Endothelial apoptotic activity of angiocidin is dependent on its polyubiquitin binding activity
2005

Angiocidin's Role in Endothelial Cell Apoptosis

publication Evidence: high

Author Information

Author(s): Dimitrov S, Sabherwal Y, Raymond D D, L'Heureux D Z, Lu Q, Tuszynski G P

Primary Institution: Temple University School of Medicine

Hypothesis

The antiendothelial activity of angiocidin could be due in part to its polyubiquitin binding activity.

Conclusion

Angiocidin induces apoptosis in endothelial cells by inhibiting proteasome activity through its polyubiquitin binding.

Supporting Evidence

  • Angiocidin binds polyubiquitin in vivo with high affinity.
  • Mutated angiocidin proteins showed diminished binding activity and apoptotic activity.
  • Angiocidin treatment led to increased levels of polyubiquitinated proteins in endothelial cells.

Takeaway

Angiocidin is a protein that can make blood vessel cells die by sticking to other proteins and stopping their normal function.

Methodology

The study involved cloning angiocidin, expressing it in bacteria, and testing its effects on endothelial cells in vitro.

Digital Object Identifier (DOI)

10.1038/sj.bjc.6602773

Want to read the original?

Access the complete publication on the publisher's website

View Original Publication