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Tris reversibly inhibits secretion of albumin and α‐1‐antitrypsin at different sites
Author(s) -
Quinn Paul,
Judah Jacob D.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81415-k
Subject(s) - tris , golgi apparatus , secretion , albumin , endoplasmic reticulum , chemistry , biochemistry , bovine serum albumin , fractionation , secretory protein , serum albumin , microbiology and biotechnology , biology , chromatography
We have investigated the effect of the weak base Tris on the processing and secretion of albumin and α‐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 α‐1 antitrypsin fails to leave the endoplasmic reticulum.