Specific membrane receptors for secretory phospholipases A (sPLAs) have been initially identified with novel snake venom sPLAs called OS and OS. One of these sPLA receptors (muscle (M)-type, 180 kDa) has a very high affinity for OS and OS and a high affinity for pancreatic and inflammatory-type mammalian sPLAs, which might be the natural endogenous ligands of PLA receptors. Primary structures of OS and OS were determined and compared with sequences of other sPLAs that bind less tightly or do not bind to the M-type receptor. In addition, the binding properties of pancreatic sPLA mutants to the M-type receptor have been analyzed. Residues within or close to the Ca-binding loop of pancreatic sPLA are crucially involved in the binding step, although the presence of Ca that is essential for the enzymatic activity is not required for binding to the receptor. These residues include Gly-30 and Asp-49, which are conserved in all sPLAs. Leu-31 is also essential for binding of pancreatic sPLA to its receptor. Many other mutations have been considered. Those occurring in the N-terminal helices and the pancreatic loop do not change binding to the M-type receptor. Conversion of pancreatic prophospholipase to phospholipase is essential for the acquisition of binding properties to the M-type receptor.

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