Purification and characterization of a galactose-specific lectin from corn (Zea mays) coleoptyle

Cruz, Margarito Martínez; Zenteno, Edgar; Córdoba, Félix

doi:10.1016/s0304-4165(01)00196-9

Cited by 22 publications

(15 citation statements)

References 38 publications

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“…Other legumes may contain 20 g of lectin per 100 g of flour (Burbano et al, 1999;Makkar et al, 1997). In addition to legumes, other foods may contain considerable amounts of lectins, such as amaranth (8.3%, Hernandez-Infante et al, 1998) and corn (0.8%, Martinez-Cruz et al, 2001). These also include cereal type foods (187.2 µg of lectin/g) and texturized protein flour (12.9 µg lectin/g).…”

Section: Introductionmentioning

confidence: 99%

Lectins as Bioactive Plant Proteins: A Potential in Cancer Treatment

Mejı́a

Prisecaru

2005

Critical Reviews in Food Science and Nutrition

292

159

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Plant lectins, a unique group of proteins and glycoproteins with potent biological activity, occur in foods like wheat, corn, tomato, peanut, kidney bean, banana, pea, lentil, soybean, mushroom, rice, and potato. Thus, dietary intakes by humans can be significant. Many lectins resist digestion, survive gut passage, and bind to gastrointestinal cells and/or enter the circulation intact, maintaining full biological activity. Several lectins have been found to possess anticancer properties in vitro, in vivo, and in human case studies; they are used as therapeutic agents, preferentially binding to cancer cell membranes or their receptors, causing cytotoxicity, apoptosis, and inhibition of tumor growth. These compounds can become internalized into cells, causing cancer cell agglutination and/or aggregation. Ingestion of lectins also sequesters the available body pool of polyamines, thereby thwarting cancer cell growth. They also affect the immune system by altering the production of various interleukins, or by activating certain protein kinases. Lectins can bind to ribosomes and inhibit protein synthesis. They also modify the cell cycle by inducing non-apoptotic G1-phase accumulation mechanisms, G2/M phase cell cycle arrest and apoptosis, and can activate the caspase cascade. Lectins can also downregulate telomerase activity and inhibit angiogenesis. Although lectins seem to have great potential as anticancer agents, further research is still needed and should include a genomic and proteomic approach.

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Section: Introductionmentioning

confidence: 99%

Lectins as Bioactive Plant Proteins: A Potential in Cancer Treatment

Mejı́a

Prisecaru

2005

Critical Reviews in Food Science and Nutrition

292

159

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“…The fact that TOA activity disappeared in the shoot, stem and leaves and essentially completely in the rump of the cotyledons by the 15th day of seed planting and would not be present in the mature plant only after seed formation argues in favour of the position that the agglutinin is not required throughout plant development. Although no direct information has been adduced in this work on the matter, it appears unlikely that the agglutinin is present for plant defensive purposes as suggested by Peuman and Van Damme (1995) and by Martinez-Cruz et al, (2001) who have proposed specific interactions with rhizobial components or microorganisms.…”

Section: Discussionmentioning

confidence: 80%

“…It is also supported by the observations of Brill et al (2001), who, using genetic engineering techniques to analyze the functions of lectin genes, concluded that the gene products are not only important for embryogenesis, but are also required throughout plant development. It is instructive to compare some of the observations described above with the results obtained by Martinez-Cruz et al (2001), from their studies on the lectin from corn (Zea mays) coleoptiles, which had the highest specific activity at the 7th day after seeding. In spite of the fact that T. occidentalis and Zea mays belong in two different classes, the functional lectin in each case is Galactoside-binding while the activity during germination peaked, in each case, on the seventh day.…”

Section: Discussionmentioning

confidence: 85%

On the Possible Function of Telfairia occidentalis Agglutinin in the Plant

Togun¹,

Otusanya²,

Aboderin³

2004

BMB Reports

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The fate of Telfairia occidentalis seed Agglutinin, TOA, has been monitored during germination. While the level of the Agglutinin in the cotyledons decreased sharply in the first three days to about half of the initial level, it stabilises at this level for the following twelve days. In this interval, Agglutinin activity becomes manifest in the radicle on the fourth day, peaking on the fifth and decreasing rapidly thereafter. In the plumule, the lectin activity becomes manifest on the sixth day, peaks on the seventh and decreases rapidly thereafter. No lectin activity is detectable in any plant tissue including the rump of the cotyledons twenty-seven days after germination. The implications of these observations on the possible role of lectins in plants are discussed.

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“…The agglutination activity of ZmCORp was demonstrated via assays with conidia and erythrocytes. The clumping action of the protein, at concentrations comparable to those used in the characterization of other lectins (10,21), and the effect on conidia of A. flavus and sheep erythrocytes reveals the lectin-like activity of ZmCORp. ZmCORp also largely inhibited fungal germination and the elongation of hyphae.…”

Section: Discussionmentioning

confidence: 91%

A Maize Lectin-Like Protein with Antifungal Activity against Aspergillus flavus

Baker

Brown

Chen

et al. 2009

Journal of Food Protection

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The filamentous fungus Aspergillus flavus causes an ear rot on maize and produces a mycotoxin (aflatoxin) in colonized maize kernels. Aflatoxins are carcinogenic to humans and animals upon ingestion. Aflatoxin contamination results in a large loss of profits and marketable yields for farmers each year. Several research groups have worked to pinpoint sources of resistance to A. flavus and the resulting aflatoxin contamination in maize. Some maize genotypes exhibit greater resistance than others. A proteomics approach has recently been used to identify endogenous maize proteins that may be associated with resistance to the fungus. Research has been conducted on cloning, expression, and partial characterization of one such protein, which has a sequence similar to that of cold-regulated proteins. The expressed protein, ZmCORp, exhibited lectin-like hemagglutination activity against fungal conidia and sheep erythrocytes. Quantitative real-time PCR assays revealed that ZmCOR is expressed 50% more in maize kernels from the Mp420 line, a type of maize resistant to A. flavus, compared with the expression level of the gene in the susceptible B73 line. ZmCORp exhibited fungistatic activity when conidia from A. flavus were exposed to the protein at a final concentration of 18 mM. ZmCORp inhibited the germination of conidia by 80%. A 50% decrease in mycelial growth resulted when germinated conidia were incubated with the protein. The partial characterization of ZmCORp suggests that this protein may play an important role in enhancing kernel resistance to A. flavus infection and aflatoxin accumulation.

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Purification and characterization of a galactose-specific lectin from corn (Zea mays) coleoptyle

Cited by 22 publications

References 38 publications

Lectins as Bioactive Plant Proteins: A Potential in Cancer Treatment

Lectins as Bioactive Plant Proteins: A Potential in Cancer Treatment

On the Possible Function of Telfairia occidentalis Agglutinin in the Plant

A Maize Lectin-Like Protein with Antifungal Activity against Aspergillus flavus

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