Effect of Lectins on the Activity of Brush Border Membrane-Bound Enzymes of Rat Small Intestine

Erickson, Roger H.; Kim, Johann; Sleisenger, Marvin H.; Kim, Young S.

doi:10.1097/00005176-198512000-00022

Cited by 17 publications

(7 citation statements)

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“…Similar effects were observed for protease inhibitors (PIs) applied to aphids via transgenic plants (Rahbé et al, 2003; Ribeiro et al, 2006; Carrillo et al, 2011). Erickson et al (1985) observed that lectins negatively affect the activity of an aminopeptidase in rats. The identified aminopeptidase inside the aphid gut, which represents 15.6% of total gut proteins, is suggested to be a potential binding site for lectins (Cristofoletti et al, 2006).…”

Section: “Plants In Action”: the Occlusion Of Sieve Tubes Is Protectivementioning

confidence: 99%

How phloem-feeding insects face the challenge of phloem-located defenses

2013

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Due to the high content of nutrient, sieve tubes are a primary target for pests, e.g., most phytophagous hemipteran. To protect the integrity of the sieve tubes as well as their content, plants possess diverse chemical and physical defense mechanisms. The latter mechanisms are important because they can potentially interfere with the food source accession of phloem-feeding insects. Physical defense mechanisms are based on callose as well as on proteins and often plug the sieve tube. Insects that feed from sieve tubes are potentially able to overwhelm these defense mechanisms using their saliva. Gel saliva forms a sheath in the apoplast around the stylet and is suggested to seal the stylet penetration site in the cell plasma membrane. In addition, watery saliva is secreted into penetrated cells including sieve elements; the presence of specific enzymes/effectors in this saliva is thought to interfere with plant defense responses. Here we detail several aspects of plant defense and discuss the interaction of plants and phloem-feeding insects. Recent agro-biotechnological phloem-located aphid control strategies are presented.

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Section: “Plants In Action”: the Occlusion Of Sieve Tubes Is Protectivementioning

confidence: 99%

How phloem-feeding insects face the challenge of phloem-located defenses

2013

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“…However, it has been proposed that lectin may affect the enzyme activities binding to these at places other than their substrate-binding site (Kim et al 1976). As mentioned earlier, the anti-nutritional activity of lectins and lectin-related proteins is mainly mediated by the binding of these molecules to glycan receptors, increasing the number of enzyme active sites, increasing enzyme activity (Erickson et al 1985;You and Chang 1992;Matsushita et al 2002). Such changes were also observed when α-amylase inhibitors were given in larval diets of three species of leaf rollers (Lepidoptera: Tortricidae), resulting in overproduction of α-amylase (Markwick et al 1996).…”

Section: Discussionmentioning

confidence: 83%

Cloning, expression and characterization of arcelin and its impact on digestive enzymes of the stored product insect pest, Callosobruchus maculatus (F.)

Hilda

Bhuvaragavan

Kamatchi

et al. 2021

Preprint

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Key message The defensive role of arcelin from Phaseolus lunatus for its protection against insect pest Callosobruchus maculatus was elucidated. The potent insecticidal property of arcelin and its impact on pest molecular physiology has identified the adaptive strategies. Abstract The pulse beetle Callosobruchus maculatus causes potential damage to legume crops by infesting the seeds and causes a reduction in the content of total protein. Arcelin found in the wild accessions of the common bean, is an insecticidal protein that has the potency to hamper the metabolism of the bruchid beetle. The arcelin gene from the wild accession of Phaseolus lunatus was isolated and the ORF encoding 158 amino acids was cloned in pET-45b (+) vector. The recombinant was transformed into BL21 STAR (DE3) pLysS cells, and the expressed arcelin was purified using Ni-NTA column. The recombinant protein was used in preparing artificial diet and the insecticidal activity was elucidated against the bruchid pest C. maculatus. Adult emergence and seed damage were drastically reduced in the treated groups. The response towards ingested diet by digested enzymes was elucidated through quantitative gene expression. Maximum expression was observed in the aminopeptidase, followed by upregulation of alpha-amylase, glycoside hydrolase family 31 and cathepsin D-like aspartic protease, and downregulation of cathepsin L-like cysteine protease. These results showed the anti-metabolic nature of the recombinant arcelin. The changes in digestive enzymes to counteract the anti-nutritional nature of the protein were the strategies of the insect defense mechanism.

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“…There have been extensive studies on the pathological effects of plant lectins in animals (36–39), but much fewer studies were conducted to examine the cellular mechanism of lectin-mediated toxicology. In the present study, both WGA and SBA induced systemic apoptosis in zebrafish.…”

Section: Discussionmentioning

confidence: 99%

Differential Apoptotic and Mitogenic Effects of Lectins in Zebrafish

et al. 2019

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Plant lectins represent a major group of anti-nutritional factors that can be toxic to human and animals. However, the mechanisms by which lectins regulate cell fates are not well-understood. In the present study, the cellular and molecular impacts of three common lectins, agglutinins from wheat germ [wheat germ agglutinin (WGA)], soybean [soybean agglutinin (SBA)], and peanut [peanut agglutinin (PNA)] were examined in zebrafish embryo and liver cells. WGA and SBA were found to induce cell apoptosis both in vitro and in vivo , while PNA stimulated cell proliferation. WGA and SBA reduced levels of B cell lymphoma-2 (Bcl-2), phosphorylation of Bcl-2-associated death promoter (Bad), cyclin-dependent kinase 4 (Cdk4), and phosphorylation of the retinoblastoma (Rb). WGA and SBA also inhibited the activities of cell survival pathways including protein kinase B (Akt), extracellular signal-regulated protein kinases 1 and 2 (Erk1/2), and target of rapamycin (Tor). Furthermore, WGA and SBA shifted the cellular metabolism characterized by reduced expression of glucose-6-phosphate dehydrogenase ( g6pd ) and increased expression of glutamine synthetase ( glul ) and glutamate dehydrogenase ( glud ). However, PNA showed the opposite effects toward these molecular markers compared to those of WGA and SBA. Therefore, our results revealed some plant lectins (WGA and SBA) were toxic while the other (PNA) was mitogenic. Further characterization of the distinct functions of individual lectins should be valuable for both nutrition and other potential applications.

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Effect of Lectins on the Activity of Brush Border Membrane-Bound Enzymes of Rat Small Intestine

Cited by 17 publications

References 0 publications

How phloem-feeding insects face the challenge of phloem-located defenses

How phloem-feeding insects face the challenge of phloem-located defenses

Cloning, expression and characterization of arcelin and its impact on digestive enzymes of the stored product insect pest, Callosobruchus maculatus (F.)

Differential Apoptotic and Mitogenic Effects of Lectins in Zebrafish

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