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Glycosylation also plays a role in cell-to-cell adhesion (a mechanism employed by cells of the immune system) via sugar-binding proteins called lectins, which recognize specific carbohydrate moieties. [2] Glycosylation is an important parameter in the optimization of many glycoprotein-based drugs such as monoclonal antibodies. [6]
Glycation (non-enzymatic glycosylation) is the covalent attachment of a sugar to a protein, lipid or nucleic acid molecule. [1] Typical sugars that participate in glycation are glucose , fructose , and their derivatives.
AGEs have a range of pathological effects, such as: [22] [23] Increased vascular permeability. Increased arterial stiffness; Inhibition of vascular dilation by interfering with nitric oxide. Oxidizing LDL. Binding cells—including macrophage, endothelial, and mesangial—to induce the secretion of a variety of cytokines. Enhanced oxidative stress.
One study found that inhibition of OGA with streptozotocin followed by glucosamine treatment resulted in O-GlcNAc accumulation and apoptosis in β cells; [160] a subsequent study showed that a galactose-based analogue of streptozotocin was unable to inhibit OGA but still resulted in apoptosis, suggesting that the apoptotic effects of ...
A congenital disorder of glycosylation (previously called carbohydrate-deficient glycoprotein syndrome) is one of several rare inborn errors of metabolism in which glycosylation of a variety of tissue proteins and/or lipids is deficient or defective. Congenital disorders of glycosylation are sometimes known as CDG syndromes.
The heavy glycosylation of these proteins can mask peptide epitopes, making designing antibodies targeted to certain proteins sections all the more difficult. Therefore, some have turned to translational glycobiology to develop antibodies using semi-synthetic and fully synthetic oligosaccharides as antigens.
I-cell disease is an autosomal recessive disorder caused by a deficiency of GlcNAc phosphotransferase, which phosphorylates mannose residues to mannose-6-phosphate on N-linked glycoproteins in the Golgi apparatus within cells.
In addition, human GCPII has ten sites of potential glycosylation, and many of these sites (including some far from the catalytic domain) affect the ability of GCPII to hydrolyze NAAG. [6] The human FOLH1 gene is positioned at the 11p11.12 locus of chromosome 11. The gene is 4,110 base pairs in length and composed of 22 exons.