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J. Biol. Chem., Vol. 256, Issue 20, 10256-10258, Oct, 1981
C Boudier, C Holle and JG Bieth
Human leukocyte cathespin G strongly stimulates the rate of solubilization
of human lung elastin by human leukocyte elastase. For instance, the
elastolytic activity of an equimolar mixture of elastase and cathepsin G is
more than 5 times higher than that of elastase alone. Optimal stimulation
occurs only if cathepsin G and elastase act simultaneously on elastin.
Potentiation of leukocyte elastase digestion of lung elastin may also be
brought about by bovine alpha-chymotrypsin. This enzyme is about half as
efficient as cathepsin G. Stimulation of leukocyte elastase activity by
cathepsin G is about 3 times less pronounced with bovine ligamentum nuchae
elastin than with human lung elastin. On the other hand, the elastolytic
activity of porcine pancreatic elastase is only enhanced by 20 to 30% by
cathepsin. Therefore, maximal potentiation of elastolysis occurs with the
lung elastin/leukocyte elastase system. The pathologic relevance of these
findings is discussed.
Stimulation of the elastolytic activity of leukocyte elastase by leukocyte cathepsin G
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