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

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.

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Histochemical demonstration of purine nucleoside phosphorylase (PNPase) in microglial and astroglial cells of adult rat brain.

Journal of Histochemistry & Cytochemistry ◽

10.1177/38.11.2120328 ◽

1990 ◽

Vol 38 (11) ◽

pp. 1535-1539 ◽

Cited By ~ 16

Author(s):

B Castellano ◽

B González ◽

B R Finsen ◽

J Zimmer

Keyword(s):

Rat Brain ◽

Glial Cells ◽

Purine Nucleoside Phosphorylase ◽

Purine Nucleoside ◽

Microglial Cells ◽

Histochemical Localization ◽

Astroglial Cells ◽

Nucleoside Phosphorylase ◽

Adult Rat ◽

Adult Rat Brain

The histochemical localization of enzymes associated with purine nucleoside metabolism indicates that glial cells might participate in the regulation of these compounds in the central nervous system. In the present study we examined the histochemical localization of purine nucleoside phosphorylase (PNPase) in sections from adult rat brain. Some sections were also sequentially stained immunocytochemically for astroglial or microglial cells utilizing glial fibrillary acidic protein (GFAP) or OX-42 antibodies, respectively. Our observations showed that PNPase was restricted to glial cells, whereas neurons always remained negative. Brain sections stained for both PNPase and GFAP showed that the GFAP-positive astroglial cells were always PNPase positive. Other PNPase-positive but GFAP-negative cells were also observed. These cells resembled microglial cells, and brain sections reacted for both PNPase and OX-42 confirmed this by showing that the major part of OX-42-positive microglial cells were PNPase positive. In these sections, the PNPase-positive but OX-42-negative cells present resembled astroglial cells. From our double staining experiments, we conclude that PNPase is present in both astroglial and microglial cells in normal adult brain.

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

Archives of Biological Sciences ◽

10.2298/abs0804581d ◽

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.

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Glial cells from normal adult rat brain established in continuous culture

Brain Research ◽

10.1016/0006-8993(78)91041-7 ◽

1978 ◽

Vol 155 (2) ◽

pp. 418-421 ◽

Cited By ~ 33

Author(s):

Vijendra K. Singh ◽

Diane Van Alstyne

Keyword(s):

Continuous Culture ◽

Rat Brain ◽

Glial Cells ◽

Normal Adult ◽

Adult Rat ◽

Adult Rat Brain

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

Biochemical Journal ◽

10.1042/bj1540559 ◽

1976 ◽

Vol 154 (2) ◽

pp. 559-560 ◽

Cited By ~ 9

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.

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Heat shock induces c-fos protein-like immunoreactivity in glial cells in adult rat brain

Experimental Neurology ◽

10.1016/0014-4886(89)90152-0 ◽

1989 ◽

Vol 106 (1) ◽

pp. 105-109 ◽

Cited By ~ 29

Author(s):

M. Dragunow ◽

R.W. Currie ◽

H.A. Robertson ◽

R.L.M. Faull

Keyword(s):

Heat Shock ◽

Rat Brain ◽

Glial Cells ◽

Adult Rat ◽

Fos Protein ◽

Adult Rat Brain

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Distribution of Aquaporin 9 in the adult rat brain: Preferential expression in catecholaminergic neurons and in glial cells

Neuroscience ◽

10.1016/j.neuroscience.2004.05.042 ◽

2004 ◽

Vol 128 (1) ◽

pp. 27-38 ◽

Cited By ~ 111

Author(s):

J. Badaut ◽

J.-M. Petit ◽

J.-F. Brunet ◽

P.J. Magistretti ◽

C. Charriaut-Marlangue ◽

...

Keyword(s):

Rat Brain ◽

Glial Cells ◽

Preferential Expression ◽

Catecholaminergic Neurons ◽

Adult Rat ◽

Aquaporin 9 ◽

Adult Rat Brain

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

Biochemical Journal ◽

10.1042/bj1540529 ◽

1976 ◽

Vol 154 (2) ◽

pp. 529-539 ◽

Cited By ~ 27

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.

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