How does mannose inhibit con a peroxidase




















Water-soluble perylene bisimide derivative 7 modified with six mannoses was synthesized and its self-assembled properties were studied by UV-Vis and CD spectroscopy , which revealed an interesting self-assembly with a solvent -tuning chiral conformation in H 2 O —DMSO solution.

Wang, H. An, Y. Wang, J. Zhang and X. Li, Org. To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page. If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given. If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given.

Read more about how to correctly acknowledge RSC content. Fetching data from CrossRef. This may take some time to load. The fact that most of the honey-inhibiting activities towards Con A and PA-IIL were removed by dialysis indicates that they are mainly associated with low molecular weight components.

These results are in accord with both the reported honey composition Qiu et al. Each sample of the honeys and RJs are analyzed at least three times. The data in the figure represent their means and s.

The details of the test are described in the Materials and methods, and detailed information on the tagged RJ gps might be found in Kimura et al. Inhibitions of Con A and PA-IIL hemagglutinating activities by the two undialyzed RJ samples were almost equal to those of the honeys and also indicated uniformity of the two RJ preparations that were obtained from different sources Figure 1.

This interpretation is confirmed in the western blot results showing the relatively prosperous interactions of the two lectins with the RJ gps Figure 2. This finding is also in consensus with Kimura's results, indicating the absence of Fuc Kimura et al. Con A interactions with RJ gps was described by Kimura et al. RJ's major highly mannosylated glycoprotein glycan structure, according to Kimura et al. It was already shown by us to display similar very high affinity to highly mannosylated quail egg white gps Lerrer and Gilboa-Garber, The high PA-IIL affinities to them is due to the fucosylation of the HM gps, which do not attract Con A, whereas its affinities to the RJ gps which are at a fold higher concentration than in the honey is owing to their mannosylation that also attracts Con A.

Hence, the honey PA-IIL-blocking effect is mainly attributable to its high Fru content which is removable by dialysis together with low mannosylated gp contribution, while the RJ powerful PA-IIL inhibition is probably mainly associated with highly mannosylated MRJPs retained after dialysis together with lower Fru contribution.

The adhesion-blocking competitive cross-reactivity of the honey, RJ, and HM-active components, hampering the lectin attraction by the animal cell surface glycans, is schematically represented in Figure 4. Attraction of this lectin to the cell surface fucosylated receptors a blocking by honey, RJ and HM saccharides functioning as decoys that mimic them b.

The family of major royal jelly proteins and its evolution. J Mol Evol 49 : — Albert S, Klaudiny J. J Insect Physiol 50 : 51— The efficacy of honey in inhibiting strains of Pseudomonas aeruginosa from infected burns. J Burn Care Rehabil 23 : — The galactophilic lectin, LecA, contributes to biofilm development in Pseudomonas aeruginosa.

Environ Microbiol 8 : — Genome Res 16 : — The antibacterial activity of honey against coagulase-negative staphylococci. J Antimicrob Chemother 56 : — Gilboa-Garber N. Pseudomonas aeruginosa lectins. Methods Enzymol 83 : — Towards anti- Pseudomonas aeruginosa adhesion therapy.

Adv Exp Med Biol : 39— Bacterial lectins: properties, structure, effects, function and applications. Glycosciences: Status and Perspectives. Google Scholar. Biosci Biotechnol Biochem 66 : — Structural features of N-glycans linked to royal jelly glycoproteins: structures of high-mannose type, hybrid type, and biantennary type glycans.

Biosci Biotechnol Biochem 64 : — The primary structures of two types of the Ulex europeus seed lectin. J Biochem Tokyo : — Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature : — Lerrer B, Gilboa-Garber N.

Can J Microbiol 47 : — J Dairy Sci 86 : — Blocking of Pseudomonas aeruginosa lectins by human milk glycans. Can J Microbiol 49 : — The immunostimulatory effect of the recombinant apalbumin 1-major honeybee royal jelly protein-on TNFalpha release. Int Immunopharmacol 6 : — Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lung of cystic fibrosis patients.

