Distinct Cellular Localization of Membrane‐Bound and Soluble Forms of Catechol‐O‐Methyltransferase in Brain

A. Jennifer Rivett, Andrew Francis, Jerome A. Roth

Research output: Contribution to journalArticle

96 Scopus citations

Abstract

Abstract: 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 Km membrane‐bound catechol‐O‐methyltransferase may be localized predominantly in neurons, whereas the high‐Km soluble enzyme is found in glial cells.

Original languageEnglish (US)
Pages (from-to)215-219
Number of pages5
JournalJournal of neurochemistry
Volume40
Issue number1
DOIs
StatePublished - Jan 1983

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Cellular and Molecular Neuroscience

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