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Anginex

Mayo et al (1998) have designed a series of synthetic peptide 33mers by incorporating beta-conformation stabilizing residues from the beta-sheet domains of CXC-Chemokines (IL8, PF4) and functionally important residues from the beta-sheet domain of BPI [Bactericidal/permeability-increasing protein], a bactericidal protein of human neutrophils known for its ability to kill bacteria and to neutralize the inflammatory actions of bacterial lipopolysaccharides. These peptides retain the bactericidal activity of the neutrophil bactericidal protein (Mayo et al, 1998).

Anginex and one of these peptides (betapep-25) has been shown to be a potent inhibitor of angiogenesis in vivo (Griffioen et al, 2001). The peptide specifically inhibits proliferation of vascular endothelial cells and induces cell death by apoptosis in these cells. It also inhibits adhesion to and migration of endothelial cells on different extracellular matrix components. van der Schaft et al (2002) have reported that anginex causes the induction of anoikis in angiogenically activated endothelial cells. This results in an up to 90 % inhibition of migration in the wound assay. Anginex inhibits angiogenesis in the in vitro mouse aortic ring assay and inhibits tumor-induced angiogenesis in the chick embryo chorioallantoic membrane assay and does not appear to have any toxicity.

Thijssen et al (2006) have reported that Galectin-1 is a receptor for anginex on endothelial cells.

See also: Angiogenesis Dictionary section of this encyclopedia for other entries directly bearing on factors and processes involved in the generation of new blood vessels.

LAST MODIFIED: March 2008

See REFERENCES for entry Anginex

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