High impact information on SLC35C1

• Restoration of GDP-fucose import activity in Golgi-enriched vesicles from the patient's fibroblasts verified the GDP-fucose transporter activity of this protein [1].
• We identified two missense mutations in the GDP-fucose transporter cDNA of patient A.C. and of two other people with LAD II [1].
• Complementation cloning identifies CDG-IIc, a new type of congenital disorders of glycosylation, as a GDP-fucose transporter deficiency [1].
• Thus, our results also indicate that the Drosophila genome encodes at least another GDP-fucose transporter that is involved in the O-fucosylation of N [2].
• Leukocyte adhesion deficiency II patients with a dual defect of the GDP-fucose transporter [3].

Biological context of SLC35C1

• Sequencing of the GDP-fucose transporter revealed a novel single nucleotide deletion producing a shift in the open-reading frame and severe truncation of the polypeptide [4].
• In order to test whether this protein serves as a GDP-fucose transporter, we performed complementation studies with fibroblasts from a patient with LADII (leukocyte adhesion deficiency II) which exhibit a strong reduction of fucosylation due to a point mutation in the human GDP-fucose transporter gene [5].
• Differential gene expression of GDP-L-fucose-synthesizing enzymes, GDP-fucose transporter and fucosyltransferase VII [6].
• Our results indicate the simultaneous upregulation of the GDP-L-fucose synthesizing enzymes of the de novo pathway, GDP-fucose transporter and fucosyltransferase VII in inflammation and in tumorigenesis [6].

Anatomical context of SLC35C1

• Insights into leukocyte adhesion deficiency type 2 from a novel mutation in the GDP-fucose transporter gene [4].
• GDP-L-fucose, synthesized in the cytosol, is translocated to the Golgi for fucosylation by a specific GDP-fucose transporter (FUCT1) [6].
• We studied the mRNA expression levels of GDP-L-fucose-synthesizing enzymes, GDP-fucose transporter and fucosyltransferase VII by quantitative real-time PCR in mouse endothelial cells, macrophages and lymphoid tumor cells [6].

Associations of SLC35C1 with chemical compounds

• In the rare LAD-II disease, the fucosylation of selectin ligands is disturbed, caused by mutations in the gene for a GDP-fucose transporter of the Golgi [7].

References