Seeds from legumes including the Gilcine max are known to be a rich source of protease inhibitors. The soybean Kunitz trypsin inhibitors (SKTIs) have been well characterised and have been found to exhibit many biological activities. However their effects on inflammatory diseases have not been studied to date. In this study, SKTI was purified using anion exchange chromatography using a Resource Q column. The purified protein was able to inhibit human neutrophil elastase (HNE) and bovine trypsin. Purified SKTI inhibited HNE with an IC(50) value of 8mug or 0.3nM. At this concentration SKTI showed neither cytotoxic nor haemolytic effects on human blood cell populations. SKTI showed no deleterious effects on organs, blood cells or the hepatic enzymes ALT and AST in the mouse model of acute systemic toxicity. Human neutrophils incubated with SKTI released less HNE than control neutrophils when stimulated with PAF or fMLP (83.1% and 70% respectively). These results showed that SKTI affected both pathways of elastase release by PAF and fMLP stimuli, suggesting that SKTI is an antagonist of fMLP/PAF receptors. In an in vivo mouse model of LPS acute lung injury, SKTI significantly suppressed the inflammatory effects caused by elastase in a dose-dependent manner. Histological sections stained by hematoxylin/eosin confirmed this decrease in inflammation. These results showed that SKTI could be used as a pharmacological agent for the therapy of many inflammatory diseases.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.ejphar.2010.06.067 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Bovine pancreatic trypsin inhibitor and soybean Kunitz trypsin inhibitor: Differential effects on proteases and larval development of the soybean pest Anticarsia gemmatalis (Lepidoptera: Noctuidae).
Pestic Biochem Physiol
October 2022
Departamento de Bioquímica e Biologia Molecular, Universidade Federal de Viçosa, Minas Gerais, Brazil; Instituto de Biotecnologia aplicada à Agropecuária, BIOAGRO-UFV, Viçosa, Minas Gerais, Brazil. Electronic address:
Pest management is challenged with resistant herbivores and problems regarding human health and environmental issues. Indeed, the greatest challenge to modern agriculture is to protect crops from pests and still maintain environmental quality. This study aimed to analyze by in silico, in vitro, and in vivo approaches to the feasibility of using the inhibitory protein extracted from mammals - Bovine Pancreatic Trypsin Inhibitor (BPTI) as a potential inhibitor of digestive trypsins from the pest Anticarsia gemmatalis and comparing the results with the host-plant inhibitor - Soybean Kunitz Trypsin Inhibitor (SKTI).
View Article and Find Full Text PDFInhibition constant and stability of tripeptide inhibitors of gut trypsin-like enzyme of the soybean pest Anticarsia gemmatalis.
Arch Insect Biochem Physiol
June 2022
Departamento de Bioquímica e Biologia Molecular, Universidade Federal de Viçosa, Viçosa, Minas Gerais, Brazil.
Insects overcome the action of natural protease inhibitors (PIs) due to evolutionary adaptations through endogenous proteolysis and reprogramming proteases. Insect adaptations complicate the formulation of IP-based crop protection products. However, small peptides designed based on the active site of enzymes have shown promising results that could change this scenario.
View Article and Find Full Text PDFIntestinal proteases profiling from Anticarsia gemmatalis and their binding to inhibitors.
Arch Insect Biochem Physiol
July 2021
Department of Biochemistry and Molecular Biology, Laboratory of Enzymology and Biochemistry of Proteins and Peptides, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa, Minas Gerais, Brazil.
Although the importance of intestinal hydrolases is recognized, there is little information on the intestinal proteome of lepidopterans such as Anticarsia gemmatalis. Thus, we carried out the proteomic analysis of the A. gemmatalis intestine to characterize the proteases by LC/MS.
View Article and Find Full Text PDFInhibition kinetics of digestive proteases for Anticarsia gemmatalis.
An Acad Bras Cienc
June 2020
Departamento de Bioquímica e Biologia Molecular, Instituto de Biotecnologia Aplicada a Agropecuária/BIOAGRO, Viçosa, MG, Brazil.
Anticarsia gemmatalis Hübner, 1818 (Lepidoptera) is a major pest of soybean in the Brazil. It is known that the reduction of proteolytic activity by the ingestion of protease inhibitors reduces digestion and larval development of the insects. Control via inhibition of the digestive enzymes necessitates deeper knowledge of the enzyme kinetics and the characterization of the inhibition kinetics of these proteases, for better understanding of the active centers and action mechanisms of this enzyme.
View Article and Find Full Text PDFPreparation and Irreversible Inhibition Mechanism Insight into a Recombinant Kunitz Trypsin Inhibitor from Glycine max L. Seeds.
Appl Biochem Biotechnol
July 2020
State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, 200237, China.
Soybean Kunitz trypsin inhibitor (SKTI), extracted from soybean (Glycine max L.) seeds, possesses insect resistance and anti-tumor properties. But its specific mechanisms of action are not yet known.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!