Inhibitory effect of colchicine on amylase secretion by rat parotid glands possible localization in the golgi area.

Content Provider	CiteSeerX
Author	Patzelt, Christoph Brown, Dennis Jeanrenaud, Bernard
Abstract	Colchicine inhibited amylase secretion by isolated rat parotid glands only 6 h after administration of the drug in vivo. This delayed effect was not the result of the inability of the drug to reach its reaction site. When parotid glands were emptied of their secretory granules by isoproterenol treatment, the subsequent replenishment of cells with granules was inhibited by colchicine. Colchicine concomitantly produced alterations of the Golgi complexes, the cisternae of which were reduced in size and surrounded by clusters of microvesicles. Incubation of parotid glands with colchicine for prolonged durations failed to alter stored amylase secretion as stimulated by isoproterenol, but it inhibited the release of de novo synthesized enzyme. Colchicine-binding activity of high speed supernatant parotid gland homogenates, likely to represent cytosolic microtubular protein, was similar to that of brain. Another colchicine-binding activity, firmly bound to the particulate fraction of homogenates, was found, of which a part may represent membranelocated microtubular protein. An assembly-disassembly cycle of microtubules
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Subject Keyword	Golgi Area Colchicine-binding Activity Parotid Gland Secretory Granule Golgi Complex Reaction Site Prolonged Duration Subsequent Replenishment Amylase Secretion Isoproterenol Treatment Stored Amylase Secretion Delayed Effect Assembly-disassembly Cycle Microtubular Protein Isolated Rat Parotid Cytosolic Microtubular Protein Particulate Fraction
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