alpha 1-Antichymotrypsin in lung secretions is not an effective proteinase inhibitor.
This paper presents evidence that alpha 1-antichymotrypsin in lung secretions is not effective as an inhibitor of chymotrypsin-like enzymes. First, lung secretion samples inhibited more cathepsin G on a one-to-one molar basis than could be accounted for by the alpha 1-antichymotrypsin present. Second, the major cathepsin G inhibitory capacity of sputum was in gel filtration fractions that corresponded to a low molecular weight (10,000-15,000) and contained immunoreactive antileucoprotease. Third, although alpha 1-antichymotrypsin purified from plasma was almost fully active against cathepsin G, that purified from lung lavage retained less than 15% of its inhibitory function. Immunoblotting following sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that alpha 1-antichymotrypsin in plasma and lung secretions are of similar molecular size and no enzyme-alpha 1-antichymotrypsin complexes could be detected in sputum or bronchoalveolar lavage fluids. However, in contrast to the alpha 1-antichymotrypsin purified from plasma, the lavage protein gave a broad elution profile following anion-exchange chromatography.
D056649:Cathepsin G; D002403:Cathepsins / Q000037:antagonists & inhibitors; D002852:Chromatography, Ion Exchange; D002918:Chymotrypsin / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007163:Immunosorbent Techniques; D008168:Lung / Q000378:metabolism*; D008970:Molecular Weight; D011480:Protease Inhibitors / Q000494:pharmacology*; D012697:Serine Endopeptidases; D000514:alpha 1-Antichymotrypsin / Q000032:analysis*
D011480:Protease Inhibitors; D000514:alpha 1-Antichymotrypsin; D002403:Cathepsins; D012697:Serine Endopeptidases; D002918:Chymotrypsin; C534094:CTSG protein, human; D056649:Cathepsin G