N-linked Glycosylation of Protease-Activated Receptor

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Besides their functions in protein degradation and digestion, proteases also serve as hormone-like signaling molecules that control critical pathophysiological processes in the body namely; pain and repair mechanisms, homeostasis and inflammation. Different types of proteases can communicate with the cells by splitting a protease activated receptors (PARs), which is a member of the four-G protein-coupled receptors (Zhao, Matthew and Nigel n.p). PARs manifested by nearly all types of cells regulates the critical psychological and disease-related processes and are now the most frequent target in therapy for primary prevalent diseases. To get more insight into the PARs activation and performance we can consider the relations of thrombin in PAR1, PAR3, and PAR4. And trypsin in the case of PAR2 and PAR4.These proteases reveal the tethered ligands, which helps in the stabilization of the conformed cleaving receptors activating the canonical pathway. PAR1 is a G-protein coupled receptor (GPCR) that plays a significant role in the Coagulation of the protease thrombin. PAR1 intertwines well to multiple heterotrimeric G-protein subgroups when in the same cell hence promoting cellular responses. However, it is still unclear on how the molecular processes and mechanism by which an activation of a particular GPCR on the same ligand allows coupling to many G proteins subsets (Soto et al. n.p). An experiment conducted proved that PAR1 mutant which was deficient in glycosylation at extracellular loop 2 (ECL2) was more reliable at stimulating Gq-linked phosphoinositide communications in comparison with glycosylated wild-type receptor. In another event, wild type PAR1 was more efficient

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