Cloning and expression of a membrane receptor for secretory phospholipases A2.

摘要: Snake venom and mammalian secretory phospholipases A2 are structurally related enzymes that have been associated with several toxic (neurotoxicity, myotoxicity, etc.), pathological (inflammation, hypersensitivity, or physiological (contraction, proliferation, etc.) processes. We previously shown snake PLA2s specific high affinity receptors. Here, we report the molecular cloning of one these PLA2 receptors (molecular mass approximately 180 kDa), purified from rabbit skeletal muscle. It is a membrane protein N-terminal cysteine-rich domain, fibronectin type II eight repeats carbohydrate recognition unique transmembrane intracellular C-terminal domain. The 1458-residue receptor, expressed in transfected cells, binds svPLA2 very affinities (Kd values 10-20 pM). also tightly two structural types msPLA2s, i.e. pancreatic synovial 1-10 nM). This receptor might key role normal actions PLA2s.