Cayman Carbamylated Alpha-1 Antitrypsin

Alpha-1 antitrypsin is a serine protease inhibitor and member of the serpin superfamily. It has a five-stranded A β-sheet and a mobile reactive center loop that acts as a pseudosubstrate for various proteases. Alpha-1 antitrypsin binds to a protease, undergoes proteolytic cleavage, and forms a covalent linkage between a carboxyl group in the reactive loop and the serine hydroxyl of the protease active site, effectively inactivating the enzyme which is then cleared from circulation. The primary targets of alpha-1 antitrypsin are neutrophil elastase and proteinase 3, however, it also inhibits trypsin, kallikreins 7 and 14, and matriptase. Alpha-1 antitrypsin protects the lower respiratory tract from proteolytic destruction via inhibition of neutrophil elastase and reduced serum levels of alpha-1 antitrypsin have been linked to early-onset liver disease and emphysema. Alpha-1 antitrypsin is an acute-phase protein that reduces production of inflammatory cytokines, inhibits apoptosis, blocks leukocyte degranulation and migration, as well as suppresses NF-κB nuclear translocation in monocytes. It delays disease onset in mouse models of inflammatory disease, including collagen-induced arthritis and experimental autoimmune encephalomyelitis (EAE). Alpha-1 antitrypsin is subject to post-translational modifications such as glycosylation and carbamylation in vivo. Carbamylated alpha-1 antitrypsin has been found in synovial fluid samples from rheumatoid arthritis patients and is predicted to act as an autoantigen.

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