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• W1989501440 abstract "These cytochemical studies have shown that there are two distinct morphological types of primary lysosomes in the rat left ventricular mural myocardial cells, those with granular matrices and those with membranous matrices, which showed differences in acid hydrolase activity. Two different pathways of synthesis, transport, and packaging of primary lysosomes were indicated: (1) In the nuclear pole zone synthesis either occurs in the cisternae of the rough ER or granular regions of the nuclear envelope. Transport may occur from either the agranular regions of the nuclear membrane or directly from other elements of the smooth ER to the Golgi for packaging. Release appears to occur from the cisternal swollen end sacs. (2) In regions of the cell far removed from the nuclear pole zone, acid hydrolases, after synthesis in the rough ER, appear to be transported, packaged, and released as primary lysosomes directly from elements of the smooth ER, bypassing the Golgi, thus providing a more direct route for activity at distant sites within the cell. Lysosomal degradation of mitochondria in autophagic vacuoles occurs by two different mechanisms: (1) The more common involves progressive densification of the matrix, concomitant loss of cristae and outer and inner membranes, followed by further degradation to residual bodies; (2) The second and less common mechanism occurs in secondary lysosomes with much residual material and involves clarification of the mitochondrial matrix, followed by loss of the outer mitochondrial membrane and disorganization of the cristal membranes. Degradation of lipid droplets occurs by lysosomal and autooxidative activity. Acid hydrolase activity in residual bodies clearly indicates their lysosomal origin." @default.
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• W1989501440 date "1974-01-01" @default.
• W1989501440 modified "2023-09-23" @default.
• W1989501440 title "An electron cytochemical study of mechanisms of lysosomal activity in the rat left ventricular mural myocardium" @default.
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• W1989501440 doi "https://doi.org/10.1016/s0022-5320(74)80018-3" @default.
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