FUOM

Last update 08 May 2025

Basic Info

Synonyms

C10orf125, FLJ26016, FucM

+ [3]

Introduction

Involved in the interconversion between alpha- and beta-L-fucoses. L-Fucose (6-deoxy-L-galactose) exists as alpha-L-fucose (29.5%) and beta-L-fucose (70.5%), the beta-form is metabolized through the salvage pathway. GDP-L-fucose formed either by the de novo or salvage pathways is transported into the endoplasmic reticulum, where it serves as a substrate for N- and O-glycosylations by fucosyltransferases. Fucosylated structures expressed on cell surfaces or secreted in biological fluids are believed to play a critical role in cell-cell adhesion and recognition processes.

100 Clinical Results associated with FUOM

100 Translational Medicine associated with FUOM

0 Patents (Medical) associated with FUOM

Literatures (Medical) associated with FUOM

01 Mar 2025·Cancer Research Communications

Identification of Causal Plasma Proteins in Hepatocellular Carcinoma via Two-Sample Mendelian Randomization and Integrative Transcriptomic‒Proteomic Analysis

Article

Author: Tang, Weihao ; Ma, Xiaoke

AbstractHepatocellular carcinoma (HCC) poses a serious threat to human health. Identifying diagnostic and therapeutic targets from plasma proteins is essential for early HCC detection and treatment. Large-scale plasma proteomics data and Mendelian randomization (MR) offer opportunities for this type of research. Proteomic data from protein quantitative trait loci were obtained from the UK Biobank Pharma Proteomics Project. Two-sample MR was used to evaluate the causal association between plasma protein levels and HCC. Sensitivity, directionality, and colocalization analyses were conducted to validate the causal associations identified by MR. Robustness was further tested through colocalization analysis. The single-cell dataset GSE166635 was used to assess the expression of genes corresponding to proteins identified via MR. Potential drugs targeting these proteins were evaluated using the DSigDB/DrugBank databases and molecular docking. Seven proteins with potential causal associations with HCC were identified: ASS1, B2M, FUOM, GABARAPL1, ST8SIA1, STOML2, and KRT8. Among these genes, ASS1, KRT8, and STOML2 presented the strongest effects in the colocalization analyses. In a single-cell liver cancer dataset, ASS1, KRT8, and STOML2 were expressed mainly in hepatic progenitor cells and malignant cells, with KRT8 predominantly found in hepatic progenitor cells and playing a role in the oncogenesis of malignant liver cells. Potential drugs targeting ASS1 include arginine, aspartic acid, and citrulline; for KRT8, ambroxol, diltiazem, and amikacin; and for STOML2, chlortetracycline, chlorzoxazone, and dirithromycin. This study identified several novel causal plasma proteins, providing new insights into the early diagnosis and treatment of HCC.Significance:In this study, we identified several causal proteins in HCC using UK Biobank Pharma Proteomics Project proteomic data via two-sample MR. We performed colocalization and sensitivity analyses, utilized single-cell RNA sequencing data for validation, and discovered potential drugs through molecular docking.

01 May 2024·Carbohydrate Polymers

Fucoidan from Ascophyllum nodosum and Undaria pinnatifida attenuate SARS-CoV-2 infection in vitro and in vivo by suppressing ACE2 and alleviating inflammation

Article

Author: Wang, Xin ; Wang, Wei-Wei ; Xu, Ling-Dong ; Shi, Fang-Shu ; Xie, Yv-Hao ; Yang, Yong-Le ; Li, Xiao-Qiong ; Zhu, Li-Ying ; Huang, Yao-Wei ; Shen, Pei-Li ; Li, Jin-Jun

The global healthcare challenge posed by COVID-19 necessitates the continuous exploration for novel antiviral agents. Fucoidans have demonstrated antiviral activity. However, the underlying structure-activity mechanism responsible for the inhibitory activity of fucoidans from Ascophyllum nodosum (FUCA) and Undaria pinnatifida (FUCU) against SARS-CoV-2 remains unclear. FUCA was characterized as a homopolymer with a backbone structure of repeating (1 → 3) and (1 → 4) linked α-l-fucopyranose residues, whereas FUCU was a heteropolysaccharide composed of Fuc1-3Gal1-6 repeats. Furthermore, FUCA demonstrated significantly higher anti-SARS-CoV-2 activity than FUCU (EC50: 48.66 vs 69.52 μg/mL), suggesting the degree of branching rather than sulfate content affected the antiviral activity. Additionally, FUCA exhibited a dose-dependent inhibitory effect on ACE2, surpassing the inhibitory activity of FUCU. In vitro, both FUCA and FUCU treatments downregulated the expression of pro-inflammatory cytokines (IL-6, IFN-α, IFN-γ, and TNF-α) and anti-inflammatory cytokines (IL-10 and IFN-β) induced by viral infection. In hamsters, FUCA demonstrated greater effectiveness in attenuating lung and gastrointestinal injury and reducing ACE2 expression, compared to FUCU. Analysis of the 16S rRNA gene sequencing revealed that only FUCU partially alleviated the gut microbiota dysbiosis caused by SARS-CoV-2. Consequently, our study provides a scientific basis for considering fucoidans as poteintial prophylactic food components against SARS-CoV-2.

01 Jul 2020·Biochemical and Biophysical Research CommunicationsQ3 · BIOLOGY

Functional and structural characterization of a novel L-fucose mutarotase involved in non-phosphorylative pathway of L-fucose metabolism

Q3 · BIOLOGY

Article

Author: Nishiwaki, Hisashi ; Watanabe, Yasunori ; Watanabe, Seiya ; Fukui, Yasutaka

Mutarotases catalyze the α-β anomeric conversion of monosaccharide, and play a key role in utilizing sugar as enzymes involved in sugar metabolism have specificity for the α- or β-anomer. In spite of the sequential similarity to l-rhamnose mutarotase protein superfamily (COG3254: RhaM), the ACAV_RS08160 gene in Acidovorax avenae ATCC 19860 (AaFucM) is located in a gene cluster related to non-phosphorylative l-fucose and l-galactose metabolism, and transcriptionally induced by these carbon sources; therefore, the physiological role remains unclear. Here, we report that AaFucM possesses mutarotation activity only toward l-fucose by saturation difference (SD) NMR experiments. Moreover, we determined the crystal structures of AaFucM in the apo form and in the l-fucose-bound form at resolutions of 2.21 and 1.75 Å, respectively. The overall structural folding was clearly similar to the RhaM members, differed from the known l-fucose mutarotase (COG4154: FucU), strongly indicating their convergent evolution. The structure-based mutational analyses suggest that Tyr18 is important for catalytic action, and that Gln87 and Trp99 are involved in the l-fucose-specific recognition.

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