α-C-Mannosyltryptophan is not recognized by conventional mannose-binding lectins

Nishikawa, Toshio; Kajii, Shigeo; Sato, Chihiro; Yasukawa, Zenta; Kitajima, Ken; Isobe, Mitsuaki

doi:10.1016/j.bmc.2004.02.009

Cited by 11 publications

(7 citation statements)

References 33 publications

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“…Although this efficacy lags behind that of chloroquine, the widely applied antimalarial, the low cytotoxicity (>100 μM) and the novelty of the structures among antimalarial medications make these compounds very promising. 129 Binding affinity of α-C-mannosyltryptophan (C-Man-Trp, compound 339 in Scheme 56) to mannose specific lectins such as Con A isolated from plant and MBL-C purified from mouse serum was investigated; 473 however, these lectins were not able to make contacts with C-Man-Trp.…”

Section: Miscellaneous Biological Studiesmentioning

confidence: 99%

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C-Glycopyranosyl Arenes and Hetarenes: Synthetic Methods and Bioactivity Focused on Antidiabetic Potential

et al. 2017

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This Review summarizes close to 500 primary publications and surveys published since 2000 about the syntheses and diverse bioactivities of C-glycopyranosyl (het)arenes. A classification of the preparative routes to these synthetic targets according to methodologies and compound categories is provided. Several of these compounds, regardless of their natural or synthetic origin, display antidiabetic properties due to enzyme inhibition (glycogen phosphorylase, protein tyrosine phosphatase 1B) or by inhibiting renal sodium-dependent glucose cotransporter 2 (SGLT2). The latter class of synthetic inhibitors, very recently approved as antihyperglycemic drugs, opens new perspectives in the pharmacological treatment of type 2 diabetes. Various compounds with the C-glycopyranosyl (het)arene motif were subjected to biological studies displaying among others antioxidant, antiviral, antibiotic, antiadhesive, cytotoxic, and glycoenzyme inhibitory effects.

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Section: Miscellaneous Biological Studiesmentioning

confidence: 99%

“…Binding affinity of α- C -mannosyltryptophan ( C -Man-Trp, compound 339 in Scheme ) to mannose specific lectins such as Con A isolated from plant and MBL-C purified from mouse serum was investigated; however, these lectins were not able to make contacts with C -Man-Trp.…”

Section: Biological Effects Of C-glycosyl (Het)arenesmentioning

confidence: 99%

C-Glycopyranosyl Arenes and Hetarenes: Synthetic Methods and Bioactivity Focused on Antidiabetic Potential

et al. 2017

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“…C-mannosylation at tryptophan, more recently discovered, has been found not to be recognized by mannose-binding lectins [188]. Lectin affinity columns do appear to bind phosphoglycosylated protein [11].…”

Section: Boronate Affinitymentioning

confidence: 98%

Development of Monolithic Column Materials for the Separation and Analysis of Glycans

Alla

Stine

2015

Chromatography

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Monolithic column materials offer great advantages as chromatographic media in bioseparations and as solid-supports in biocatalysis. These single-piece porous materials have an interconnected ligament structure that limits the void volume inside the column, thus increasing the efficiency without sacrificing the permeability. The preparation of monolithic materials is easy, reproducible and has available a wide range of chemistries to utilize. Complex, heterogeneous and isobaric glycan structures require preparation methods that may include glycan release, separation and enrichment prior to a comprehensive and site-specific glycosylation analysis. Monolithic column materials aid that demand, as shown by the results reported by the research works presented in this review. These works include selective capture of glycans and glycoproteins via their interactions with lectins, boronic acids, hydrophobic, and hydrophilic/polar functional groups on monolith surfaces. It also includes immobilization of enzymes trypsin and PNGase F on monoliths to digest and deglycosylate glycoproteins and glycopeptides, respectively. The use of monolithic capillary columns for glycan separations through nano-liquid chromatography (nano-LC) and capillary electrochromatography (CEC) and coupling these columns to MS instruments to create multidimensional systems show the potential in the development of miniaturized, high-throughput and automated systems of glycan separation and analysis.

