Immunomodulatory and anti-tumor activities of native and heat denatured Abrus agglutinin

Ghosh, Dipanjan; Maiti, Tapas K.

doi:10.1016/j.imbio.2007.03.005

Cited by 34 publications

(16 citation statements)

References 31 publications

(31 reference statements)

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“…Various African tribes use AP powdered seeds as oral contraceptives (Watt and Breyer-Brandwijk, 1962). AP possesses different pharmacological activities including antifertility (Ross, 2005), anti-implantation (Okoko et al, 2010), antimicrobial (Adelowotan et al, 2008), antitumor (Ghosh and Maiti, 2007), immunopotentiating (Ramnath et al, 2002) and sperm antimotility. Zia-ul-Haque et al (1983b) reported the post-coital (days 2-5) antifertility (100% sterility) effect of abridine, isolated constituent from AP, when administered p.o.…”

Section: Abrus Precatorius Linn (Family: Fabaceae)mentioning

confidence: 99%

Potential antifertility agents from plants: A comprehensive review

Kumar

Prakash

2012

Journal of Ethnopharmacology

116

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Section: Abrus Precatorius Linn (Family: Fabaceae)mentioning

confidence: 99%

Potential antifertility agents from plants: A comprehensive review

Kumar

Prakash

2012

Journal of Ethnopharmacology

116

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“…The anti-pathogenic activities of plant lectins enable themselves to act as defense proteins to protect the plants from invasion of harmful organisms. Other than for the plants’ own uses, the plant lectins also exhibit other biological activities, such as inducing mitogenic response in mammalian splenocytes [1], [2], [6] and anti-proliferative effects toward tumor cells [7], [8]. These activities provide insights for plant lectins to be applied to humans for therapeutic uses, such as development of immunomodulatory drugs or anti-tumor drugs.…”

Section: Introductionmentioning

confidence: 99%

Isolation of a Glucosamine Binding Leguminous Lectin with Mitogenic Activity towards Splenocytes and Anti-Proliferative Activity towards Tumor Cells

et al. 2012

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A dimeric 64-kDa glucosamine-specific lectin was purified from seeds of Phaseolus vulgaris cv. “brown kidney bean.” The simple 2-step purification protocol involved affinity chromatography on Affi-gel blue gel and gel filtration by FPLC on Superdex 75. The lectin was absorbed on Affi-gel blue gel and desorbed using 1M NaCl in the starting buffer. Gel filtration on Superdex 75 yielded a major absorbance peak that gave a single 32-kDa band in SDS-PAGE. Hemagglutinating activity was completely preserved when the ambient temperature was in the range of 20°C–60°C. However, drastic reduction of the activity occurred at temperatures above 65°C. Full hemagglutinating activity of the lectin was observed at an ambient pH of 3 to 12. About 50% activity remained at pH 0–2, and only residual activity was observed at pH 13–14. Hemagglutinating activity of the lectin was inhibited by glucosamine. The brown kidney bean lectin elicited maximum mitogenic activity toward murine splenocytes at 2.5 µM. The mitogenic activity was nearly completely eliminated in the presence of 250 mM glucosamine. The lectin also increased mRNA expression of the cytokines IL-2, TNF-α and IFN-γ. The lectin exhibited antiproliferative activity toward human breast cancer (MCF7) cells, hepatoma (HepG2) cells and nasopharyngeal carcinoma (CNE1 and CNE2) cells with IC50 of 5.12 µM, 32.85 µM, 3.12 µM and 40.12 µM respectively after treatment for 24 hours. Flow cytometry with Annexin V and propidum iodide staining indicated apoptosis of MCF7 cells. Hoechst 33342 staining also indicated formation of apoptotic bodies in MCF7 cells after exposure to brown kidney bean lectin. Western blotting revealed that the lectin-induced apoptosis involved ER stress and unfolded protein response.

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“…Lectins (AGG and ABR) bind to the terminal galactose residue of cell surface receptors through the B subunit, enter the cells by receptor mediated endocytosis, and are finally transported to the endoplasmic reticulum (ER) by the retrograde pathway. Interestingly, AGG in a heat-denatured condition (prepared by maintaining it at 50 C for 30 minutes and then immediately at 100 C for 2 minutes in a water bath) exerts similar types of cellular growth inhibition potential as demonstrated in DL cells (Ghosh & Maiti, 2007). The depurination prevents the binding of ribosome to elongation factors, thereby arresting the protein synthesis that causes cell death.…”

Section: Applications To Health Promotion and Disease Preventionmentioning

confidence: 89%