Nat Struct Biol 9 : — Molan PC. The evidence supporting the use of honey as a wound dressing. Int J Low Extrem Wounds 5 : 40— Glycobiology 8 : — Bees as Superorganisms — An Evolutionary Reality. Springer Verlag: Berlin, Heidelberg. Book Google Scholar. Human-milk glycans that inhibit pathogen binding protect breast-feeding infants against infectious diarrhea. Evaluation of mannose and sialic acid expression on normal and cancer cells from human lung, liver, and prostate was performed by an electrochemical lectin-based biosensor based on Con A and SNA [ ].

Con A and SNA lectins were used as biorecognition element for mannose and sialic acid, respectively. The proposed biosensor could successfully detect the expression levels of specific sugars. Sialic acid was more evident in cancer cells, and mannose showed a high expression in both normal and cancer cells.

The biosensor could quantify cancer cells and measure the amount of sialic acid expressed on single cell surface, being a promise approach for profiling glycan expression on cell surfaces providing an early diagnosis and treatment. Cramoll lectin biosensors have been reported for revelation of glycoproteins in solutions and serum samples by electrochemical finding.

EIS and CV characterizations revealed distinct changes in the charge transfer resistance and current signals after interactions with the serum samples, being able to recognize serum glycoproteins from dengue serotypes. A label-free Cramoll nanosensor based on assembled carboxylated carbon nanotubes and poly-L-lysine film showed differential serum glycoproteins from prostate cancer and benign prostatic hyperplasia [ 9 ].

DPV responses of nanosensor revealed that Cramoll was able to distinguish between benign and malign prostate tumor, in addition to showing a significant statistical correlation with the degree of staging prostate cancer. Another Cramoll biosensor contained self-assembled Cramoll lectin on the hybrid cysteine-gold nanoparticles-modified gold electrode and was used as a recognition interface for bacterial lipopolysaccharide LPS [ 10 ].

Thus, Cramoll has been able to recognize bacterial LPS and serum glycoproteins, becoming a potential approach for diagnosis of diseases. The ability of lectins to recognize glycans, in addition to the attractive analytical performance of electrochemical biosensors, has been successfully applied for detection of virus and bacteria as well as glycoprofiling of serum glycoproteins and cell surfaces.

Early discovered infections and diseases can help in the diagnosis and appropriate treatment. Lectins from several origins exert cytotoxic effects such as inhibition of proliferation and activation of cell death pathways, on different types of cancer cells. In addition, many anticancer lectins usually possess low cytotoxicity to nontransformed cells.

This fact is probably associated with the distinct expression of glycans on surface of cancer and normal cells, allowing lectins specifically to recognize malignant cells [ 11 , 12 ]. The ability of lectins to inhibit the growth of cancer cells in vitro is well documented in the literature and some examples are listed in Table 1 [ 13 — 21 , 23 — 25 , 27 — 29 , 89 , , — ]. On the other hand, the Bauhinia forficata seed lectin induced necrosis and secondary necrosis in MCF-7 cells, with caspase 9 inhibition [ 21 ].

Sources of lectins with in vitro inhibitory effect on growth of different cancer cells. A mannose-binding lectin from Clematis montana induced apoptosis in L cells murine fibro sarcoma with activation of caspases. Authors proposed that there is a correlation between carbohydrate-binding ability and anticancer effect of this lectin since the cytotoxic activity decreased with the assay performed in presence of mannose [ 23 ].

In the same sense, Carvalho et al. Mechanisms of apoptosis or necrosis induction by lectins have been studied. Wu et al. On the other hand, authors mentioned upregulation of microRNAa-3p, which mediates ROS-p53 44 pathway linked to apoptosis and autophagy.

