[HTML][HTML] A novel mechanism for bradykinin production at inflammatory sites: diverse effects of a mixture of neutrophil elastase and mast cell tryptase versus tissue and …
A Kozik, RB Moore, J Potempa, T Imamura… - Journal of Biological …, 1998 - ASBMB
Coprocessing of kininogens by a mixture of human mast cell tryptase and neutrophil
elastase was explored as a potential substitute for the kallikrein-dependent pathway for kinin
generation during inflammation. Tryptase easily excised bradykinin from the synthetic
heptadecapeptide, ISLMKRPPGFSPFRSSR, but was unable to produce significant amounts
of kinin by proteolysis of kininogens. However, a mixture of tryptase and elastase released
bradykinin from each protein with a yield comparable to that of human plasma kallikrein …
elastase was explored as a potential substitute for the kallikrein-dependent pathway for kinin
generation during inflammation. Tryptase easily excised bradykinin from the synthetic
heptadecapeptide, ISLMKRPPGFSPFRSSR, but was unable to produce significant amounts
of kinin by proteolysis of kininogens. However, a mixture of tryptase and elastase released
bradykinin from each protein with a yield comparable to that of human plasma kallikrein …