Phospholipases A(2) (PLA(2)s) are enzymes that catalyse the hydrolysis of the sn-2 acyl bond of glycerophospholipids to produce free fatty acids and lysophospholipids. Numerous intra cellular and secreted PLA(2)s (sPLA(2)s) have now been characterized. Because PLA(2) products are important for cell signalling and the biosynthesis of biologically active lipids, including eicosanoids and platelet-activating factor, PLA(2)s are generally considered as key enzymes that control the release of lipid mediator precursors. However, the increasing number of mammalian sPLA(2)s and the recent identification of different membrane proteins that bind sPLA(2)s makes it likely that these enzymes also behave as ligands for receptors, and that their physiological function is not limited to their catalytic activity. Here, the current state of awareness regarding the different types of sPLA(2)-binding proteins is described. To date, five distinct mammalian sPLA(2)s and two main types (M and N) of sPLA(2) receptors have been identified. Because most is known about the M-type receptor, particular attention will be paid to it, including a description of it molecular properties and of its possible biological roles with regard to sPLA(2) function.