Embryotoxic activity and differential binding of plant-derived carbohydrate-recognizing proteins towards the sea urchin embryo cells

Macedo, Nívea Maria R.; Costa-Lotufo, Letı́cia V.; Wilke, Diego Veras; Bomfim, Liezelotte R.; Pessoa, Cláudia; Moraes, Manoel Odoríco de; Ramos, Márcio V.

doi:10.1016/j.ijbiomac.2005.03.014

Cited by 5 publications

(7 citation statements)

References 37 publications

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“…As one example from such diversity, many plant lectins induce changes in the course of inflammatory processes in acute inflammation models [3]. Frequently, previous incubation of a lectin with the specific carbohydrate inhibitor of its hemagglutinating activity rendered the lectin unable to provoke any effect, thus confirming the involvement of the carbohydrate-binding domain in mediating the biological effect studied [4]. These findings were important to the understanding of the general requirements of the lectins to display anti-inflammatory and other activities [5].…”

Section: Introductionmentioning

confidence: 90%

An anti-inflammatory lectin from Luetzelburgia auriculata seeds inhibits adhesion and rolling of leukocytes and modulates histamine and PGE2 action in acute inflammation models

et al. 2009

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Section: Introductionmentioning

confidence: 90%

An anti-inflammatory lectin from Luetzelburgia auriculata seeds inhibits adhesion and rolling of leukocytes and modulates histamine and PGE2 action in acute inflammation models

et al. 2009

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“…In a previous report, we have shown the ability of some plant lectins in detecting changes in the glycoconjugates patterns during embryogenesis of sea urchin [4]. The present manuscript reports binding of lectins differing in terms of monosaccharide specificity to eggs and sperms of the sea urchin Lytechinus variegatus and their inhibitory effect on the in vitro fertilization.…”

Section: Introductionmentioning

confidence: 60%

“…Molecular basis of carbohydrate recognition during sperm/egg interaction as well as structural information of these receptors is still limited and it is expected to be unique for each species. Studies on this direction are additionally difficult since dynamics of these glycoconjugates in eggs surface are particularly intense immediately after fertilization [4]. This further limits extraction and isolation of such structures in view of their full structural and functional characterization.…”

Section: Introductionmentioning

confidence: 99%

“…The sea urchin fertilization process is an excellent model for the in vivo study of effects caused by drugs, temperature or other factors on cell metabolism as it can be followed over a short time-course [4]. Accordingly, this model has been explored to study toxic effects of natural products or engineered drugs in attempt to understand and quantify the extent of their action on cells [5].…”

Section: Introductionmentioning

confidence: 99%

“…The potential of lectins to perceive changes in the glycoconjugate properties of cell membranes throughout cell differentiation can therefore be tested using the sea urchin embryogenesis model [4]. Lectins are proteins with an ability to recognize and bind certain monosaccharides and some of their corresponding derivatives [9].…”

Section: Introductionmentioning

confidence: 99%

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Inhibition of Sea Urchin Fertilization by Plant Lectins

Macedo

Costa-Lotufo²,

Pessoa³

et al. 2007

PPL

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Effects of plant lectins on sea urchin (Lytechinus variegatus) fertilization and a partial characterization of lectin-binding involved in the process were evaluated. IC50 doses for inhibition of fertilization varied from 4.1 to 135.5 microg/ml when the lectins were pre-incubated with sperms and from 0.7 to 33.4 microg/ml when pre-incubated with eggs. Such effects were reversed when the lectins were heat inactivated. FITC-labeled lectins bound egg surfaces while their denatured forms did not. Glucose/mannose specific lectins bound weaker to eggs when pre-incubated with the glycoprotein bovine lactotransferrin. None of the glycoproteins assayed diminished FITC patterns of the Gal/GalNAc binding lectins. Pre-incubation of Glucose/mannose binding lectins with eggs did not alter binding of Gal/GalNAc lectins. Lectins with distinct competencies for binding monosaccharide and glycoconjugates were able to inhibit sea urchin fertilization.

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Toxic effects of Microgramma vacciniifolia rhizome lectin on Artemia salina, human cells, and the schistosomiasis vector Biomphalaria glabrata

et al. 2014

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The present study evaluated the toxicity of Microgramma vacciniifolia rhizome lectin (MvRL) to Artemia salina, human tumour cell lines (larynx epidermoid carcinoma Hep-2, NCI-H292 lung mucoepidermoid carcinoma, and chronic myelocytic leukaemia K562), and normal peripheral blood mononuclear cells (PBMCs), as well as to Biomphalaria glabrata embryos and adults. MvRL was toxic to A. salina (LC50=159.9 μg/mL), and exerted cytotoxic effects on NCI-H292 cells (IC50=25.23 μg/mL). The lectin (1-100 μg/mL) did not affect the viability of K562 and Hep-2 tumour cells, as well as of PBMCs. MvRL concentration of 1, 10, and 100 μg/mL promoted malformations (mainly exogastrulation) in 7.8%, 22.5%, and 27.7% of embryos, respectively, as well as delayed embryo development in 42.0%, 69.5%, and 54.7% of embryos, respectively. MvRL at a concentration of 100 μg/mL killed B. glabrata embryos (17.7%) and adults (25%). Further, MvRL damaged B. glabrata reproductive processes, which was evidenced by observations that snails exposed to the lectin (100 μg/mL) deposited fewer eggs than those in the control group, and approximately 40% of the deposited eggs exhibited malformations. Comparison of these results with that from A. salina assay indicates that MvRL is adulticidal at the concentration range which is toxic to environment. In conclusion, the cytotoxicity of MvRL on tumour cell and absence of toxicity to normal cell indicate its potential as chemotherapeutic drug. Also, the study revealed that the lectin is able to promote deleterious effects on B. glabrata embryos at environmentally safe concentrations.

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Embryotoxic activity and differential binding of plant-derived carbohydrate-recognizing proteins towards the sea urchin embryo cells

Cited by 5 publications

References 37 publications

An anti-inflammatory lectin from Luetzelburgia auriculata seeds inhibits adhesion and rolling of leukocytes and modulates histamine and PGE2 action in acute inflammation models

An anti-inflammatory lectin from Luetzelburgia auriculata seeds inhibits adhesion and rolling of leukocytes and modulates histamine and PGE2 action in acute inflammation models

Inhibition of Sea Urchin Fertilization by Plant Lectins

Toxic effects of Microgramma vacciniifolia rhizome lectin on Artemia salina, human cells, and the schistosomiasis vector Biomphalaria glabrata

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