Title: Annexins

Literature References: Family of calcium and phopholipid binding proteins; virtually ubiquitous in both animal and plant cells. Characterized by a common structure composed of 4 or 8 homologous repeats of ~70 amino acids. Involved in membrane trafficking, transmembrane channel activity, inhibition of phospholipase A2, and inhibition of coagulation. Known variously by such names as synexin, lipocortin, anchorin, and calpactin, the term annexins was chosen for their ability to bind, or "annex", to cellular membranes. Description of nomenclature: M. J. Crumpton, J. R. Dedman, Nature 345, 212 (1990). Isoln of synexin from bovine adrenal medullary tissue: C. E. Creutz et al., J. Biol. Chem. 253, 2858 (1978). Review of discovery, molecular biology and bioactivites: P. Raynal, H. B. Pollard, Biochim. Biophys. Acta 1197, 63-93 (1994); of annexins in plant cells: G. B. Clark, S. J. Roux, Plant Physiol. 109, 1133-1139 (1995). Review of three-dimensional structure: S. Liemann, R. Huber, Cell. Mol. Life Sci. 53, 516-521 (1997). Review of role in plasminogen binding: H.-M. Kang et al., Trends Cardiovasc. Med. 9, 92-102 (1999); K. A. Hajjar, S. Krishman, ibid. 128-138; of role in membrane fusion: H. Kubista et al., Subcell. Biochem. 34, 73-131 (2000); as nucleotide binding proteins: J. Bandorowicz-Pikula et al., BioEssays 23, 170-178 (2001). Comprehensive description: V. Gerke, S. E. Moss, Physiol. Rev. 82, 331-371 (2002).