Abstract
Phosphoglucomutase was identified as a potential intracellular S100 target protein because it interacted with two members of the S100 family of calcium-modulated proteins, S1 00A1 and S1 00B, in gel overlay experiments. These results were confirmed by affinity chromatography experiments demonstrating that S100Al and S100B bound to phosphoglucomutase-Sepharose in a calcium-dependent manner. In the reverse experiment, phosphoglucomutase bound to S100A1 and S100B-Sepharose in a calcium-dependent manner. S100Al inhibited phosphoglucomutase activity in a calcium-dependent manner. In contrast, S100B stimulated phosphoglucomutase activity in a calcium-dependent manner. Other calcium-binding proteins (calmodulin, troponin C, parvalbumin, and (x-lactalbumin) had no effect on phosphoglucomutase. These results suggest that the effects of S100Al and S100B are not nonspecific effects of low molecular weight, acidic proteins. This is the first report of an S100 target protein whose activity is antagonistically regulated by S100Al and S100B, suggesting that cellular diversity in intracellular calcium signaling pathways may be due, at least in part, to the complement of S100 proteins expressed in different cell types.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
