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A spider-derived Kunitz-type serine protease inhibitor that acts as a plasmin inhibitor and an elastase inhibitor.

PloS one (2013-01-12)
Hu Wan, Kwang Sik Lee, Bo Yeon Kim, Feng Ming Zou, Hyung Joo Yoon, Yeon Ho Je, Jianhong Li, Byung Rae Jin
ABSTRACT

Kunitz-type serine protease inhibitors are involved in various physiological processes, such as ion channel blocking, blood coagulation, fibrinolysis, and inflammation. While spider-derived Kunitz-type proteins show activity in trypsin or chymotrypsin inhibition and K(+) channel blocking, no additional role for these proteins has been elucidated. In this study, we identified the first spider (Araneus ventricosus) Kunitz-type serine protease inhibitor (AvKTI) that acts as a plasmin inhibitor and an elastase inhibitor. AvKTI possesses a Kunitz domain consisting of a 57-amino-acid mature peptide that displays features consistent with Kunitz-type inhibitors, including six conserved cysteine residues and a P1 lysine residue. Recombinant AvKTI, expressed in baculovirus-infected insect cells, showed a dual inhibitory activity against trypsin (K(i) 7.34 nM) and chymotrypsin (K(i) 37.75 nM), defining a role for AvKTI as a spider-derived Kunitz-type serine protease inhibitor. Additionally, AvKTI showed no detectable inhibitory effects on factor Xa, thrombin, or tissue plasminogen activator; however, AvKTI inhibited plasmin (K(i) 4.89 nM) and neutrophil elastase (K(i) 169.07 nM), indicating that it acts as an antifibrinolytic factor and an antielastolytic factor. These findings constitute molecular evidence that AvKTI acts as a plasmin inhibitor and an elastase inhibitor and also provide a novel view of the functions of a spider-derived Kunitz-type serine protease inhibitor.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Plasmin from human plasma, lyophilized powder, ≥2.0 units/mg protein
Sigma-Aldrich
α-Chymotrypsin−Agarose from bovine pancreas, lyophilized powder, 2,000-3,500 units/g agarose (One ml gel will yield 65-120 units)
Sigma-Aldrich
Elastase from porcine pancreas, Type IV, Protein 50-90 %, lyophilized powder, ≥4.0 units/mg protein (biuret)
Sigma-Aldrich
Aprotinin from bovine lung, saline solution, 3-7 TIU/mg protein
Sigma-Aldrich
α-Chymotrypsin from human pancreas, lyophilized powder
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Elastase from porcine pancreas, Type III, lyophilized powder, Protein 55-85 %, ≥4.0 units/mg protein
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Elastase from porcine pancreas, lyophilized powder, suitable for cell culture
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Aprotinin from bovine lung, lyophilized powder, 3-7 TIU/mg solid
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Aprotinin from bovine lung, lyophilized powder, 3-8 TIU/mg solid, BioReagent, suitable for cell culture
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Aprotinin from bovine lung, lyophilized powder, 3-8 TIU/mg solid
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Aprotinin from bovine lung, lyophilized, ~80% (HPCE), crystalline (fine), white, ≥3500 U/mg
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α-Chymotrypsin from bovine pancreas, (TLCK treated to inactivate residual tryspin activity), Type VII, essentially salt-free, lyophilized powder, ≥40 units/mg protein
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α-Chymotrypsin from bovine pancreas, ≥40 units/mg protein, vial of 5 mg
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α-Chymotrypsin from bovine pancreas, Type II, lyophilized powder, ≥40 units/mg protein
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α-Chymotrypsin from bovine pancreas, suitable for protein sequencing, salt-free, lyophilized powder
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α-Chymotrypsin from bovine pancreas, Type I-S, essentially salt-free, lyophilized powder
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Elastase from porcine pancreas, Type I, ≥4.0 units/mg protein
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Aprotinin from bovine lung
Sigma-Aldrich
Aprotinin from bovine lung, BioUltra, 3-8 TIU/mg solid, ≥98% (SDS-PAGE)