title: Tris reversibly inhibits secretion of albumin and alpha-1-antitrypsin at different sites.
abstract: We have investigated the effect of the weak base Tris on the processing and secretion of albumin and alpha-1 antitrypsin by hepatocytes in culture. We show that the secretion of both proteins is 90% inhibited by 30 mM Tris. The post-synthetic processing of both proteins is inhibited to the same extent. These effects are completely reversible. Cell fractionation indicates that albumin accumulates in the Golgi, whereas alpha-1 antitrypsin fails to leave the endoplasmic reticulum.
authors.affiliation: Department of Physiology, University College London, UK.
authors.forename: P
authors.initials: P
authors.lastname: Quinn
authors.forename: J D
authors.initials: JD
authors.lastname: Judah
mesh_terms: D000418:Albumins / Q000378:metabolism*; D000818:Animals; D002478:Cells, Cultured; D004721:Endoplasmic Reticulum / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism; D007525:Isoelectric Focusing; D008099:Liver / Q000187:drug effects / Q000378:metabolism*; D011228:Prealbumin / Q000378:metabolism; D011233:Precipitin Tests; D051381:Rats; D014325:Tromethamine / Q000494:pharmacology*; D000515:alpha 1-Antitrypsin / Q000378:metabolism*
chemical_list: D000418:Albumins; D011228:Prealbumin; D000515:alpha 1-Antitrypsin; D014325:Tromethamine