Polymeric osteopontin employs integrin alpha9beta1 as a receptor and attracts neutrophils by presenting a de novo binding site.

@article{Nishimichi2009PolymericOE,
  title={Polymeric osteopontin employs integrin alpha9beta1 as a receptor and attracts neutrophils by presenting a de novo binding site.},
  author={Norihisa Nishimichi and Fumiko Higashikawa and Hiromi H. Kinoh and Yoshiko Tateishi and Haruo Matsuda and Yasuyuki Yokosaki},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 22},
  pages={14769-76}
}
Osteopontin (OPN) is a cytokine and ligand for multiple members of the integrin family. OPN undergoes the in vivo polymerization catalyzed by cross-linking enzyme transglutaminase 2, which consequently increases the bioactivity through enhanced interaction with integrins. The integrin alpha9beta1, highly expressed on neutrophils, binds to the sequence SVVYGLR only after intact OPN is cleaved by thrombin. The SVVYGLR sequence appears to be cryptic in intact OPN because alpha9beta1 does not… CONTINUE READING

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