Protein disulfide isomerase associates with misfolded human lysozyme in vivo.
Year: 1994
Type: article
Abstract: Wild-type human lysozyme (hLZM) is quantitatively secreted into the media when expressed in mouse fibroblast cells, but some misfolded hLZMs are retained and rapidly degraded in a pre-Golgi compartment (Omura, F., Otsu, M., Yoshimori, T., Tashiro, Y., and Kikuchi, M. (1992) Eur. J. Biochem. 210, 591-599). To detect the association with misfolded hLZMs of cellular proteins involved in their folding, retention, and pre-Golgi degradation, a co-precipitation experiment was carried out using anti-hLZM antibody and metabolically labeled cell lysates, which were treated with a membrane-permeable cross-linking reagent. Here we report that protein disulfide isomerase associated in vivo with misfolded hLZMs, but not with the wild-type protein, and discuss the possible role of protein disulfide isomerase in the quality control of newly synthesized proteins in the endoplasmic reticulum.
Source: Journal of Biological Chemistry
Authors: M. Otsu, F. Omura, T. Yoshimori, M. Kikuchi
Institution: Protein Engineering Research Institute
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1519333122