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- W85039860 abstract "Publisher Summary The secretion of lipoproteins and other serum proteins is greatly inhibited in colchicine-treated rats. The effect of colchicine on a number of cellular processes is related to its primary interaction with the microtubules. Golgi membranes are enriched with glycosyltransferases and play a role in the rapid renewal of plasma membrane—a process linked to exocytosis. Inhibition of exocytosis by colchicine is mediated through its effect on the glycosyl-transferases in the rapidly renewing Golgi and other membranes. The activity of glycosyl-transferases measured in cellular fraction enriched with Golgi membrane. However, the enzyme activities measured in serum showed a dramatic increase of sialyltransferase after colchicine treatment. Colchicine produces the maximal effect on the sialyltransferase with a dose of 0.25 mg/100 g of body weight. The effect of colchicine is restricted to a remarkable elevation of sialyltransferase, whereas the galactosyl-transferase activity was only slightly affected. Increased level of glycosyl transferases in the serum of patients with liver disease suggested that the serum enzymes are at least partly originating in the liver. The experiments offer an excellent model for correlating the cell-cycle and other membrane-related changes caused by colchicine with the release or shedding of the surface and membrane-bound glycosyltransferases. Sialic acid and fucose as terminal residues of the oligosaccharide chain may have special significance for the recognition mechanism of the membrane renewal and for the process of exocytosis." @default.
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- W85039860 date "1979-01-01" @default.
- W85039860 modified "2023-09-27" @default.
- W85039860 title "Membrane and Soluble Glycosyltransferases in Colchicine-Treated Rats. Marked Increase of Sialyltransferase in Serum" @default.
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- W85039860 doi "https://doi.org/10.1016/b978-0-12-301302-6.50097-x" @default.
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