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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 ; Ferrell, G A ; Dishon, D S ; Le, Q Q ; Sifers, R N

The Journal of biological chemistry, 1992-01, Vol.267 (2), p.1072-1080 [Periódico revisado por pares]

BETHESDA: Elsevier Inc

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Título:
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
Autor: Le, A ; Ferrell, G A ; Dishon, D S ; Le, Q Q ; Sifers, R N
Assuntos: 1-Deoxynojirimycin ; 2,4-Dinitrophenol ; alpha 1-Antitrypsin - genetics ; alpha 1-Antitrypsin - metabolism ; Animals ; Biochemistry & Molecular Biology ; Brefeldin A ; Cycloheximide - pharmacology ; Cyclopentanes - pharmacology ; Dinitrophenols - pharmacology ; Electrophoresis, Polyacrylamide Gel ; Endoplasmic Reticulum - drug effects ; Endoplasmic Reticulum - metabolism ; Glucosamine - analogs & derivatives ; Glucosamine - pharmacology ; Golgi Apparatus - drug effects ; Golgi Apparatus - enzymology ; Humans ; Life Sciences & Biomedicine ; Liver Neoplasms, Experimental - enzymology ; Mice ; Nocodazole - pharmacology ; Protein Synthesis Inhibitors ; Puromycin - pharmacology ; Science & Technology ; Transfection ; Tumor Cells, Cultured
É parte de: The Journal of biological chemistry, 1992-01, Vol.267 (2), p.1072-1080
Notas: Medline
NIH RePORTER
Descrição: Greater than 85 of the transport-impaired PiZ variant of human alpha 1-antitrypsin is retained within transfected mouse hepatoma cells and is subjected to intracellular degradation (Le, A., Graham, K., and Sifers, R.N. (1990) J. Biol. Chem. 265, 14001-14007). The retained protein undergoes a discrete size reduction that results from the modification of its endoglycosidase H-sensitive oligosaccharides and is inhibited by 1-deoxymannojirimycin. Metabolic poisons and inhibitors of protein synthesis perturb the intracellular degradation of the retained protein but do not affect its size reduction. The ability of metabolic poisons to influence the degradation of the PiZ variant in cells treated with brefeldin A indicates that export of the macromolecule from the endoplasmic reticulum (ER) is not the energy-dependent component of its degradation. Subcellular fractionation experiments have verified that both the size reduction and degradation of the retained PiZ variant occur within the rough ER. Finally, sedimentation velocity centrifugation analysis of radiolabeled cell extracts has indicated that approximately 80 of the PiZ variant consists as soluble aggregates immediately after its synthesis. An inability to detect more extensive aggregation during the retention period supports our previous conclusion that only a small fraction of the macromolecules actually form large insoluble aggregates (Graham, K.S., Le, A., and Sifers, R.N. (1990) J. Biol. Chem. 265, 20463-20468). Overall, these findings indicate that soluble aggregates of the PiZ variant are degraded within the ER by a mechanism sensitive to inhibitors of protein synthesis.
Editor: BETHESDA: Elsevier Inc
Idioma: Inglês

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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 ; Ferrell, G A ; Dishon, D S ; Le, Q Q ; Sifers, R N

BETHESDA: Elsevier Inc

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