Advanced

Neuronal and non-neuronal catechol-O-methyltransferase in primary cultures of rat brain cells

Karhunen, T.; Tilgmann, C. LU ; Ulmanen, I. and Panula, P. (1995) In International Journal of Developmental Neuroscience 13(8). p.825-834
Abstract

Previous biochemical and histochemical studies have suggested that catechol-O-methyltransferase (COMT) is a predominantly glial enzyme in the brain. The aim of this work was to study its localization and molecular forms in primary cultures, where cell types can be easily distinguished with specific markers. COMT immunoreactivity was studied in primary astrocytic cultures from newborn rat cerebral cortex, and in neuronal cultures from rat brain from 18-day-old rat embryos using antisera against rat recombinant COMT made in guinea pig. Double-staining studies with specific cell markers to distinguish astrocytes, neurons and oligodendrocytes were performed. COMT immunoreactivity colocalized with a specific oligodendrocyte marker... (More)

Previous biochemical and histochemical studies have suggested that catechol-O-methyltransferase (COMT) is a predominantly glial enzyme in the brain. The aim of this work was to study its localization and molecular forms in primary cultures, where cell types can be easily distinguished with specific markers. COMT immunoreactivity was studied in primary astrocytic cultures from newborn rat cerebral cortex, and in neuronal cultures from rat brain from 18-day-old rat embryos using antisera against rat recombinant COMT made in guinea pig. Double-staining studies with specific cell markers to distinguish astrocytes, neurons and oligodendrocytes were performed. COMT immunoreactivity colocalized with a specific oligodendrocyte marker galactocerebroside in cells displaying oligodendrocyte morphology, flat cells displaying type-1 astrocyte morphology and glial fibrillary acidic protein, in branched cells displaying type-2 astrocyte morphology and in cell bodies of neurons, the processes of which displayed neurofilament immunoreactivity. Western blots detected both soluble 24 kDa and membrane-bound 28-kDa COMT proteins in neuronal and astrocyte cultures. The results suggest that COMT is synthesized by cultured astrocytes, oligodendrocytes and neurons. © 1995.

(Less)
Please use this url to cite or link to this publication:
author
publishing date
type
Contribution to journal
publication status
published
keywords
astrocytes, catecholamines, oligodendrocytes
in
International Journal of Developmental Neuroscience
volume
13
issue
8
pages
10 pages
publisher
Elsevier
external identifiers
  • Scopus:0029586493
ISSN
0736-5748
DOI
10.1016/0736-5748(95)00070-4
language
English
LU publication?
no
id
f275dd5e-092a-4af5-82ff-f9ff3d0b0305
date added to LUP
2016-04-11 13:20:21
date last changed
2016-06-29 09:03:34
@misc{f275dd5e-092a-4af5-82ff-f9ff3d0b0305,
  abstract     = {<p>Previous biochemical and histochemical studies have suggested that catechol-O-methyltransferase (COMT) is a predominantly glial enzyme in the brain. The aim of this work was to study its localization and molecular forms in primary cultures, where cell types can be easily distinguished with specific markers. COMT immunoreactivity was studied in primary astrocytic cultures from newborn rat cerebral cortex, and in neuronal cultures from rat brain from 18-day-old rat embryos using antisera against rat recombinant COMT made in guinea pig. Double-staining studies with specific cell markers to distinguish astrocytes, neurons and oligodendrocytes were performed. COMT immunoreactivity colocalized with a specific oligodendrocyte marker galactocerebroside in cells displaying oligodendrocyte morphology, flat cells displaying type-1 astrocyte morphology and glial fibrillary acidic protein, in branched cells displaying type-2 astrocyte morphology and in cell bodies of neurons, the processes of which displayed neurofilament immunoreactivity. Western blots detected both soluble 24 kDa and membrane-bound 28-kDa COMT proteins in neuronal and astrocyte cultures. The results suggest that COMT is synthesized by cultured astrocytes, oligodendrocytes and neurons. © 1995.</p>},
  author       = {Karhunen, T. and Tilgmann, C. and Ulmanen, I. and Panula, P.},
  issn         = {0736-5748},
  keyword      = {astrocytes,catecholamines,oligodendrocytes},
  language     = {eng},
  number       = {8},
  pages        = {825--834},
  publisher    = {ARRAY(0x7de0da8)},
  series       = {International Journal of Developmental Neuroscience},
  title        = {Neuronal and non-neuronal catechol-O-methyltransferase in primary cultures of rat brain cells},
  url          = {http://dx.doi.org/10.1016/0736-5748(95)00070-4},
  volume       = {13},
  year         = {1995},
}