Article
The affinity of a major Ca2+ binding site on GRP78 is differentially enhanced by ADP and ATP.
The Journal of biological chemistry - 31 Mar 2006
Lamb Heather K, Mee Christopher, Xu Weiming, Liu Lizhi, Blond Sylvie, Cooper Alan, Charles Ian G, Hawkins Alastair R
Abstract excerpt
GRP78 is a major protein regulated by the mammalian endoplasmic reticulum stress response, and up-regulation has been shown to be important in protecting cells from challenge with cytotoxic agents. GRP78 has ATPase activity, acts as a chaperone, and interacts specifically with other proteins, such as caspases, as part of a mechanism regulating apoptosis. GRP78 is also reported to have a possible role as a Ca2+...
Topics
- Adenosine Diphosphate
- Adenosine Triphosphate
- Animals
- Binding Sites
- Calcium
- Calorimetry
- Calorimetry, Differential Scanning
- Circular Dichroism
- Dose-Response Relationship, Drug
- Endoplasmic Reticulum Chaperone BiP
- Heat-Shock Proteins
- Least-Squares Analysis