A novel vasorelaxant lectin purified from seeds of Clathrotropis nitida : partial characterization and immobilization in chitosan beads

Alves, Ana Cecília; Vasconcelos, Mayron Alves de; Santiago, M.Q.; Pinto-Junior, Vanir Reis; Osterne, Vinicius Jose Da Silva; Lossio, Claudia Figueiredo; Bringel, Pedro Henrique Souza Ferreira; Castro, Rondinelle Ribeiro; Nagano, Celso Shiniti; Delatorre, P.; Souza, Luiz Augusto Gomes de; Nascimento, Kyria S.; Assreuy, Ana Maria Sampaio; Cavada, Benildo S.

doi:10.1016/j.abb.2015.10.020

Cited by 3 publications

(3 citation statements)

References 61 publications

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“…Purified lectin was found to be a glycoprotein as determined by PAS staining whereas carbohydrate content of lectin was observed up to 5.2%. Similar carbohydrate contents of lectin have been reported in case of lectin purified from Artocarpus integerifolia and Clathrotropis nitida [34] Hemagglutination activity of hyacinth lectin was inhibited by mannose and ovalbumin which suggested that its manose binding lectin which is one of the significant properties of lectin purified from monocotyledon plants. Hyacinth lectin showed moderate temperature and pH stability.…”

Section: Discussionsupporting

confidence: 79%

“…Carbohydrate content and glycosylation nature of Hyacinth bulb lectin was determined by anthrone assay and PAS staining respec- tively. The carbohydrate content of purified lectin was found to be 5.2% and according to literature carbohydrate content of lectin vary from 1.5 to 16% [33,34]. PAS stain result indicated that hyacinth lectin was glycoprotein in nature ( Fig.…”

Section: Carbohydrate Content and Glycosylation Nature Of Hyacinth Lementioning

confidence: 60%

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

Naik

Rawat

Khandai

et al. 2017

International Journal of Biological Macromolecules

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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.

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Section: Discussionsupporting

confidence: 79%

Section: Carbohydrate Content and Glycosylation Nature Of Hyacinth Lementioning

confidence: 60%

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

Naik

Rawat

Khandai

et al. 2017

International Journal of Biological Macromolecules

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“…The lectin proved to be thermostable with maximum activity at temperatures of 30 ºC, 40 ºC and 50 ºC, but its activity was reduced when 100 ºC was reached. Other lectins of the same botanical family show maximum activity at similar temperatures, such as the Collaea speciosa lectin isolated by Oliveira et al (2021) and the lectin isolated by Alves et al (2015) from seeds of Clathrotropis nitida, which showed low hemagglutinating activity at 100 ºC. Total dependence of CiL on divalent ions, as noted above, closely resembled the findings of Pinto-Junior et al (2016) who isolated a metal-dependent lectin from the seeds of Dioclea reflexa.…”

Section: Physicochemical Characterizationsupporting

confidence: 71%

A new lectin from Crotalaria incana seeds and studies of toxicity in Artemia salina nauplii

Pereira,

Martins,

Oliveira

et al. 2024

Acta Bot. Bras.

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Lectins are proteins that recognize and bind to carbohydrates in a reversible and specific manner. In this work, a lectin from Crotalaria incana L. seeds was purified by Sephadex G-50 affinity chromatography. The purified lectin was named CiL and presented affinity towards D-mannose, D-glucose, D-galactose, α-methyl-D-mannoside and derivatives. CiL was stable over a wide range of temperatures and pH values, and it was divalent cation-dependent. SDS-PAGE analysis indicated that CiL is composed of two subunits with apparent masses of 29 and 30 kDa. The amino acid sequence of five tryptic peptides was obtained through mass spectrometry. Partial primary structure data indicated the similarity between CiL and lectins from Phaseolus vulgaris, Cladrastis kentukea, Lens culinaris, Pisum sativum, Crotalaria pallida and C. juncea. CiL showed no toxicity to Artemia salina nauplii at the concentration of 2 mg/mL, thus reinforcing the potential of this protein for further studies in other biological models and elucidation of possible effects.

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A Review of the Leishmanicidal Properties of Lectins

Grangeiro,

Santos,

Barbosa

et al. 2024

CPPS

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Lectins are proteins widely distributed among plants, animals and microorganisms that have the ability to recognize and interact with specific carbohydrates. They have varied biological activities, such as the inhibition of the progression of infections caused by fungi, bacteria, viruses and protozoa, which is related to the interaction of these proteins with the carbohydrates present in the cell walls of these microorganisms. Leishmaniasis are a group of endemic infectious diseases caused by protozoa of the genus Leishmania. In vitro and in vivo tests with promastigotes and amastigotes of Leishmania demonstrated that lectins have the ability to interact with glycoconjugates present on the cell surface of the parasite, it prevents their development through various mechanisms of action, such as the production of ROS and alteration of membrane integrity, and can also interact with defense cells present in the human body, thus showing that these molecules can be considered alternative pharmacological targets for the treatment of leishmaniasis. The objective of the present work is to carry out a bibliographic review on lectins with leishmanicidal activity, emphasizing the advances and perspectives of research in this theme. Through the analysis of the selected studies, we were able to conclude that lectins have great potential for inhibiting the development of leishmaniasis. However, there are still few studies on this subject.

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A novel vasorelaxant lectin purified from seeds of Clathrotropis nitida : partial characterization and immobilization in chitosan beads

Cited by 3 publications

References 61 publications

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

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

A new lectin from Crotalaria incana seeds and studies of toxicity in Artemia salina nauplii

A Review of the Leishmanicidal Properties of Lectins

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