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- MakaleYalnız künye2026Scopus SJRQ3A new lectin from Amanita vaginata mushroom with potent anti-inflammatory activity
Seliman, Thoiba Mogahid Hussein; Ozsoy, Nurten; Altiparmak-Ulbegi, Gulsum; Alp-Kavlo, Hevidar; Arcan, Gulsah Gamze; Akev, Nuriye; Can, Ayse; Aksoy-Sagirli, Pinar
This study used 80% ammonium sulphate fractional precipitation, followed by affinity chromatography to purify a new lectin (AVL) from the crude extract of the Amanita vaginata mushroom. The purification procedure achieved a 20% yield, a specific activity of 5120 HU/mg protein, and a 16-fold increase in purity. SDS-PAGE analysis showed a single band of 45 kDa. We assessed AVL's anti-inflammatory effect by measuring levels of inducible nitric oxide synthase (iNOS) and cyclooxygenase-2 (COX-2), induced by lipopolysaccharide (LPS), in RAW 264.7 macrophages. Western blot analysis showed that iNOS and COX-2 protein levels were barely detectable in the control groups, but markedly elevated in the LPS-treated groups. However, AVL treatment significantly inhibited the expression of both iNOS and COX-2 in LPS-stimulated cells. This effect was dose-dependent. These findings suggest that AVL's anti-inflammatory effects are mediated through the suppression of iNOS and COX-2 expression.
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- MakaleAçık Erişim2024Anti-inflammatory activity of a novel lectin isolated from Pleurotus eryngii var. ferulae mushroom
Seliman, Thoiba Mogahid Hussein; Ülbegi, Gulsum Altiparmak; Ozsoy, Nurten; Kavlo, Hevidar Alp; Sagirli, Pinar Aksoy
Background and Aims: Pleurotus species are edible mushrooms with important economic and medicinal value. Many pharmacological properties of these species, such as anticancer, immunomodulating, and anti-inflammatory activities, have been attributed to lectin. The aim of this study was to purify a novel lectin from Pleurotus eryngii var. ferulae (PEFL) and investigate its anti-inflammatory activity. Methods: PEFL was purified by 80% ammonium sulphate fractionation, diethylaminoethyl (DEAE)-Sepharose-4B anion exchange, and Sephadex G-100 gel filtration chromatography. The molar mass of the purified lectin was determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) under denaturing conditions. Inhibition of lectin-induced haemagglutination by several carbohydrates and one glycoprotein (ovalbumin) was also performed using the haemagglutination inhibition activity test. The anti-inflammatory effect of PEFL was tested in a lipopolysaccharide (LPS)-induced inflammation model in mouse macrophage cells (RAW 264.7). The levels of prostaglandin (PG)-E2, tumour necrosis factor-alpha (TNF-alpha), interleukin1-beta (IL-1 beta), interleukin-6 (IL-6), interleukin-10 (IL-10), and interferon-gamma (IFN-gamma) were determined using enzyme-linked immunosorbent assay (ELISA) kits. Furthermore, the expression of nitric oxide synthase (iNOS) and cyclooxygenase-2 (COX-2) was estimated by western blot analysis. Results: PEFL was obtained in 16% yield. The specific activity of PEFL was calculated as 1280 haemagglutinating units (HU)/mg protein and was inhibited only by D-galactose. The molecular weight was determined to be 46 kDa. PEFL showed an anti-inflammatory effect by reducing the production of pro-inflammatory PGs through COX-2 inhibition, as well as reducing iNOS expression. Furthermore, our findings reported that PEFL has a protective effect on inflammation by decreasing the production of pro-inflammatory cytokines and increasing the production of the anti-inflammatory cytokine (IL-10). Conclusion: The results suggest that PEFL can be considered as a potential therapeutic agent in the development of new therapeutic strategies for inflammatory diseases.
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