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lüll Annexin 1: the new face of an old molecule Lim LH; Pervaiz SFASEB J 2007[Apr]; 21 (4): 968-75The annexin superfamily consists of 13 calcium or calcium and phospholipid binding proteins with a significant degree of biological and structural homology (40-60%). First described in the late 1970s and subsequently referred to as macrocortin, renocortin, lipomodulin, lipocortin-1, and more recently Annexin 1, this 37 kDa calcium and phospholipid binding protein is a strong inhibitor of glucocorticoid-induced eicosanoid synthesis and PLA2. Recent interest in the biological activity of this intriguing molecule has unraveled important functional attributes of Annexin 1 in a variety of inflammatory pathways, on cell proliferation machinery, in the regulation of cell death signaling, in phagocytic clearance of apoptosing cells, and most importantly in the process of carcinogenesis. Here we attempt to present a short review on these diverse biological activities of an interesting and important molecule, which could be a potential target for novel therapeutic intervention in a host of disease states.|Animals[MESH]|Annexin A1/metabolism/*physiology[MESH]|Apoptosis[MESH]|Calcium/chemistry[MESH]|Cell Proliferation[MESH]|Glucocorticoids/metabolism[MESH]|Humans[MESH]|Models, Biological[MESH]|Neoplasms/metabolism[MESH]|Phagocytosis[MESH]|Phospholipids/chemistry[MESH]|Protein Binding[MESH]|Signal Transduction[MESH] |