Article
Lysozyme Mutants Accumulate in Cells while Associated at their N-terminal Alpha-domain with the Endoplasmic Reticulum Chaperone GRP78/BiP.
International journal of biological sciences - 1 Jan 2016
Kamada Yoshiki, Nawata Yusuke, Sugimoto Yasushi
Abstract excerpt
Amyloidogenic human lysozyme variants deposit in cells and cause systemic amyloidosis. We recently observed that such lysozymes accumulate in the endoplasmic reticulum (ER) with the ER chaperone GRP78/BiP, accompanying the ER stress response. Here we investigated the region of lysozyme that is critical to its association with GRP78/BiP. In addition to the above-mentioned variants of lysozyme, we constructed...
Topics
- Amino Acid Sequence
- Amino Acid Substitution
- Endoplasmic Reticulum
- Endoplasmic Reticulum Chaperone BiP
- HEK293 Cells
- Heat-Shock Proteins
- Humans
- Hydrophobic and Hydrophilic Interactions
- Models, Molecular
- Muramidase
- Mutation
- Protein Domains
- Protein Folding