A Novel Core Fucose-specific Lectin from the Mushroom Pholiota squarrosa

Kobayashi, Yuka; Tateno, Hiroaki; Dohra, Hideo; Moriwaki, Kazuo; Miyoshi, Eiji; Hirabayashi, Jun; Kawagishi, Hirokazu

doi:10.1074/jbc.m111.327692

Cited by 110 publications

(105 citation statements)

References 51 publications

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“…PhoSL is a reliable reagent to detect specifically core α1,6-fucosylated asparagine-linked oligosaccharides [23]. NSCLCs with both high and low expression of FUT8 and GMD were used for PhoSL histochemistry to determine whether FUT8 and GMD expression resulted in the synthesis of core α1,6-fucosylated asparagine-linked oligosaccharides (online suppl.…”

Section: Resultsmentioning

confidence: 99%

“…High expression of GMD was more prevalent in cases with high expression of FUT8, indicating that concordant expression of FUT8 and GMD frequently occurred in NSCLCs (table 3). When we stained tumor sections using PhoSL to detect specifically core α1,6-fucosylated asparagine-linked oligosaccharides [23], PhoSL-positive cells were observed more frequently in tumors with high expression of both FUT8 and GMD than in those with low expression of both FUT8 and GMD (online suppl. fig.…”

Section: Discussionmentioning

confidence: 99%

“…The expression of core α1,6-fucosylated asparagine-linked oligosaccharides (glycans) was analyzed by Pholiota squarrosa lectin (PhoSL) histochemistry [23]. After deparaffinization, the labeled biotin-streptavidin method was used on 4-μm-thick sections of formalin-fixed paraffin-embedded tissues, which were consecutively made for immunohistochemistry for FUT8 and GMD as well as PhoSL histochemistry.…”

Section: Methodsmentioning

confidence: 99%

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Expression of Fucosyltransferase 8 Is Associated with an Unfavorable Clinical Outcome in Non-Small Cell Lung Cancers

Honma¹,

Kinoshita²,

Miyoshi

et al. 2015

Oncology

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Objecitive: Fucosyltransferase 8 (FUT8), the only enzyme responsible for the core α1,6-fucosylation of asparagine-linked oligosaccharides of glycoproteins, is a vital enzyme in cancer development and progression. We examined FUT8 expression in non-small cell lung cancers (NSCLCs) to analyze its clinical significance. We also examined the expression of guanosine diphosphate-mannose-4,6-dehydratase (GMD), which is imperative for the synthesis of fucosylated oligosaccharides. Methods: Using immunohistochemistry, we evaluated the expression of FUT8 and GMD in relation to patient survival and prognosis in potentially curatively resected NSCLCs. Results: High expression of FUT8 was found in 67 of 129 NSCLCs (51.9%) and was significantly found in non-squamous cell carcinomas (p = 0.008). High expression of FUT8 was associated with poor survival (p = 0.03) and was also a significant and independent unfavorable prognostic factor in patients with potentially curatively resected NSCLCs (p = 0.047). High expression of GMD was significantly associated with high FUT8 expression (p = 0.04). Conclusions: High expression of FUT8 is associated with an unfavorable clinical outcome in patients with potentially curatively resected NSCLCs, suggesting that FUT8 can be a prognostic factor. The analysis of FUT8 expression and its core fucosylated products may provide new insights for the therapeutic targets of NSCLCs.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Expression of Fucosyltransferase 8 Is Associated with an Unfavorable Clinical Outcome in Non-Small Cell Lung Cancers

Honma¹,

Kinoshita²,

Miyoshi

et al. 2015

Oncology

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“…The glycan array data did show that the lectins from Pisum sativum and Lens culinaris may be specific for 6’-linked fucose (Table S6), as reported earlier 35 , but a closer examination of the glycan array data suggested a requirement for certain mannose linkages in each cases, rendering them not exclusive binders to 6’-linked fucose. We did not have glycan array data for the lectin from Pholiota squarrosa , described by Kobayashi and coworkers as specific for α1–6 fucose 36 .…”

