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Objective: Lectins are extremely significant biomolecules to study several biological progressions. In this present investigation, we are screening the crude phloem exudate/sap sample from different ethnomedicinal plants were evaluated for lectin and anticancer activity. Methods: The lectin activity of crude phloem exudate/sap samples were confirmed by haemgglutination assay and anticancer activity by using trypan blue, MTT and in-ovo CAM angiogenic assay. The tumor cell nuclei resulting in Giemsa stain, AO/EtBr stain, DNA Fragmentation and Caspase-3 inhibitor assay. Results: Our experimental data show that the phloem exudate/sap sample S2 (Musa Acuminata), sample S4 (Euphorbia Geniculate) exerting the potent lectin activity, sample S5 exerting very low lectin activity against the trypsinized rabbit erythrocytes and decreases the cell viability in EAC cells in-vitro. Sample S2, S4 and S5 exerts significant cytotoxic effect against the various human cancer cell lines and regressed the neovasculature (development of new blood vessels) in the developing CAM embryos when compared to the other crude samples. The apoptotic inducing activity of crude phloem exudate/sap samples was revealed by DNA fragmentation assay, caspase-3 inhibitor assay and cellular morphology were studied by fluorescence staining methods. Conclusion: This study reports that some of the isolated crude phloem exudate/sap samples show potent lectin activity and anti-cancer activity in different human cancer cell lines. The further additional experiment needs to purify and characterize the bioactive lectin components from the potent sample which is responsible for pro-apoptotic, anti-angiogenic activity and mechanism involved. [ABSTRACT FROM AUTHOR]

Lifestyle and nutritional changes have contributed much to the somatic genetic changes which have concurrently led to an increase cancer in humans. Hence the plant-based and nutritional involvements block oncogenic transformation are in good demand. We evaluate Phloem exudates of the dietary plant, Musa acuminate pseudostem, the initial domesticated plant species with the effective lectin activity for its functional role against the tumor development and its mechanism of action. Our experimental data exhibit that Musa acuminata Lectin Protein (MALP) shows a promising cytotoxic effect against the various human cancer cell lines. Supporting this, we evaluate the in vivo anti-tumor and anti-angiogenic activity of MALP in Ehrlich Ascites Carcinoma mice model (EAC). MALP treatment resulted in tumor growth inhibition and increased the lifespan of the EAC-bearing mice without showing any side effects on normal mice, as revealed by histological parameters. Further, a significant decrease in the ascites vascular endothelial growth factor (VEGF) secretion and microvessel density supports the anti-angiogenic property of the MALP. Apoptosis-inducing activity of MALP was revealed by DNA fragmentation assay, Caspase-3 inhibitor assay and cellular morphology were studied by fluorescence staining methods. Our study delivers the real evidence that MALP with a promising an anticancer potential expressively degenerates the tumor development by affecting angiogenesis and apoptosis. [ABSTRACT FROM AUTHOR]

This study aims to explore possible involvement of Sesbania grandiflora leaves extract on haemostatic pathway. The crude dialyzed fraction ( SgCDF ) hydrolyses casein and exhibiting a protease activity (19.7 ± 1.5 U/Hr) at 100 μg/ml. Zymography (casein) studies further reveal the presence of two high molecular weight protease(s). Presence of possible protease(s) was confirmed by inhibition of Proteolytic activity by mercury chloride (HgCl 2 ) suggesting the presence of Cysteine protease. The stability of protease activity against various parameters viz., temperature, pH, salt (NaCl) has been evaluated. These protease(s) exhibiting a promising Fibrinogenolytic activity by hydrolyzing Aα and Bβ subunit of fibrinogen at 25 μg and 50 μg concentration, whereas SgCDF fails to degrade the γ-subunit at the same concentration. The protease shows a promising recalcification time up to 80 ± 2% against Trypsin. These findings suggest the possible role of proteolytic fraction of Sesbania grandiflora in haemostatic and wound healing process. [ABSTRACT FROM AUTHOR]