scholarly journals Pattern of chondroitin sulfate proteoglycan expression after ablation of the sensorimotor cortex of the neonatal and adult rat brain

2008 ◽  
Vol 60 (4) ◽  
pp. 581-591
Author(s):  
Sanja Dacic ◽  
Sanja Pekovic ◽  
Maja Stojiljkovic ◽  
Irena Lavrnja ◽  
Danijela Stojkov ◽  
...  
Keyword(s):  
Chondroitin Sulfate ◽  
Rat Brain ◽  
Sensorimotor Cortex ◽  
Immunohistochemical Analysis ◽  
Recovery Process ◽  
Adult Brain ◽  
Sulfate Proteoglycan ◽  
Adult Rats ◽  
Adult Rat ◽  
Adult Rat Brain

The central nervous system has a limited capacity for self-repair after damage. However, the neonatal brain has agreater capacity for recovery than the adult brain. These differences in the regenerative capability depend on local environmental factors and the maturational stage of growing axons. Among molecules which have both growth-promoting and growth-inhibiting activities is the heterogeneous class of chondroitin sulfate proteoglycans (CSPGs). In this paper, we investigated the chondroitin-4 and chondroitin-6 sulfate proteoglycan expression profile after left sensorimotor cortex ablation of the neonatal and adult rat brain. Immunohistochemical analysis revealed that compared to the normal uninjured cortex, lesion provoked up regulation of CSPGs showing a different pattern of expression in the neonatal vs. the adult brain. Punctuate and membrane-bound labeling was predominate after neonatal lesion, where as heavy deposition of staining in the extracellular matrix was observed after adult lesion. Heavy deposition of CSPG immunoreactivity around the lesionsite in adult rats, in contrast to a less CSPG-rich environment in neonatal rats, indicated that enhancement of the recovery process after neonatal injury is due to amore permissive environment.

scholarly journals Competition of glycerol with other oxidizable substrates in rat brain

1986 ◽  
Vol 237 (1) ◽  
pp. 47-51 ◽  
Author(s):  
M C McKenna ◽  
L I Bezold ◽  
S J Kimatian ◽  
J T Tildon
Keyword(s):  
Rat Brain ◽  
Glutamine Metabolism ◽  
Glycerol Oxidation ◽  
Adult Rats ◽  
Adult Rat ◽  
Rat Pups ◽  
Age Related ◽  
Adult Rat Brain ◽  
14Co2 Production ◽  
Age Related Changes

The rate of conversion of [1,3-14C]glycerol into 14CO2 was measured in the presence and absence of unlabelled alternative substrates in whole homogenates from the brains of young (4-6 and 18-20 days old) and adult rats. Unlabelled glucose decreased 14CO2 production from [1,3-14C]glycerol by about 40% at all ages studied. Unlabelled 3-hydroxybutyrate significantly decreased the 14CO2 production from both low (0.2 mM) and high (2.0 mM) concentrations of glycerol in 4-6- and 18-20-day-old rat pups. However, the addition of 3-hydroxybutyrate had no effect on the rate of 14CO2 production from 2.0 mM-glycerol in adult rats, suggesting that the interaction of 3-hydroxybutyrate with glycerol in adult rat brain is complex and may be related to the biphasic kinetics previously reported for glycerol oxidation. Unlabelled glutamine decreased the production of 14CO2 by brain homogenates from 18-20-day-old and adult rats, but not in 4-6-day-old rat pups. In the converse situation, the addition of unlabelled glycerol to whole brain homogenates had little effect on the rate of 14CO2 production from [6-14C]glucose, 3-hydroxy[3-14C]butyrate and [U-14C]glutamine, although some significant differences were noted. Collectively these results suggest that glycerol and these other substrates may be metabolized in separate subcellular compartments in brain such that the products of glucose, 3-hydroxybutyrate and glutamine metabolism can dilute the oxidation of glycerol, but the converse cannot occur. The data also demonstrate that there are complex age-related changes in the interaction of glycerol with 3-hydroxybutyrate and glutamine. The fact that glycerol oxidation was only partially suppressed by the addition of 1-5 mM-glucose, -3-hydroxybutyrate or -glutamine could also suggest that glycerol may be selectively utilized as an energy substrate in some discrete brain region.

scholarly journals Regional distribution of 5α-reductase type 2 in the adult rat brain: An immunohistochemical analysis

2013 ◽  
Vol 38 (2) ◽  
pp. 281-293 ◽  
Author(s):  
M. Paola Castelli ◽  
Alberto Casti ◽  
Angelo Casu ◽  
Roberto Frau ◽  
Marco Bortolato ◽  
...  
Keyword(s):  
Rat Brain ◽  
Regional Distribution ◽  
Immunohistochemical Analysis ◽  
Adult Rat ◽  
Adult Rat Brain

scholarly journals Activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in brains of adult and 7-day-old rats

