The annexin family of calcium-binding proteins is composed of at least ten mammalian genes and is characterized by a conserved core domain which binds phospholipids in a Ca2+-dependent manner and a unique amino-terminal region which may confer binding specificity. The interaction between these proteins and biological membranes has led to the hypothesis that they are involved in cellular trafficking processes such as endocytosis, exocytosis and cellular adhesion. Annexin I, alternatively referred to as lipocortin, has been implicated as a mediator of the anti-inflammatory response produced by glucocorticoids and as an inhibitor of cPLA2, a potent mediator of inflammation. Annexin II, also called p36, exists as a monomer or as a heterotetramer, complexed with the S-100-related protein p11. This complex is termed calpactin I. In the tetrameric form, Annexin II is an efficient substrate of PKC family and Src pp60.
