Soluble aggregates of the human PiZ alpha 1-antitrypsin variant are degraded within the endoplasmic reticulum by a mechanism sensitive to inhibitors of protein synthesis.

Le, A

Soluble aggregates of the human PiZ alpha 1-antitrypsin variant are degraded within the endoplasmic reticulum by a mechanism sensitive to inhibitors of protein synthesis. [electronic resource] - The Journal of biological chemistry Jan 1992 - 1072-80 p. digital

Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.

0021-9258


1-Deoxynojirimycin
2,4-Dinitrophenol
Animals
Brefeldin A
Cycloheximide--pharmacology
Cyclopentanes--pharmacology
Dinitrophenols--pharmacology
Electrophoresis, Polyacrylamide Gel
Endoplasmic Reticulum--drug effects
Glucosamine--analogs & derivatives
Golgi Apparatus--drug effects
Humans
Liver Neoplasms, Experimental--enzymology
Mice
Nocodazole--pharmacology
Protein Synthesis Inhibitors
Puromycin--pharmacology
Transfection
Tumor Cells, Cultured
alpha 1-Antitrypsin--genetics