Biochemical characterisation of lectin from Indian hyacinth plant bulbs with potential inhibitory action against human cancer cells

Abstract

This work describes purification and characterisation of a monocot mannose-specific lectin from Hyacinth bulbs. The purified lectin has a molecular mass of ∼30kDa in reducing as well as in non-reducing SDS-PAGE. In hydrodynamic studies by Dynamic Light Scattering (DLS) showed that purified lectin was monomeric in nature with a molecular size of 2.38±0.03nm. Agglutination activity of purified lectin was confirmed by rabbit erythrocytes and its agglutination activity was inhibited by d-mannose and a glycoprotein (ovalbumin). Glycoprotein nature of purified lectin was confirmed by Periodic Acid Schiff's (PAS) stain. Purified lectin showed moderate pH and thermal stability by retaining hemagglutination activity from pH 6-8 and temperature up to 60°C. It also suppressed the growth of human colon cancer cells (Caco-2) and cervical cancer cells (HeLa) with IC values of 127μg/mL and 158μg/mL respectively, after 24-h treatment. Morphological studies of treated cells (Caco-2 and HeLa) with hyacinth lectin by AO/EB dual staining indicated that purified lectin is capable of inducing apoptosis.

Comparative clinical significance and biological roles of PFKFB family members in oral squamous cell carcinoma

“…Although PFKFB3 inhibitors such as 3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one (3PO) [ 69 ] or PFKFB4 inhibitor such as 5-(n-(8-methoxy-4-quinolyl)amino)pentyl nitrate (5MPN) have been reported, their problems in low specificity and off targets are difficult to avoid [ 67 ]. Therefore, identifying more effective small molecule by computational approach involving virtual screening, drug-likeness, ADEM (absorption, distribution, metabolism, and excretion), molecular docking simulation, thermodynamic free energy calculations, per residue binding free energy contribution[ 70 ] and silico approach [ 71 ] or identifying plant extracts for inhibition of PFKFB3 and PFKFB4 enzymes for OSCC therapy is essential [ 72 ].…”

Legume Lectins with Different Specificities as Potential Glycan Probes for Pathogenic Enveloped Viruses

“…Initially recognized as potent mitogenic proteins [131][132][133], plant lectins have been known for a long time as non-specific immune-modulatory proteins that are susceptible to interaction with various cell surface glycoproteins/glycolipids and for interfering with various signaling pathways triggering cytotopathologic effects on the targeted cells. Although most plant lectins with antiviral activity activate different sets of T lymphocytes and, more scarcely, B lymphocytes, they also activate both the apoptotic and necrotic pathways in many other types of healthy and cancer cells [134][135][136][137][138][139][140][141][142][143]. The cellular activation mediated by plant lectins on healthy and transformed cells elicits the release of various chemokines and/or cytokines that are, in turn, susceptible to interfere with the cytokine stimulation associated with the viral infection, e.g., HIV infection [59].…”

Applications of Plant Lectins in Biotechnology and Therapeutics

“…The selective nature of phytohemagglutinin named as lectin from the Latin verb that's means "to select" proposed by Boyd and Shapleigh (Hou et al, 2003). Lectins are isolated and characterized by almost all five kingdoms (Monera, Protista, Fungi, Plantae, and Animalia) (Naik et al, 2017). In case of plants, the source of lectins are roots, bulbs, pulps, tubers, rhizome, latex, barks, stems, leaves, flowers, fruits, and seeds (Table 1).…”