Shen et al. exploit glycobiology to dampen transforming growth factor-β (TGF-β) signaling and ameliorate renal fibrosis after ureteral obstruction. Core fucosylation of N-linked oligosaccharides in TGF-β receptors is required for receptor function. Adenoviruses expressing Fut8-fucosyl transferase-shRNA inhibited receptor fucosylation, decreased tubule TGF-β signaling, and reduced fibrosis. Fut8-shRNA interferes with core fucosylation of other receptors also. Regardless, this first attempt to capitalize on a new aspect of TGF-β receptor function provides a basis for further research.
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http://dx.doi.org/10.1038/ki.2013.95 | DOI Listing |
J Biol Chem
January 2025
Division of Regulatory Glycobiology, Graduate School of Pharmaceutical Sciences, Tohoku Medical and Pharmaceutical University; Institute of Molecular Biomembrane and Glycobiology, Tohoku Medical and Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai, Miyagi 981-8558, Japan. Electronic address:
Core fucosylation is one of the most essential modifications of the N-glycans, catalyzed by α1,6-fucosyltransferase (Fut8), which transfers fucose from guanosine 5'-diphosphate (GDP)-fucose to the innermost N-acetylglucosamine residue of N-glycans in an α1-6 linkage. Our previous studies demonstrated that lipopolysaccharide (LPS) can induce a more robust neuroinflammatory response in Fut8 homozygous knockout (KO) (Fut8) and heterozygous KO (Fut8) mice contrasted to the wild-type (Fut8) mice. Exogenous administration of L-fucose suppressed LPS-induced neuroinflammation.
View Article and Find Full Text PDFJ Virol
January 2025
Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas, USA.
Unlabelled: Human noroviruses (HuNoVs) are the leading cause of acute gastroenteritis worldwide. Currently, there are no targeted antivirals for the treatment of HuNoV infection. Histo-blood group antigens (HBGAs) on the intestinal epithelium are cellular attachment factors for HuNoVs; molecules that block the binding of HuNoVs to HBGAs thus have the potential to be developed as antivirals.
View Article and Find Full Text PDFViruses
December 2024
Department of Infectious Diseases, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, 413 46 Gothenburg, Sweden.
The tick-borne encephalitis virus is a pathogen endemic to northern Europe and Asia, transmitted through bites from infected ticks. It is a member of the family and possesses a positive-sense, single-stranded RNA genome encoding a polypeptide that is processed into seven non-structural and three structural proteins, including the envelope (E) protein. The glycosylation of the E protein, involving a single N-linked glycan at position N154, plays a critical role in viral infectivity and pathogenesis.
View Article and Find Full Text PDFFood Chem
December 2024
Chinese Academy of Inspection and Quarantine, Beijing 100176, People's Republic of China. Electronic address:
Glycoproteins, which are involved in numerous biological functions, are among the most critical functional ingredients in an edible bird's nest (EBN). To gain a comprehensive understanding of the glycoprotein species within EBN, a label-free, site-specific glycoproteomic approach was used to analyze their N-glycoproteins, N-glycopeptides, and N-glycans systematically. A total of 127 N-glycoproteins were identified in EBN, of which 72 were found in house-EBN and 63 in cave-EBN, yielding 4195 and 5649 glycopeptides, respectively.
View Article and Find Full Text PDFGlycobiology
January 2025
Laboratório de Tecido Conjuntivo, Hospital Universitário Clementino Fraga Filho and Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-913, Brazil.
Fucosylated chondroitin sulfate (FCS) is a unique polysaccharide, first described nearly four decades ago, and found exclusively in sea cucumbers. It is a component of the extracellular matrix, possibly associated with peculiar properties of the invertebrate tissue. The carbohydrate features a chondroitin sulfate core with branches of sulfated α-Fuc linked to position 3 of the β-GlcA.
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