Ask about this productRelated genes to: SLC35C1 Blocking Peptide
- Gene:
- SLC35C1 NIH gene
- Name:
- solute carrier family 35 member C1
- Previous symbol:
- -
- Synonyms:
- FUCT1, FLJ11320
- Chromosome:
- 11p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2003-10-08
- Date modifiied:
- 2019-04-23
Related products to: SLC35C1 Blocking Peptide
Related articles to: SLC35C1 Blocking Peptide
- Anxiety disorders are highly heritable, but their underlying genetic mechanisms remain poorly understood. This study aimed to identify and functionally characterize genes whose expression is causally linked to anxiety disorder risk by integrating the parallel single-tissue genetic data. - Source: PubMed
Publication date: 2026/04/21
Wang LeshengXu ZhipengLuo GaomengWei WeiGuo MeimeiYuan YunheShi BeiGuan HaowenLiu ShaLi Xiang - Fucosylation disorders are rare types of congenital disorders of glycosylation (CDG), the most common being SLC35C1-CDG, which is classically described as a leukocyte adhesion deficiency (hence the previous name of "leukocyte adhesion deficiency type II") with dysmorphic features, short stature, and moderate-to-severe developmental and intellectual disabilities. In more recent years, several cases have been described of individuals with bi-allelic SLC35C1 variants and biochemical proof of hypofucosylation who had short stature, dysmorphic features, and intellectual disability, but no hematological abnormalities. In this article, we report a patient with growth faltering, neuroirritability, nystagmus, developmental delays, microcephaly, dysmorphic features, and hypogammaglobulinemia G. Biochemical investigations including serum N-glycan profiling, fucosylation-focused whole serum glycoprotein profiling, and serum lectin blots, all of which showed significant global hypofucosylation. Exome sequencing revealed a single likely pathogenic variant, SLC35C1 (NM_018389.4):c.503_505delTCT, p.(Phe168del), which was inherited from an unaffected mother. Whole genome sequencing with manual review of raw data did not reveal any second pathogenic variants; SLC35C1 mRNA sequencing was negative for changes in the second allele or allelic imbalance. The patient was started on L-fucose supplementation, with subsequent improvements in weight and head circumference, normalization of IgG levels, and remarkable developmental catch-up. Biochemically, there was an increase in abundance of previously decreased fucosylated glycan species in serum, especially FucGlcNAcMan (a glycan that is known to be enriched in neutrophils). In summary, we present here further evidence for the role of L-fucose supplementation in treating hypofucosylation disorders and suggest that IgG and fucosylated glycan species may be useful as biomarkers in this scenario, although further research is needed to validate them as such. It is likely that the early introduction of L-fucose in this patient may have led to the excellent developmental outcomes observed. - Source: PubMed
Publication date: 2026/01/08
Starosta Rodrigo THe MiaoGracie SaraKierstein JanellThiel ChristianHimmelreich NastassjaLiu YupengZhang WenyueEdmondson Andrew CMeeks NaomiLarson AustinVan Hove Johan L KKochhar Aaina - Glycosylation occurs mainly in the Golgi apparatus, whereas the synthesis of nucleotide sugars occurs in the cytoplasm or nucleus. GDP-fucose in mammalian cells could be produced via de novo and salvage pathways in the cytoplasm; the first one is responsible for about 90% of GDP-fucose in the total pool of this nucleotide sugar in the cell. SLC35C1 (C1) is the primary transporter of GDP-fucose to the Golgi apparatus. In the absence of this transporter, it was proposed that nucleotide sugar could still reach the Golgi apparatus via a SLC35C2, the homologue of SLC35C1. However, simultaneous inactivation of the two transporters did not influence GDP-fucose transport across the Golgi apparatus membranes after external fucose supplementation. In this study, we combined the inactivation of SLC35C1 and enzymes of the GDP-fucose biosynthesis pathways (FCSK, GMDS and TSTA3) to study the impact of double inactivation on the production of nucleotide sugar and fucosylated glycans. We found that a lack of SLC35C1 changed the level of enzymes of both de novo and salvage pathways. Upon fucose supplementation, stimulation of the salvage pathway was remarkably high in the absence of the TSTA3 protein, and the concentration of GDP-fucose increased to millimolar values. In this work, we discovered that simultaneous deficiency of the SLC35C1 protein and TSTA3 enzyme increased GDP-fucose production via the salvage pathway to an even higher level. Finally, we found that nucleotide sugar still accessed the Golgi apparatus and had differential effects on N- and O-glycans. - Source: PubMed
Publication date: 2025/05/27
Skurska EdytaOlczak Mariusz - Non-small-cell lung cancer (NSCLC) remains a global health challenge, driving morbidity and mortality. The emerging field of radiogenomics utilizes statistical methods to correlate radiographic tumor features with genomic characteristics from biopsy samples. Radiomic techniques automate the precise extraction of imaging features from tumor regions in radiographic scans, which are subjected to machine learning (ML) to predict genomic attributes. - Source: PubMed
Sukhadia Shrey SSadee ChristophGevaert OlivierNagaraj Shivashankar H - Congenital disorders of glycosylation (CDG) include a group of diseases characterized by defects of N-glycan fucosylation. The analytical molecule of choice for the diagnosis of CDG affecting N-glycosylation is serum transferrin: approximately 10% of the glycans attached to transferrin are fucosylated via an α1,6 linkage at the innermost -acetylglucosamine residue, termed "core fucosylation." Isoelectric focusing (IEF) of transferrin is often used for diagnosis, but IEF is ineffective in detecting abnormal fucosylation. Here, we present mass spectrometry (MS) methods for detecting fucosylation disorders. First, the level of core fucosylation of the glycan attached to Asn630 of transferrin can be measured by the signal intensity ratio of tryptic peptide ions containing fucosylated and nonfucosylated biantennary oligosaccharides. The core fucosylation level at this glycosylation site in the 0- to 32-year-old group ( = 68) was 7.9 ± 1.7 (%, mean ± SD), and nearly null for SLC35C1-CDG caused by defects in the GDP-fucose transporter. More simply, fucosylation levels can be measured by quadrupole time-of-flight (QTOF) MS of intact transferrin. The fucosylation levels of intact transferrin measured by MS with a Q-mass analyzer, which is currently used as an instrumental standard for newborn screening for inborn errors of metabolism and has a lower resolution than the QTOF analyzer, correlated well with the values obtained by glycopeptide analysis. These methods, namely the analysis of glycopeptides or intact transferrin by Q MS, can also be used on dried blood spots and are expected to help facilitate the diagnosis of CDG affecting N-glycan fucosylation. - Source: PubMed
Publication date: 2024/11/26
Wada YoshinaoKadoya Machiko