1976 ◽  
Vol 154 (2) ◽  
pp. 559-560 ◽  
Author(s):  
M M. Sudjic ◽  
R Booth
Keyword(s):  
Rat Brain ◽  
Coenzyme A ◽  
Reductase Activity ◽  
Cholesterol Biosynthesis ◽  
Adult Brain ◽  
Adult Rat ◽  
Adult Rat Brain ◽  
Old Rats ◽  
Coa Reductase ◽  
Coenzyme A Reductase

Rat brain contains 3-hydroxy-3-methylglutaryl-CoA reductase activity, but this enzyme is far more active in 7-day-old brain than in adult brain. This difference may partly explain why cholesterol biosynthesis is more rapid in growing than in adult rat brain.

scholarly journals Demonstration of poly-N-acetyl lactosamine residues in ameboid and ramified microglial cells in rat brain by tomato lectin binding.

1994 ◽  
Vol 42 (8) ◽  
pp. 1033-1041 ◽  
Author(s):  
L Acarin ◽  
J M Vela ◽  
B González ◽  
B Castellano
Keyword(s):  
Rat Brain ◽  
Glial Cells ◽  
Lectin Histochemistry ◽  
Adult Brain ◽  
Microglial Cells ◽  
Electron Microscopic Level ◽  
Sugar Residue ◽  
Adult Rat ◽  
Tomato Lectin ◽  
Adult Rat Brain

This study was designed to demonstrate the localization of poly-N-acetyl lactosamine residues in postnatal and adult rat brain, visualized by their specific binding to a lectin obtained from Lycopersicon esculentum (tomato). Lectin histochemistry was carried out on cryostat, paraffin, and vibratome sections and was examined by light microscopy. Selected vibratome sections were processed for electron microscopy. Our results showed that tomato lectin histochemistry was found in relation to blood vessels and glial cells in both postnatal and adult rat brain. Since tomato lectin-positive glial cells did not show GFAP immunoreactivity and displayed the same morphological features and overall distribution as nucleoside diphosphatase (NDPase)-positive cells, they were consequently identified as microglial cells. At the electron microscopic level, both ameboid and ramified microglial cells displayed intracytoplasmic and plasma membrane lectin reactivity. In postnatal brain, ameboid microglial cells always showed stronger binding of tomato lectin compared with ramified microglial cells in the adult brain. The putative significance of this decrease in poly-N-acetyl lactosamine from ameboid to ramified microglial cells and the possible role(s) of this sugar residue are discussed.

scholarly journals Nucleo-cytoplasmic relationships of high-molecular-weight ribonucleic acid, including polyadenylated species, in the developing rat brain

1976 ◽  
Vol 154 (2) ◽  
pp. 529-539 ◽  
Author(s):  
W Berthold ◽  
L Lim
Keyword(s):  
Molecular Weight ◽  
Rat Brain ◽  
High Molecular Weight ◽  
18S Rrna ◽  
Electrophoretic Analysis ◽  
Adult Brain ◽  
Considerable Proportion ◽  
Adult Rat ◽  
Polyadenylated Rna ◽  
Adult Rat Brain

The metabolism of high-molecular-weight RNA in the nuclear and cytoplasmic fractions of newborn and adult rat brain was investigated after the intracranial administration of [32P]Pi. In young brain, a considerable proportion of the newly synthesized radioactive RNA is transferred to the cytoplasm, in contrast with the adult brain, where there appears to be a high intranuclear turnover. Electrophoretic analysis of the newly synthesized RNA showed that processing of the rRNA precursor to yield the 28S and 18S rRNA may be more rapid in the adult than in the young, although most of the adult rRNA in the nucleus is not transferred to the cytoplasm. In young brain, processing is probably tightly coupled to transport of rRNA into the cytoplasm, so that 28S and 18S rRNA are not subjected to possible degradation within the nucleus. Polyadenylated RNA turns over in concert with high-molecular-weight RNA in the nuclei of the adult rat brain. In the cytoplasm the polyadenylated RNA has a higher turnover rate relative to rRNA. In the young brain the polyadenylated RNA is transferred to the cytoplasm along with rRNA, although polyadenylated RNA is transported into the cytoplasm at a faster rate. The nuclear and cytoplasmic polyadenylated RNA species of young brain are larger than their corresponding adult counterparts. These results suggest that there are considerable changes in the regulation of the nucleo-cytoplasmic relationship of rRNA and polyadenylated RNA during the transition of the brain from a developing replicative phase to an adult differentiated and non-dividing state.

scholarly journals Immunohistochemical Analysis of Nucleotide Excision Repair Factors XPA and XPB in Adult Rat Brain

