Title: The Bovine Basic Pancreatic Trypsin Inhibitor (Kunitz Inhibitor): A Milestone Protein
Volume: 4
Issue: 3
Author(s): Paolo Ascenzi, Alessio Bocedi, Martino Bolognesi, Andrea Spallarossa, Massimo Coletta, Raimondo De Cristofaro and Enea Menegatti
Affiliation:
Keywords:
aprotinin, bovine basic pancreatic trypsin inhibitor, kunitz inhibitor, trypsin-kallikrein inhibitor, structure, inhibition properties, bio-medical aspects
Abstract: The pancreatic Kunitz inhibitor, also known as aprotinin, bovine basic pancreatic trypsin inhibitor (BPTI), and trypsin-kallikrein inhibitor, is one of the most extensively studied globular proteins. It has proved to be a particularly attractive and powerful tool for studying protein conformation as well as molecular bases of protein / protein interaction(s) and (macro)molecular recognition. BPTI has a relatively broad specificity, inhibiting trypsin- as well as chymotrypsinand elastase-like serine (pro)enzymes endowed with very different primary specificity. BPTI reacts rapidly with serine proteases to form stable complexes, but the enzyme:inhibitor complex formation may involve several intermediates corresponding to discrete reaction steps. Moreover, BPTI inhibits the nitric oxide synthase type-I and -II action and impairs K+ transport by Ca2+-activated K+ channels. Clinically, the use of BPTI in selected surgical interventions, such as cardiopulmonary surgery and orthotopic liver transplantation, is advised, as it significantly reduces hemorrhagic complications and thus blood-transfusion requirements. Here, the structural, inhibition, and bio-medical aspects of BPTI are reported.
