Loading...
  • protein
  • Bradykinin binding and bradykinin-induced Ca2+ release are both restored by expression of full-length calreticulin and the N + P domain of the protein. (nih.gov)
  • receptor
  • Our results indicate that calreticulin may play a role in folding of the bradykinin receptor, which affects its ability to initiate InsP3-dependent Ca2+ release in calreticulin-deficient cells. (nih.gov)
  • We have shown that expression of the InsP3R is reduced in calreticulin-deficient (K42) cells, whereas expression of the bradykinin receptor is not. (nih.gov)
  • membrane
  • To test this hypothesis, we loaded wild-type and calreticulin-deficient cells with fluo-3, and then we added saponin to permeabilize the plasma membrane (Favre et al. (nih.gov)
  • cells
  • Calreticulin-deficient cells show inhibited Ca2+ release in response to bradykinin, yet they release Ca2+ upon direct activation with the inositol 1,4,5-trisphosphate (InsP3). (nih.gov)
  • Ca2+ release in saponin-permeabilized calreticulin-deficient cells. (nih.gov)
  • Wild-type (K41) and calreticulin-deficient (K42) cells were loaded with a fluorescent Ca2+ indicator fluo-3 and permeabilized with saponin. (nih.gov)
  • Fig. 8 shows that InsP3-induced Ca2+ release from the ER was indistinguishable in the wild-type (K41) and calreticulin-deficient (K42) cells, indicating that there is no difference in function of the InsP3Rs in the different cell types. (nih.gov)