2008 ◽  
Vol 291 (7) ◽  
pp. 775-780 ◽  
Author(s):  
Shan-Zheng Yang ◽  
Yi-Fan Zhang ◽  
Ling-Mei Zhang ◽  
Ya-Ling Huang ◽  
Feng-Yan Sun
Keyword(s):  
Rat Brain ◽  
Nucleotide Excision Repair ◽  
Excision Repair ◽  
Immunohistochemical Analysis ◽  
Adult Rat ◽  
Nucleotide Excision ◽  
Adult Rat Brain

The BDNF content of postnatal and adult rat brain: the effects of 6-hydroxydopamine lesions in adult brain

1996 ◽  
Vol 97 (2) ◽  
pp. 297-303 ◽  
Author(s):  
Jiawei Zhou ◽  
Bernardo Pliego-Rivero ◽  
Henry F. Bradford ◽  
Gerald M. Stern
Keyword(s):  
Rat Brain ◽  
Adult Brain ◽  
Adult Rat ◽  
Adult Rat Brain ◽  
6 Hydroxydopamine

Immunohistochemical analysis of nuclear lamins in the glial cells of adult rat brain

2007 ◽  
Vol 58 ◽  
pp. S209
Author(s):  
Yasuharu Takamori ◽  
Tetsuji Mori ◽  
Taketoshi Wakabayashi ◽  
Hisao Yamada
Keyword(s):  
Rat Brain ◽  
Glial Cells ◽  
Immunohistochemical Analysis ◽  
Adult Rat ◽  
Nuclear Lamins ◽  
Adult Rat Brain

scholarly journals Acetoacetate metabolism in infant and adult rat brain in vitro

1970 ◽  
Vol 116 (4) ◽  
pp. 641-655 ◽  
Author(s):  
T. Itoh ◽  
J. H. Quastel
Keyword(s):  
Rat Brain ◽  
Brain Cortex ◽  
Brain Slices ◽  
Adult Brain ◽  
Adult Rat ◽  
Infant Rat ◽  
Rat Brain Cortex ◽  
Adult Rat Brain ◽  
Brain Cortex Slices ◽  
Cortex Slices

1. Acetoacetate or dl-β-hydroxybutyrate increases the rate of oxygen consumption to a smaller extent than that brought about by glucose or pyruvate in adult rat brain-cortex slices but to the same extent as that in infant rat brain-cortex slices. 2. The rate of 14CO2 evolution from [1-14C]glucose considerably exceeds that from [6-14C]glucose in respiring infant rat brain-cortex slices, in contrast with adult brain-cortex slices, suggesting that the hexose monophosphate shunt operates at a greater rate in the infant rat brain than in the adult rat brain. 3. The rate of 14CO2 evolution from [3-14C]acetoacetate or dl-β-hydroxy[3-14C]butyrate, in the absence of glucose, is the same in infant rat brain slices as in adult rat brain slices. It exceeds that from [2-14C]glucose in infant rat brain but is less than that from [2-14C]glucose in adult rat brain. 4. Acetoacetate is oxidized in the brain through the operation of the citric acid cycle, as shown by the accelerating effect of glucose on acetoacetate oxidation in adult brain slices, by the inhibitory effects of malonate in both infant and adult brain slices and by its conversion into glutamate and related amino acids in both tissues. 5. Acetoacetate does not affect glucose utilization in adult or infant brain slices. It inhibits the rate of 14CO2 formation from [2-14C]glucose or [U-14C]-glucose the effect not being wholly due to isotopic dilution. 6. Acetoacetate inhibits non-competitively the oxidation of [1-14C]pyruvate, the effect being attributed to competition between acetyl-CoA and CoA for the pyruvate-oxidation system. 7. Acetoacetate increases the rate of aerobic formation of lactate from glucose with both adult and infant rat brain slices. 8. The presence of 0.1mm-2,4-dinitrophenol diminishes but does not abolish the rate of 14CO2 formation from [3-14C]acetoacetate in rat brain slices. This points to the participation of ATP in the process of oxidation of acetoacetate in infant or adult rat brain. 9. The presence of 5mm-d-glutamate inhibits the rate of 14CO2 formation from [3-14C]acetoacetate, in the presence or absence of glucose. 10. Labelled amino acids are formed from [3-14C]acetoacetate in both adult and infant rat brain-cortex slices, but the amounts are smaller than those found with [2-14C]glucose in adult rat brain and greater than those found with [2-14C]glucose in infant rat brain. 11. Acetoacetate is not as effective as glucose as a precursor of acetylcholine in adult rat brain but is as effective as glucose in infant rat brain slices. 12. Acetoacetate or β-hydroxybutyrate is a more potent source of acetyl-CoA than is glucose in infant rat brain slices but is less so in adult rat brain slices.

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