This action might not be possible to undo. Are you sure you want to continue?
marrow B cells. In IgA2, the heavy and light chains are not linked with disulfide but with noncovalent bonds. IgA2 is made by B cells located in the mucosae and has been found to secrete into colostrum, maternal milk, tears and saliva. In secretory IgA, the form of IgA that is found in secretions, polymers of 2-4 IgA monomers are linked by two additional chains. One of these is the J chain (joining chain), which is a polypeptide of molecular mass 15kD, rich with cysteine and structurally completely different from other immunoglobulin chains. This chain is formed in the IgA -secreting cells.The oligomeric forms of IgA in the external (mucosal) secretions also contain a polypeptide of a much larger molecular mass (70 kD) called the secretory component that is produced by epithelial cells. This molecule originates from the poly-Ig receptor (130 kD) that is responsible for the uptake and transcellular transport of oligomeric (but not monomeric) IgA across the epithelial cells and into secretions such as tears, saliva, sweat, and gut fluid. Found highly in secretions of the eye. The high prevalence of IgA in mucosal areas is a result of a cooperation between plasma cells that produce polymeric IgA (pIgA), and mucosal epithelial cells that express an immunoglobulin receptor called the polymeric Ig receptor (pIgR). pIgA is released from the nearby activated plasma cells and binds to pIgR. This results in transportation of IgA across mucosal epithelial cells and its cleavage from pIgR for release into external secretions.In the blood, IgA interacts with an Fc receptor called Fc RI (or CD89), which is expressed on immune effector cells, to initiate inflammatory reactions. Ligation of Fc RI by IgA containing immune complexes causes antibody-dependent cell-mediated cytotoxicity (ADCC), degranulation of eosinophils and basophils, phagocytosis by monocytes, macrophages, neutrophils and eosinophils, and triggering of respiratory burst activity by polymorphonuclear leukocytes. Polymeric IgA (mainly the secretory dimer) is produced by plasma cells in the lamina propria adjacent to mucosal surfaces. It binds to the polymeric immunoglobulin receptor on the basolateral surface of epithelial cells and is taken up into the cell via endocytosis. The receptor-IgA complex passes through the cellular compartments before being secreted on the luminal surface of the epithelial cells, still attached to the receptor. Proteolysis of the receptor occurs and the dimeric IgA molecule, along with a portion of the receptor known as the secretory component, are free to diffuse throughout the lumen. In the gut, it can bind to the mucus layer on top of the epithelial cells to form a barrier capable of neutralizing threats before they reach the cells. Decreased or absent IgA, termed selective IgA deficiency, can be a clinically significant immunodeficiency.Neisseria gonorrh ae (which causes gonorrhea) releases a protease which destroys IgA.IgA nephropathy is caused by IgA deposits in the kidneys. It is not yet known why IgA deposits occur in this chron disease. Some ic theories suggest it is an abnormality of immune system that results in these deposits
IgD- IgD starts to be expressed when the B-cell exits the bone marrow to populate peripheral lymphoid tissues. When a B-cell reaches its mature state, it co-expresses both IgM and IgD. No bilogical effector function has been found. IgE- IgE is a monomeric antibody with 4 Ig-like domains (CH1->CH4).  It plays an important role in allergy, and is especially associated with type 1 hypersensitivity. IgE elicits an immune response by binding to Fc receptors found on the surface of mast cells and basophils, and are also found on eosinophils, monocytes, macrophages and platelets in humans. Fc has two types:Fc RI, the high-affinity IgE receptor Fc RII, also known as CD23, is the low-affinity IgE receptor .IgE can upregulate the expression of both Fc receptors. Fc RI is expressed only on mast cells and/or basophils in both mice and humans. Aggregation of antigens and binding of IgE to the Fc RI on mast cells causes degranulation and the release of mediators from the cells, while basophils cross-linked with IgE release type 2 cytokines like interleukin-4 (IL-4) and interleukin-13 (IL-13) and other inflammatory mediators. The low affinity receptor (Fc RII) is always expressed on B cells, but its expression can be induced on the surfaces of macrophages, eosinophils, platelets and some T cells by IL-4. Atopic individuals can have up to 10 times the normal level of IgE in their blood. IgE that can specifically recognise an "allergen". has a unique long-lived interaction with its high affinity receptor, Fc RI, so that basophils and mast cells, capable of mediating
leukotrienes and certain interleukins. bacteria.3 and 4 cross the placenta and play and important role in protecting the developing fetus. Colostrum contains a high percentage of IgG. however.inflammatory reactions. . which cause many of the symptoms we associate with allergy. IgM possesses high avidity. and fungi. 4 has an intermediate affinity for Fc receptors and 2 has an extremely low affinity. IgG . especially in bovine colostrum. residual IgG absorbed through the placenta provides the neonate with humoral immunity before its own immune system develops. IgG3 and IgG4. 3 is the most effective complement activator followed by 1. complement activation (classical pathway).2 and 4 is not able to complement at all. IgG2.two heavy chains and two light chains. Each IgG has two antigen binding sites. become "primed". IgG antibodies are predominantly involved in the secondary immune response (the main antibody involved in primary response is IgM). opsonization for phagocytosis and neutralization of their toxins. Typically. 1 and 3 bind with high affinity to Fc receptors on phagocytic cells and thus mediate opsonization. It also plays an important role in Antibody-dependent cell-mediated cytotoxicity(ADCC) and Intracellular antibody-mediated proteolysis. a pentameric IgM has 10 binding sites. and protects the body against them by agglutination and immobilization.IgG can bind to many kinds of pathogens. 1. IgG is the only isotype that can pass through the human placenta. Because each monomer has two antigen binding sites. and is particularly effective at complement activation. Its pentameric valency makes it effcient with epitopes such as rbc virus. IgG is also associated with Type II and Type III Hypersensitivity. its polymeric nature. such as airway constriction in asthma. local inflammation in eczema. but which can lead to a potentially fatal drop in blood pressure as in anaphylaxis.composed of four peptide chains -. ready to release chemicals like histamine. increased mucus secretion in allergic rhinitis and increased vascular permeability. Plays an important role as a secretory immunoglobulin. The presence of specific IgG generally corresponds to maturation of the antibody response. Its the first immunoglobulin produced in a primary response to an antigen. for example viruses. thereby providing protection to the fetus in utero. IgG subclasses consists of IgG1. IgM cannot bind 10 antigens at the same time because the large size of most antigens hinders binding to nearby sites. ostensibly to allow other immune cells to gain access to tissues. IgM ± Accounts for 5% to 10% of the total serum immunoglobulin. Along with IgA secreted in the breast milk. in which it binds to TRIM21 (the receptor with greatest affinity to IgG in humans) in order to direct marked virions to the proteasome in the cytosol.