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Distinct Cellular Localization of Membrane‐Bound and Soluble Forms of Catechol‐ O ‐Methyltransferase in Brain
Author(s) -
Rivett A. Jennifer,
Francis Andrew,
Roth Jerome A.
Publication year - 1983
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1983.tb12673.x
Subject(s) - catechol o methyl transferase , enzyme , biochemistry , glutamine synthetase , striatum , chemistry , catechol , kainic acid , glutamate decarboxylase , glutamate receptor , biology , medicine , endocrinology , dopamine , glutamine , amino acid , allele , receptor , gene
The cellular localization of the two forms of catechol‐ O ‐methyltransferase (COMT) was investigated by measuring their activities in rat striatum following unilateral stereotaxic injection of kainic acid, which causes degeneration of striatal neurons followed by proliferation of astroglial cells. Membrane‐bound COMT activity was decreased in the lesioned striatum, while soluble COMT activity was increased. There was a statistically significant correlation between the ratio of lesioned to control activity for membrane‐bound COMT and the neuronal marker enzyme glutamate decarboxylase. Similarly the increase in soluble COMT activity paralleled that of the astroglial marker enzyme, glutamine synthetase. These results indicate that the K m membrane‐bound catechol‐ O ‐methyltransferase may be localized predominantly in neurons, whereas the high‐K m soluble enzyme is found in glial cells.