Bothrops leucurus venom lectin triggered necrosis in BF10 murine melanoma cells, with increase in cytosolic calcium concentration and mitochondrial superoxide generation; this lectin activated the opening of mitochondrial permeability transition pore [ 16 ]. Yang et al. Lectins may also affect the adhesion ability of cancer cells. As mentioned above, lectins can reach the cytosol and promote several alterations in cell physiology. Authors also described that this lectin caused aggregation of Golgi complex, protein accumulation in the endoplasmic reticulum, mitochondrial malformation, and membrane depolarization [ 29 ].

The several reports on the potential of lectins for cancer treatment stimulated studies at in vivo conditions using different models. Cratylia mollis seed lectin encapsulated into liposomes was evaluated for in vivo antitumor activity against sarcoma Pisum sativum and Momordica charantia seed lectins showed in vitro and in vivo inhibitory effects on Ehrlich carcinoma ascitic tumor in mice. The P. The proapoptotic gene Bax was expressed intensively in cells treated with P. The seed lectin from Glycine max caused Finally, the anticancer potential of lectins also includes antimetastatic properties.

Leaf lectin from Viscum album coloratum showed a preventive effect against lung metastasis caused by BBL6 and M3. This lectin also inhibited liver and spleen metastasis of LY-ML25 cells when administered one day after tumor inoculation [ ].

Lectins from diverse sources with distinct carbohydrate recognition events have important roles for many biotechnological applications and disease therapies.

In vitro and in vivo uses showed that lectins have protective effects against virus and microorganisms; they are potent modulators of immune response, mitosis, proliferation, healing, drug delivery therapies, and cancer regression.

Altered glycans on cells or tissue surfaces and serum samples can be located using lectin-based techniques, such as histochemistry and biosensors, detecting diseases and infection agents. Besides, the effects described for the same or different lectins on biological systems could unravel new interpretations or insights to the field. National Center for Biotechnology Information , U. Evid Based Complement Alternat Med. Published online Mar 7. Author information Article notes Copyright and License information Disclaimer.

This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. This article has been cited by other articles in PMC.

Abstract Lectins are proteins extensively used in biomedical applications with property to recognize carbohydrates through carbohydrate-binding sites, which identify glycans attached to cell surfaces, glycoconjugates, or free sugars, detecting abnormal cells and biomarkers related to diseases.

Introduction Considering the diverse diseases and infectious agents that affect the human species and their consequences, the biotechnological field has searched biorecognition molecules from natural or recombinant sources with diagnostic and therapeutic potential. Lectin Induced Mechanisms of Immunological and Inflammatory Responses Immunological and inflammatory responses play a role in the protection of an organism against an invasive agent and transformed cells.

Open in a separate window. Figure 1. Antifungal and Antiparasitic Activities of Lectins Recent studies have demonstrated the potential of lectins from different origin and carbohydrate specificities as antifungal and antiparasitic agents.

Lectins for Healing Applications Many researchers have reported healing effect induced by lectins. Figure 2. Lectins for Drug Delivery The therapies using chemical agents have some barriers, mainly regarding the need of increasing dosages and action of metabolism, which reduce the effectiveness of treatment.

Figure 3. Figure 4. Lectins as Histochemical Markers The glycan moieties covering cell surfaces are involved in many physiological and pathological processes related to cell. Figure 5. Lectin-Based Biosensors for Disease Detection Many known biomarkers established to specific physio- and pathological processes are glycoprotein and glycan detectable in biological fluids and cell surface [ ]. Figure 6. Lectins as Anticancer Agents Lectins from several origins exert cytotoxic effects such as inhibition of proliferation and activation of cell death pathways, on different types of cancer cells.

Table 1 Sources of lectins with in vitro inhibitory effect on growth of different cancer cells. Conclusions Lectins from diverse sources with distinct carbohydrate recognition events have important roles for many biotechnological applications and disease therapies. Competing Interests The authors have declared that no competing interests exist. References 1. Sharon N. History of lectins: from hemagglutinins to biological recognition molecules. Lectins: carbohydrate-specific reagents and biological recognition molecules.

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