Distinct Cellular Localization of Membrane-Bound and Soluble Forms of Catechol-O-Methyltransferase in Brain
Article first published online: 12 DEC 2006
Journal of Neurochemistry
Volume 40, Issue 1, pages 215–219, January 1983
How to Cite
Rivett, A. J., Francis, A. and Roth, J. A. (1983), Distinct Cellular Localization of Membrane-Bound and Soluble Forms of Catechol-O-Methyltransferase in Brain. Journal of Neurochemistry, 40: 215–219. doi: 10.1111/j.1471-4159.1983.tb12673.x
- Issue published online: 12 DEC 2006
- Article first published online: 12 DEC 2006
- Received March 16, 1982; accepted June 30, 1982.
- Kainic acid;
- Cellular localization;
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.