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: 2.3). 06/2005; 76(25):2881-91. DOI: 10.1016/j.lfs.2004.10.053
Source: PubMed

ABSTRACT 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.

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Available from: Leonardo Lima Pepino de Macedo, Apr 01, 2015
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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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