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“…The C-mannosylated peptides showed no significant interaction with LPS or Tolllike receptor 4, a receptor for LPS, and the specific target for C-mannosylated peptides was not clear in the cells. Interestingly, Nishikawa et al reported that C-Man-W is not recognized by conventional mannose-binding lectins, such as concanavalin A and mannose binding lectin-C (68). Thus it would be interesting to clarify the molecules which Recently, proteins bound to C-mannosylated TSRderived peptides were searched for using chemically synthesized C-mannosylated peptides (14).…”

Section: D-4 Cellular Signaling Functions Of the W-x-x-w Motif With C-mannosementioning

confidence: 99%

Protein C-Mannosylation and Its Prospective Functions in the Cell

Ihara

Inai

Ikezaki

2011

TIGG

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Protein C-Mannosylation is unique in that an α-mannose attaches directly to the indole C2 carbon atom of a Trp residue through a C-C bond. C-Mannosylation usually occurs at the first tryptophan in the consensus amino acid sequence Trp-x-x-Trp (W-x-x-W) through an enzymatic reaction with a specific mannosyltransferase, which has yet to be identified. Most substrates for C-mannosylation are part of either the thrombospondin type-1 repeat (TSR) superfamily or cytokine receptor family, suggesting a functional role for C-mannosylation in specific substrates. Site-directed mutagenesis in the W-x-x-W motif has revealed C-mannosylation to be important in the folding or targeting of substrate proteins, such as mucins and ADAMTS-like 1, in the cell. Furthermore, using chemically synthesized C-mannosylated TSR-derived peptides, Hsc70 was identified as a protein bound to C-mannosylated peptides, and the interaction enhanced the TNF-α-producing signaling by Hsc70 in macrophage-like cells. These recent findings suggest that the C-mannosylation of specific target proteins plays pivotal functional roles in the cell.©2011 FCCA (Forum: Carbohydrates Coming of Age)RNase, an acceptor substrate for C-mannosylation, in cultured cells transfected with an expression vector for several chimeric RNase genes. The precursor donor of the mannose in C-mannosylation was revealed to be dolichyl-P-mannose, in that the uptake of [ 3 H]-mannose into hybrid RNase 2.4 was apparently suppressed in gene-transfected CHO Lec15 cells (9), in which dolichyl-P-mannose synthesis is impaired. A defect of C-mannosylation was also observed in Lec35 cells (10), in which dolichyl-P-mannose utilization was impaired. In addition, the activity was estimated in vitro by measuring the uptake of [ 3 H]-mannose from dolichyl-P-[ 3 H]-mannose into a peptide containing the W-x-x-W motif (i.e., N-Acetyl-KPPQFAWAQWFE-NH 2 ). In the assay, no uptake of [ 3 H]mannose into the substrate was detected when GDP-[ 3 H]mannose was used as a precursor. Taken together, these results support that dolichyl-P-mannose is a direct donor for C-mannosylation.The availability of dolichyl-P-mannose is thought important to be different types of glycosylation in the endoplasmic reticulum (ER), including N-glycosylation, the GPI-anchor 's formation, O-mannosylation, and C-mannosylation (11). Recently, a unique clinical phenotype of a mild muscular dystrophy with dilated cardiomyopathy was reported to correlate with a mild defect of dolichyl-P-mannose due to DPM3 gene mutations (12). In the disorder, O-mannosylation of α-dystroglycan is severely abrogated, and the most dominant factor determining clinical outcome. On the other hand, a mild influence was observed on C-mannosylation, N-glycosylation, and formation of the GPI-anchor in the patients. This study suggests that C-mannosylation reaction is not so sensitive to the availability of dolychil-P-mannose in the cell.C -M a n n o s y l t r a n s f e r a s e a c t i v i t y i s p r e s e n t i n Caenorhabditis elegans, amphibians, birds, and mam...

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α-C-Mannosyltryptophan is not recognized by conventional mannose-binding lectins

Cited by 11 publications

References 33 publications

C-Glycopyranosyl Arenes and Hetarenes: Synthetic Methods and Bioactivity Focused on Antidiabetic Potential

C-Glycopyranosyl Arenes and Hetarenes: Synthetic Methods and Bioactivity Focused on Antidiabetic Potential

Development of Monolithic Column Materials for the Separation and Analysis of Glycans

Protein C-Mannosylation and Its Prospective Functions in the Cell

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