INTERFERENCE OF TRIS(HYDROXYMETHYL)AMINOMETHANE WITH STRUCTURE AND FUNCTION OF GOLGI MEMBRANES

  • 1 January 1979
    • journal article
    • research article
    • Vol. 40  (3) , 313-316
Abstract
Short term perfusion of isolated rat liver with tris(hydroxymethyl)aminomethane or other nonamphoteric amines (glycinamide, diethylamine) in moderate concentrations (10 to 20 mM) causes blistering of Golgi stacks on the concave side as well as swelling of lysosomes and of secretory vesicles in otherwise unaltered hepatocytes. Similar vacuolization is observed in Kupffer cells, pancreatic .beta.-cells, intestinal epithelial cells, and renal proximal tubule cells, but not in .alpha.-cells of the pancreas or in kidney glomerular podocytes. Fusion of the vesicles occurs frequently and involves denudation of intramembranous particles from contact areas. Since protein synthesis is not affected, inhibition by tris(hydroxymethyl)aminomethane of protein secretion into the perfusate indicates a block in protein processing at a postribosomal level. This finding together with morphologic evidence unravels the Golgi and post-Golgi membranes as specific site of tris(hydroxymethyl)aminomethane interaction with intracellular structures. Tris(hydroxymethyl)aminomethane (Tris) is widely used as a buffer substance in biologic experiments and also as a therapeutic agent for correction of severe acidosis in humans.

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