Article
Accumulation of the insoluble PiZ variant of human alpha 1-antitrypsin within the hepatic endoplasmic reticulum does not elevate the steady-state level of grp78/BiP.
The Journal of biological chemistry - 25 Nov 1990
Graham K S, Le A, Sifers R N
Abstract excerpt
Greater than 85% of the transport-impaired PiZ variant of human alpha 1-antitrypsin is retained within cells and subsequently degraded within a pre-Golgi nonlysosomal compartment that is apparently separate from the endoplasmic reticulum (ER) (Le, A., Graham, K. S., and Sifers, R. N. (1990) J. Bi...
Topics
- Animals
- Carrier Proteins
- Cell Line
- Endoplasmic Reticulum
- Endoplasmic Reticulum Chaperone BiP
- Genetic Variation
- Heat-Shock Proteins
- Humans
- Immunoglobulin Heavy Chains
- Liver
- Liver Neoplasms, Experimental
- Mice
- Mice, Transgenic
- Molecular Chaperones
- Transfection
- Tunicamycin
- alpha 1-Antitrypsin