TY - JOUR
T1 - The bovine basic pancreatic trypsin inhibitor (Kunitz inhibitor)
T2 - A milestone protein
AU - Ascenzi, Paolo
AU - Bocedi, Alessio
AU - Bolognesi, Martino
AU - Spallarossa, Andre
AU - Colletta, Massimo
AU - De Cristofaro, Raimondo
AU - Menegatti, Enea
PY - 2003/6
Y1 - 2003/6
N2 - 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 chymotrypsin- and 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.
AB - 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 chymotrypsin- and 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.
KW - Aprotinin
KW - Bio-medical aspects
KW - Bovine basic pancreatic trypsin inhibitor
KW - Inhibition properties
KW - Kunitz inhibitor
KW - Structure
KW - Trypsin-kallikrein inhibitor
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U2 - 10.2174/1389203033487180
DO - 10.2174/1389203033487180
M3 - Article
C2 - 12769721
AN - SCOPUS:0012813996
VL - 4
SP - 231
EP - 251
JO - Current Protein and Peptide Science
JF - Current Protein and Peptide Science
SN - 1389-2037
IS - 3
ER -