Management of the human mucosal defensive barrier: evidence for glycan legislation
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Georgios Patsos
Abstract
The human gastrointestinal barrier comprises several layers which enable protection against the external environment. The mucosal epithelium, lamina propria, glycocalyx and secreted mucus each make a contribution to barrier protection. Glycocalyx and secreted mucins constitute a glycosylated environment which interacts with the enteric microflora. Turnover of the mucus layer and the creation of binding ligands for bacteria are significant factors in gut homeostasis. The gut microbiota is composed of many bacterial species, but improved technology has allowed detection of populations present at different stages of development and in disease. Interaction of the microflora with the gut occurs from birth onwards and enables maturation of gut angiogenesis and glycosylation as demonstrated in mouse models. Glycan legislation regulates the ongoing interaction between the microflora and the host mucosa. This accounts for host glycosylation mechanisms providing a dynamic response to fluctuations in the gut microflora. Evidence for glycan legislation is based on a surgical model where intact mucosa can be compared with and without contact to the faecal microflora. In addition, mucosal cell glycosylation is assessed using inhibitors of O-glycan synthesis. These inhibitors lead to growth arrest in cultured colorectal cancer cell lines through the induction of apoptosis and downregulation of proliferation.
©2009 by Walter de Gruyter Berlin New York
Articles in the same Issue
- Guest Editorial
- Highlight: Perspectives in glycobiology
- Cell biology and glycosylation: protein targeting by O- and N-linked glycosylation
- Glycosylation- and phosphorylation-dependent intracellular transport of lysosomal hydrolases
- Glycosylation pattern of brush border-associated glycoproteins in enterocyte-like cells: involvement of complex-type N-glycans in apical trafficking
- Impact of glycosylation and detergent-resistant membranes on the function of intestinal sucrase-isomaltase
- MUC1 traverses apical recycling endosomes along the biosynthetic pathway in polarized MDCK cells
- Cell biology and glycosylation: carbohydrate-mediated recognition and signaling in cell proliferation and differentiation
- From structural to functional glycomics: core substitutions as molecular switches for shape and lectin affinity of N-glycans
- Brain development needs sugar: the role of polysialic acid in controlling NCAM functions
- Beyond glycosylation: sialic acid precursors act as signaling molecules and are involved in cellular control of differentiation of PC12 cells
- Glycosylation and disease
- Management of the human mucosal defensive barrier: evidence for glycan legislation
- Regulation and pathophysiological implications of UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE) as the key enzyme of sialic acid biosynthesis
- GD3 synthase overexpression enhances proliferation and migration of MDA-MB-231 breast cancer cells
- Tumor-associated MUC1 glycopeptide epitopes are not subject to self-tolerance and improve responses to MUC1 peptide epitopes in MUC1 transgenic mice
- Protein-specific glycosylation and its control
- Protein-specific glycosylation: signal patches and cis-controlling peptidic elements
- O-glycosylation pattern of CD24 from mouse brain
- Advancements in analytical techniques
- Carbohydrate microarrays: key developments in glycobiology
- On-line nano-HPLC/ESI QTOF MS monitoring of α2–3 and α2–6 sialylation in granulocyte glycosphingolipidome
Articles in the same Issue
- Guest Editorial
- Highlight: Perspectives in glycobiology
- Cell biology and glycosylation: protein targeting by O- and N-linked glycosylation
- Glycosylation- and phosphorylation-dependent intracellular transport of lysosomal hydrolases
- Glycosylation pattern of brush border-associated glycoproteins in enterocyte-like cells: involvement of complex-type N-glycans in apical trafficking
- Impact of glycosylation and detergent-resistant membranes on the function of intestinal sucrase-isomaltase
- MUC1 traverses apical recycling endosomes along the biosynthetic pathway in polarized MDCK cells
- Cell biology and glycosylation: carbohydrate-mediated recognition and signaling in cell proliferation and differentiation
- From structural to functional glycomics: core substitutions as molecular switches for shape and lectin affinity of N-glycans
- Brain development needs sugar: the role of polysialic acid in controlling NCAM functions
- Beyond glycosylation: sialic acid precursors act as signaling molecules and are involved in cellular control of differentiation of PC12 cells
- Glycosylation and disease
- Management of the human mucosal defensive barrier: evidence for glycan legislation
- Regulation and pathophysiological implications of UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE) as the key enzyme of sialic acid biosynthesis
- GD3 synthase overexpression enhances proliferation and migration of MDA-MB-231 breast cancer cells
- Tumor-associated MUC1 glycopeptide epitopes are not subject to self-tolerance and improve responses to MUC1 peptide epitopes in MUC1 transgenic mice
- Protein-specific glycosylation and its control
- Protein-specific glycosylation: signal patches and cis-controlling peptidic elements
- O-glycosylation pattern of CD24 from mouse brain
- Advancements in analytical techniques
- Carbohydrate microarrays: key developments in glycobiology
- On-line nano-HPLC/ESI QTOF MS monitoring of α2–3 and α2–6 sialylation in granulocyte glycosphingolipidome
