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Tridimensional architecture of the Golgi apparatus in the atrial muscle cell of the rat.

The American journal of anatomy

metabolism, Thiamine Pyrophosphatase, Rats, Nucleotidases, ultrastructure, Myocardium, Models, Structural, Microscopy, Electron, Histocytochemistry, Heart Atria, enzymology, Golgi Apparatus, Animals

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      The tridimensional structure of the Golgi apparatus of atrial muscle cells has been studied in thin and thick sections with low- and high-voltage electron microscopes. Cardiac tissue was inpregnated with osmium, stained to demonstrate phosphate activity (i.e., nicotinamide adenine dinucleotide phosphatase or NADPase; thiamine pyrophosphatase or TPPase; cytidine monophosphatase or CMPase) or postfixed and stained with potassium ferrocyanide-reduced osmium. At low power, in thick (3-10 micron) sections, the cisosmiophilic element and the NADPase- and the TPPase-positive saccules each appeared as a continuous irregular ribbon that formed, at the two poles of the nucleus, two conical masses connected to each other by beltlike bands encircling the nucleus. At higher magnifications, the continuous Golgi apparatus showed saccular regions along its length connected by short intersaccular tubular regions. In the saccular regions, the following five superimposed elements formed a stack: (1) the cis-osmiophilic network of anastomosed tubules; (2) a chromophobic, dilated saccule perforated with numerous pores; (3) a thin NADPase-positive saccule showing few pores; (4) a thin TPPase-positive saccule perforated with numerous minute pores; and (5) a CMPase-positive transelement that showed saccular and tubular regions and was often partly separated from the overlying saccule. In the intersaccular tubular regions, membranous tubules connected and bridged saccules of two adjacent saccular regions. Secretory granules usually appeared in this region as dilations of the tubules connected to all elements of the Golgi stack except the cis-osmiophilic element.

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