Calpain-mediated truncation of rat brain AMPA receptors increases their Triton X-100 solubility.

Previous studies have indicated that calpain activation results in the truncation of the C-terminal domains of AMPA and NMDA receptor subunits. The present study determined the distribution of the truncated species of the subunits between Triton-soluble and -insoluble fractions. Western blots were performed with various antibodies to quantify the amounts of the various species of GluR1, GluR2, GluR3 and NR2B subunits. The results indicate that calpain activation decreased the amount of all the intact subunits in Triton-insoluble fractions. Calpain-generated truncated forms of GluR1 and GluR2, but not NR2B, were absent in these fractions, and were recovered in Triton-soluble fractions. These findings suggest that calpain-mediated truncation of AMPA but not NMDA receptor C-terminal domains results in modifications of the interactions between the receptors and postsynaptic densities, and that this mechanism could be involved in activity-dependent changes in the subcellular distribution of AMPA receptors.