Thrombospondin mediates calcium mobilization in fibroblasts via its Arg-Gly-Asp and carboxyl-terminal domains.

@article{Tsao1995ThrombospondinMC,
  title={Thrombospondin mediates calcium mobilization in fibroblasts via its Arg-Gly-Asp and carboxyl-terminal domains.},
  author={P W Tsao and Shaker A. Mousa},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 40},
  pages={23747-53}
}
Thrombospondin is a matrix glycoprotein found in various cells that can modulate cell attachment, migration, and proliferation. We now show that intact soluble thrombospondin causes a transient [Ca2+]i increase in IMR-90 fibroblasts. This [Ca2+]i increase is mediated partly by the RGD-containing domain of thrombospondin that binds to the integrin alpha v beta 3 as demonstrated by inhibitor studies using anti-alpha v beta 3 antibody and RGD-containing peptides. A non-RGD and non-alpha v beta 3… CONTINUE READING