Possible Interaction: Aprotinin and Trypsin

“BACKGROUND The serine protease inhibitor aprotinin inhibits trypsin , kallikrein, and plasmin and enhances the complement hemolytic activity of the first complement component C1.”

“The subsequent infusion of aprotinin at a dose of 1·5 × 106 KIU for 30 min led to an almost complete inhibiton of trypsin.”

“ Aprotinin decreased trypsin expression and activation in plaques, blocked PAR-2 and MMP-9 activation, and decreased cytokine expression; it also increased fibrous cap thickness, decreased the intima-media thickness and intimal/medial ratio, thus significantly ameliorating plaque vulnerability.”

“Bovine pancreatic trypsin inhibitor BPTI ) forms an extremely stable and cleavage-resistant complex with trypsin , and thus provides a rigorous challenge of mesotrypsin catalytic activity toward polypeptide inhibitors.”

“Third, the ability of aprotinin to neutralize, to varying degrees, the action of several serine proteases, such as trypsin , chymotrypsin, and particularly the urokinase-type plasminogen activator (uPA) and kallikreins is important, because these proteases have been implicated in tumor progression and development of metastasis.”

“The two major classes of inhibitors are the Kunitz trypsin inhibitor , which inhibits trypsin , and the Bowman-Birk inhibitor (BBI), which inhibits both trypsin and chymotrypsin.”

“ BPTI is an extremely potent inhibitor of trypsin , but it also specifically binds to various active and inactive serine proteinase homologs with KD values that range over eight orders of magnitude.”

“One line of evidence includes the finding that the complex of BPTI and trypsin , in which the inhibitory loop of BPTI is masked by interaction with trypsin, is completely ineffective in the production of substate events in the KCa channel.”

“The action of either chymotrypsin or trypsin was completely prevented by the serine protease inhibitor aprotinin , indicating that the proteolytic activity of the enzymes accounts for apoptosis induction.”

“We found that the loss of lipase activity was partly prevented by inhibiting trypsin with aprotinin (910 KU/ml; P = 0.03) and was accelerated by adding bovine trypsin (2.5 mg/ml; P = 0.01).”

“Standard inhibitors such as bovine pancreatic trypsin inhibitor BPTI ), soybean trypsin inhibitor (SBTI), alpha 1-antitrypsin inhibitor, and a protease inhibitor derived from human articular cartilage have been examined by this method and displayed sharp inhibition bands when the gels were treated with bovine trypsin , chymotrypsin, or other enzymes.”