vargas, V.I., Carminatti, H. "Development modulates the serum induced effect on the incorporation of [2-3H]mannose into chick optic lobe protein: The possible role of glia" . Neurochemistry International, vol. 21, no. 2, 1992, pp. 281-286.
http://dx.doi.org/10.1016/0197-0186(92)90159-O
---------- VANCOUVER ----------
Rossi, S., Vargas, V.I., Carminatti, H. Development modulates the serum induced effect on the incorporation of [2-3H]mannose into chick optic lobe protein: The possible role of glia. Neurochem. Int. 1992;21(2):281-286.
http://dx.doi.org/10.1016/0197-0186(92)90159-O