Distribution of glutamine synthetase and glial fibrillary acidic protein and correlation of glutamine synthetase with glutamate decarboxylase in different regions of the rat central nervous system.

Abstract:

:The concentration of soluble glial fibrillary acidic (GFA) protein and the specific activity of glutamine synthetase (GS) were estimated in 11 central nervous system (CNS) regions of the 90-day-old rat. Marked differences were observed in the regional distribution of these astrocyte marker proteins. The striatum and spinal cord contained the lowest concentration (per g wet weight) of GFA protein and GS activity, respectively, while the olfactory bulbs had the highest level of both astrocytic proteins. Differences between the lowest and the highest values were 3-fold for GS and 4-fold for GFA protein. More significant was the marked variation in the ratio of GS to GFA protein in different CNS regions; the highest and lowest values were in the striatum and the spinal cord respectively, and the difference between the highest and the lowest value was about 5-fold. The spinal cord contained low GS and high GFA protein; on the other hand, the colliculi had high GS and relatively low GFA protein. Immunochemical detection of GS and GFA proteins in whole homogenates of different regions showed that the variation of the specific activities of GS and the concentration of soluble GFA protein were due to the differences in their absolute protein concentrations. In different regions of the brain the activity of GS was significantly correlated with that of glutamate decarboxylase, but not with that of choline acetyltransferase. These observations provide further evidence for differing biochemical properties of astrocytes from various CNS regions and for the involvement of GS in processes associated with amino acid neurotransmission.

journal_name

Brain Res

journal_title

Brain research

authors

Patel AJ,Weir MD,Hunt A,Tahourdin CS,Thomas DG

doi

10.1016/0006-8993(85)90708-5

subject

Has Abstract

pub_date

1985-04-01 00:00:00

pages

1-9

issue

1

eissn

0006-8993

issn

1872-6240

pii

0006-8993(85)90708-5

journal_volume

331

pub_type

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