A serine proteinase inhibitor isolated from Tamarindus indica seeds and its effects on the release of human neutrophil elastase. Life Sci

Departamento de Bioquímica, Centro de Biociências, Universidade Federal do Rio Grande do Norte, Campus Universitário, 59072-970, Natal, RN, Brasil.
Life Sciences (Impact Factor: 2.7). 06/2005; 76(25):2881-91. DOI: 10.1016/j.lfs.2004.10.053
Source: PubMed


Proteinaceous inhibitors with high inhibitory activities against human neutrophil elastase (HNE) were found in seeds of the Tamarind tree (Tamarindus indica). A serine proteinase inhibitor denoted PG50 was purified using ammonium sulphate and acetone precipitation followed by Sephacryl S-300 and Sephadex G-50 gel filtration chromatographies. Inhibitor PG50 showed a Mr of 14.9 K on Sephadex G-50 calibrated column and a Mr of 11.6 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. PG50 had selective activity while cysteine proteinases (papain and bromelain) and serine proteinases (porcine pancreatic elastase and bovine chymotrypsin) were not inhibited, it was strongly effective against serine proteinases such as bovine trypsin and isolated human neutrophil elastase. The IC50 value was determined to be 55.96 microg.mL-1. PG50 showed neither cytotoxic nor haemolytic activity on human blood cells. After pre-incubation of PG50 with cytochalasin B, the exocytosis of elastase was initiated using PAF and fMLP. PG50 exhibited different inhibition on elastase release by PAF, at 44.6% and on release by fMLP, at 28.4%. These results showed that PG50 preferentially affected elastase release by PAF stimuli and this may indicate selective inhibition on PAF receptors.


Available from: Leonardo Lima Pepino de Macedo, Apr 01, 2015
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    • "indica). A serine proteinase inhibitor denoted PG50 was purified using ammonium sulfate and acetone precipitation activity showed that PG50 preferentially affected elastase release by platelet activating factor stimuli and this may indicate selective inhibition on platelet activating factor (PAF) receptors.[109] Other bioinsecticidal studies included both in vivo and in vitro studies. "
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    ABSTRACT: Tamarindus is a monotypic genus and belongs to the subfamily Caesalpinioideae of the family Leguminosae (Fabaceae), Tamarindus indica L., commonly known as Tamarind tree is one of the most important multipurpose tropical fruit tree species in the Indian subcontinent. Tamarind fruit was at first thought to be produced by an Indian palm, as the name Tamarind comes from a Persian word "Tamar-I-hind," meaning date of India. Its name "Amlika" in Sanskrit indicates its ancient presence in the country. T.indica is used as traditional medicine in India, Africa, Pakistan, Bangladesh, Nigeria,and most of the tropical countries. It is used traditionally in abdominal pain, diarrhea and dysentery, helminthes infections, wound healing, malaria and fever, constipation, inflammation, cell cytotoxicity, gonorrhea, and eye diseases. It has numerous chemical values and is rich in phytochemicals, and hence the plant is reported to possess antidiabetic activity, antimicrobial activity, antivenomic activity, antioxidant activity, antimalarial activity, hepatoprotective activity, antiasthmatic activity, laxative activity, and anti-hyperlipidemic activity. Every part of the plant from root to leaf tips is useful for human needs. Thus the aim of the present review is to describe its morphology, and explore the phytochemical constituents, commercial utilization of the parts of the plant, and medicinal and pharmacologic activities so that T. indica's potential as multipurpose tree species can be understood.
    Pharmacognosy Reviews 03/2011; 5(9):73-81. DOI:10.4103/0973-7847.79102
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    • "Among various groups of protease inhibitors, the serine protease inhibitors are the most studied and have been purified from various legume seeds (Oliveira et al., 2007; Araújo et al., 2005; Macedo et al., 2004; Mello et al., 2002; Oliva et al., 2000). Many reports showed that serine protease inhibitors have the capacity to inhibit elastase, a serine protease found in the azurophilic granules of neutrophils (Hojima., 1983; Larinova., 1993; Fook et al., 2005). In legume seeds, the soy (Glicine max), revealed such a rich source of serine protease inhibitors against human neutrophil elastase: soybean Kunitz trypsin inhibitors (SKTIs) and Bowman-Birk inhibitors (BBIs). "
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    ABSTRACT: 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.
    European journal of pharmacology 10/2010; 644(1-3):238-44. DOI:10.1016/j.ejphar.2010.06.067 · 2.53 Impact Factor
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    • "Since the past decade, natural compounds and plant extracts have been the targets of research as a potential source to explore for efficient elastase inhibitors [24] [25] [26] [27] [28]. The aim of this study was therefore to investigate the effects of a variety of extracts from some Yemeni plants on the activity of human neutrophil elastase. "

    Planta Medica 07/2008; 74(09). DOI:10.1055/s-0028-1084168 · 2.15 Impact Factor
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