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Aberrant glycosylation of IgA appears to lead to polymerisation of the IgA molecules in tissues, especially the glomerular mesangium. [5] A similar mechanism has been claimed to underlie Henoch–Schönlein purpura, a vasculitis that mainly affects children and can feature renal involvement that is almost indistinguishable from IgA nephritis.
IgA exists in two isotypes, IgA1 and IgA2.They are both heavily glycosylated proteins. [9] While IgA1 predominates in serum (~80%), IgA2 percentages are higher in secretions than in serum (~35% in secretions); [10] the ratio of IgA1 and IgA2 secreting cells varies in the different lymphoid tissues of the human body: [11]
In IgG, IgA and IgD antibody isotypes, the Fc region is composed of two identical protein fragments, derived from the second and third constant domains of the antibody's two heavy chains; IgM and IgE Fc regions contain three heavy chain constant domains (C H domains 2–4) in each polypeptide chain.
The changes are indistinguishable from those observed in IgA nephropathy. [12] Microphotograph of a histological section of human skin prepared for direct immunofluorescence using an anti-IgA antibody, the skin is a biopsy of a patient with Henoch–Schönlein purpura. IgA deposits are found in the walls of small superficial capillaries (yellow ...
It has 8 cysteine residues, 6 of which are involved in intramolecular disulfide bonds while the remaining two function to bind the Fc tailpiece regions of IgA or IgM antibodies, the α chain and μ chain respectively. An N-linked carbohydrate resulting from N-glycosylation is also essential in the protein's incorporation to antibody polymers. [12]
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]
The water-accessible surface area of an IgG antibody. Immunoglobulin G (IgG) is a type of antibody.Representing approximately 75% of serum antibodies in humans, IgG is the most common type of antibody found in blood circulation. [1]
The different types of lipid-linked oligosaccharide (LLO) precursor produced in different organisms.. N-linked glycosylation is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom (the amide nitrogen of an asparagine (Asn) residue of a protein), in a process called N-glycosylation, studied in ...
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