Toxicon 2010 Sep 01;563:458-65. doi: 10.1016/j.toxicon.2010.04.015.

A novel annexin A2 protein with platelet aggregation-inhibiting activity from amphibian Bombina maxima skin.

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Annexin A2 is a unique member of annexin family with multi-functions in membrane physiology, implicated in inflammation and cancer progression. mRNA of Annexin A2 is abundant in the skin of some amphibians. However, no annexin A2 protein has been isolated and characterized from amphibian skin. In this report, a novel annexin A2 protein with apparent molecular weight of 33 kDa and named Bm-ANXA2, was purified from frog Bombina maxima skin, which is highly toxic to mammals, by a combination of ion exchange and gel filtration chromatography. A full-length cDNA encoding the protein was obtained from the cDNA library constructed from the frog skin. Sequence analysis indicates that Bm-ANXA2 shares 89% and 80% amino acid sequence identities with those of Xenopus and human annexin A2, respectively. Different from other annexin A2 proteins, the N-terminal 26 amino acids of Bm-ANXA2 were truncated. Bm-ANXA2 dose-dependently inhibited human platelet aggregation stimulated by various agonists in a Ca(2+)-dependent manner. It bound to activated platelets and significantly inhibited alpha(IIb)beta(3) activation and alpha-granular secretion. This is the first report that an annexin A2 protein possesses platelet aggregation-inhibiting activity, providing novel clues in the illustration of pathophysiological roles of annexin A2 proteins.

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Species referenced: Xenopus
Genes referenced: anxa2