Section: Resultsmentioning

confidence: 99%

Upregulation of Glycans Containing 3′ Fucose in a Subset of Pancreatic Cancers Uncovered Using Fusion-Tagged Lectins

et al. 2015

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The fucose post-translational modification is frequently increased in pancreatic cancer, thus forming the basis for promising biomarkers, but a subset of pancreatic cancer patients does not elevate the known fucose-containing biomarkers. We hypothesized that such patients elevate glycan motifs with fucose in linkages and contexts different from the known fucose-containing biomarkers. We used a database of glycan array data to identify the lectins CCL2 to detect glycan motifs with fucose in a 3’ linkage; CGL2 for motifs with fucose in a 2’ linkage; and RSL for fucose in all linkages. We used several practical methods to test the lectins and determine the optimal mode of detection, and we then tested whether the lectins detected glycans in pancreatic cancer patients who did not elevate the sialyl-Lewis A glycan, which is upregulated in ~75% of pancreatic adenocarcinomas. Patients who did not upregulate sialyl-Lewis A, which contains fucose in a 4’ linkage, tended to upregulate fucose in a 3’ linkage, as detected by CCL2, but they did not upregulate total fucose or fucose in a 2’ linkage. CCL2 binding was high in cancerous epithelia from pancreatic tumors, including areas negative for sialyl-Lewis A and a related motif containing 3’ fucose, sialyl-Lewis X. Thus glycans containing 3’ fucose may complement sialyl-Lewis A to contribute to improved detection of pancreatic cancer. Furthermore, the use of panels of recombinant lectins may uncover details about glycosylation that could be important for characterizing and detecting cancer.

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“…Xenopus galectin-VIIa [81] Human, chicken, nematode, sponge, fungal galectrins [36] Human galectin-9 [82] Nematode galectin LEC-1 and N-and C-CRDs [83] C-type PF00059 C-type α/β-fold Atlantic salmon serum [84] calcium-dependent Sea cucumber lectin CEL-IV [85] DC-SIGN, DC-SIGNR, and LSECtin [86] Langerin to sulfated and mannsylated glycans [87] MGL1, MGL2, and their mutants [88] Atlantic salmon C-type lectin receptor C (SCLRC) [89] Acorn barnacle Megabalanus rosa, Balanus rostatus [90] R-type PF00652 β-trefoil Mutants of earthworm lectin EW29Ch [91] ricin B chain-related RCA120/RCA-I [58] Phytopathogenic Sclerotinia sclerotiorum [92] Jacalin-related PF01419 β-prism I Human ZG16 p [93] Mannose-binding type Jacalin-related lectins [37] Jacalin [94] Castanea crenata agglutinin (CCA) [95] Cycas revoluta leaf lectin (CRLL) [95] GNA-related monocot-type PF04152 β-prism II Two-domain GNA-related lectins [96] Sea urchin egg PF02140 α/β-fold with two long Shishamo smelt Osmerus (Spirinchus) lanceolatus [97] Fungal fucose-specific PF07938 6-bladed β-propeller Mushroom Pholiota squarrosa [104] Aspergillus oryzae [105] AAL-like Fungal fruit body lectin PF07367 α/β-sandwich Agaricus bisporus agglutinin (ABA) [106] Others Mussel, Mytilus galloprovincialis [107] orphan or family Mushroom Hygrophorus russula [108] unidentified Eggs of Japanese sea hare Aplysia kurodai [109] Feather star Oxycomanthus japonicas [110] Coronate moon turban Turbo (Lunella)…”

Section: Erythrina Species [58]mentioning

confidence: 99%

The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography

et al. 2015

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Lectins are a large group of carbohydrate-binding proteins, having been shown to comprise at least 48 protein scaffolds or protein family entries. They occur ubiquitously in living organisms-from humans to microorganisms, including viruses-and while their functions are yet to be fully elucidated, their main underlying actions are thought to mediate cell-cell and cell-glycoconjugate interactions, which play important roles in an extensive range of biological processes. The basic feature of each lectin's function resides in its specific sugar-binding properties. In this regard, it is beneficial for researchers to have access to fundamental information about the detailed oligosaccharide specificities of diverse lectins. In this review, the authors describe a publicly available lectin database named "Lectin frontier DataBase (LfDB)", which undertakes the continuous publication and updating of comprehensive data for lectin-standard oligosaccharide interactions in terms of dissociation constants (Kd's). For Kd determination, an advanced system of frontal affinity chromatography (FAC) is used, with which quantitative datasets of interactions between immobilized lectins and >100 fluorescently labeled standard glycans have been generated. OPEN ACCESS

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A Novel Core Fucose-specific Lectin from the Mushroom Pholiota squarrosa

Cited by 110 publications

References 51 publications

Expression of Fucosyltransferase 8 Is Associated with an Unfavorable Clinical Outcome in Non-Small Cell Lung Cancers

Expression of Fucosyltransferase 8 Is Associated with an Unfavorable Clinical Outcome in Non-Small Cell Lung Cancers

Upregulation of Glycans Containing 3′ Fucose in a Subset of Pancreatic Cancers Uncovered Using Fusion-Tagged Lectins

The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography

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