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Ultrastructural localization of cytochrome oxidase and monoamine oxidase on microcylinders, a Long-Evans rat-specific mitochondrial inclusion

OY Pin and HS Lin

Department of Anatomy, College of Medicine, National Taiwan University, Taipei, Republic of China.

The presence of a unique inclusion body, the microcylinder, in the intracristal space of mitochondria was previously reported in various types of cells from spotted rats of the Long-Evans strain, but was not found in cells of albino rats. The microcylinder is about 30 nm in diameter and of indefinite length, and is composed of six filamentous subunits surrounding a central one. We performed electron microscopic cytochemical studies on the cells of uriniferous tubules and the corpus striatum in normal spotted rats of the Long-Evans strain and albino rats of Wistar and Sprague-Dawley strains. On the basis of oxidative polymerization of 3, 3'-diaminobenzidine by cytochrome oxidase (CYO) an cupric ferrocyanide deposition by monoamine oxidase (MAO), microcylinders were demonstrated to exhibit activity of these enzymes. Reaction products of other mitochondrial enzymes, such as succinate dehydrogenase and lactate dehydrogenase, were not deposited on microcylinders. We conclude that microcylinders are rat strain-specific mitochondrial inclusions and consist of protein components, particularly containing the mitochondrial enzymes CYO and MAO.

Volume 39, Issue 2, pp. 205-212, 02/01/1991
Copyright © 1991 by The Histochemical Society


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