Human neutrophil elastase and cathepsin G cleavage sites in the bait region of alpha 2-macroglobulin. Proposed structural limits of the bait region.
The sites of cleavage in the "bait region" of human alpha 2-macroglobulin made by both neutrophil elastase and cathepsin G, as the first step in their inactivation by this inhibitor, have been identified. These positions are at a valylhistidyl bond for elastase and a phenylalanyl-tyrosyl bond for cathepsin G. All of the proteinases tested so far, including those utilized in this study, are cleaving within a twenty-seven aminoacid peptide sequence occurring between two proline residues. It is suggested that this area represents the outer limits of the "bait region" loop.
D000595:Amino Acid Sequence; D056649:Cathepsin G; D002403:Cathepsins / Q000097:blood*; D006801:Humans; D009504:Neutrophils / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000097:blood*; D010446:Peptide Fragments / Q000032:analysis; D012697:Serine Endopeptidases; D013379:Substrate Specificity; D000511:alpha-Macroglobulins / Q000378:metabolism*
D010446:Peptide Fragments; D000511:alpha-Macroglobulins; D002403:Cathepsins; D012697:Serine Endopeptidases; C534094:CTSG protein, human; D056649:Cathepsin G; D010196:Pancreatic Elastase