A5089456462- Glycosylation and Glycoproteins Research
- Galectins and Cancer Biology
- Carbohydrate Chemistry and Synthesis
- HIV Research and Treatment
- Cell Adhesion Molecules Research
- Helicobacter pylori-related gastroenterology studies
- Reproductive tract infections research
- Pediatric health and respiratory diseases
- Milk Quality and Mastitis in Dairy Cows
- Digestive system and related health
- Infant Nutrition and Health
University of Gothenburg
2019-2020
Institute for Biomedicine
2020
Swedish Academy
2020
Boehringer Ingelheim (United States)
2017
The HIV-AIDS pandemic is prevalent in sub-Saharan Africa. Breastfeeding a risk factor, with transmission from mother to child being as high 40%.To determine the antiviral activity of crude breast milk and its purified mucins MUC1 MUC4 against HIV-1 patients who were HIV positive compared those not.Twenty-one human samples taken both groups. Breast by density-gradient ultracentrifugation caesium chloride analyzed SDS-PAGE, Western blotting amino acid content. inhibition virus mucin was...
The synovial fluid glycoprotein lubricin (also known as proteoglycan 4) is a mucin-type O-linked glycosylated biological lubricant implicated to be involved in osteoarthritis (OA) development. Lubricin's ability reduce friction related its glycosylation consisting of sialylated and unsialylated Tn-antigens core 1 2 structures. glycans on have also been suggested crosslinking stabilization the lubricating superficial layer cartilage by mediating interaction between galectin-3. However, with...
The β4-<italic>N</italic>-acetylgalactosaminyltransferase 3 (B4GALNT3) transfers GalNAc in a β1,4-linkage to GlcNAc forming the LacdiNAc (LDN) determinant on oligosaccharides.
ABSTRACT Synovial fluid lubricin (proteoglycan 4) is a mucin-type O -linked glycosylated (60% of the mass) biological lubricant involved in osteoarthritis (OA) development. Lubricin has been reported to be cross-linked by synovial galectin-3 on lubricating articular surface. Here, we confirm that binding depended core-2 glycans, where surface plasmon resonance recombinant (rhPRG4) devoid structures lacked capacity galectin-3. Both levels and interactions with were found decreased late-stage...