A role for microglial cells in reshaping neuronal circuitry of the adult rat auditory brainstem after its sensory deafferentation

2014 ◽  
Vol 92 (4) ◽  
pp. 432-445 ◽  
Author(s):  
Philipp Janz ◽  
Robert-Benjamin Illing
Keyword(s):  
Auditory Brainstem ◽  
Microglial Cells ◽  
Neuronal Circuitry ◽  
Adult Rat

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

1990 ◽  
Vol 38 (11) ◽  
pp. 1535-1539 ◽  
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.

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.

Rate and frequency interactions in the auditory brainstem response of the adult rat

1992 ◽  
Vol 60 (1) ◽  
pp. 73-79 ◽  
Author(s):  
Elizabeth H. Newton ◽  
William A. Cooper ◽  
James R. Coleman
Keyword(s):  
Auditory Brainstem Response ◽  
Auditory Brainstem ◽  
Adult Rat ◽  
Brainstem Response

Immunoenzymatic demonstration of the simultaneous presence of transferrin, hemopexin and albumin in a same hepatocyte and their ultrastructural localization

1978 ◽  
Vol 36 (2) ◽  
pp. 88-89
Author(s):  
M. Kraemer ◽  
J. Foucrier ◽  
J. Vassy ◽  
M.T. Chalumeau
Keyword(s):  
Plasma Proteins ◽  
Rat Hepatocytes ◽  
Ultrastructural Localization ◽  
Carrier Proteins ◽  
Normal Cells ◽  
Adult Rat ◽  
Adult Rat Hepatocytes ◽  
Monospecific Antisera ◽  
Different Levels

Some authors using immunofluorescent techniques had already suggested that some hepatocytes are able to synthetize several plasma proteins. In vitro studies on normal cells or on cells issued of murine hepatomas raise the same conclusion. These works could be indications of an hepatocyte functionnal non-specialization, meanwhile the authors never give direct topographic proofs suitable with this hypothesis.The use of immunoenzymatic techniques after obtention of monospecific antisera had seemed to us useful to bring forward a better knowledge of this problem. We have studied three carrier proteins (transferrin = Tf, hemopexin = Hx, albumin = Alb) operating at different levels in iron metabolism by demonstrating and localizing the adult rat hepatocytes involved in their synthesis.Immunological, histological and ultrastructural methods have been described in a previous work.

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