Fine structure and immunogold labeling of crystalline inclusion bodies in mitochondria
1988
Kim, S.J. | Lee, K.O. (Hallym Univ., Chunchon (Korea R.). Dept. of Biology) | Capaldi, Roderick A. (Univ. of Oregon (U.S.A.). Institute of Molecular Biology)
The distribution of respiratory chain complexes in beef heart and human muscle mitochondria has been explored by immunoelectron microscopy with antibodies made against beef heart mitochondrial proteins in conjunction with protein A colloidal gold (12nm particles). The antibodies used were made against NADH-conezyme Q reductase(complex I), ubi-quinol-cytochrome-c-oxidoreductase (complex III) and cytochrome-c-oxidase(complex IV). Labeling of beef heart tissue with any of these antibodies gave gold particles randomly distributed along the mitochondrial inner membrane. The labeling of muscle tissue mitochondria from a patient with a mitochondrial myopathy localized by biochemical analysis to complex III was quantitated and compared with the labeling of human control muscle tissue mitochondria. Four kinds of morphological changes in the mitochondrial fine structure in the myopaty patient tissue have been found; paracrystalline inclusions consisting of densely packed multilamellar structures, globular crystalline inclusions with high electron density, multilamellar structure inclusion body(compactly and irregularly arranged concentric whirl shaped cristae) and globular cyistalline inclusions located in the center of the whirl shaped cristae. Complex I and cytochrome-c-oxidase antibodies reacted to the same level in the mitochondria containing the crystalline inclusions and control mitochondria. Antibodies to complex III reacted very poorly to the mitochondria containing the crystalline inclusions but strongly to control mitchondria. The globular crystalline inclusions in the mitochondria are not reacted antibodies to respiratory chain complexes
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