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20-September-2008 09:55:54 - M Redirected from IgM IgM Immunoglobulin M antibody molecule consisting of 5 base units.1: Base unit. 2: Heavy chains.3: Light chains.4: J chain.5: Intermolecular disulfide bonds. IgM Immunoglobulin M antibody molecule consisting of 5 base units. 1: Base unit. 2: Heavy chains. 3: Light chains. 4: J chain. 5: Intermolecular disulfide bonds. IgM scheme. Heavy chains are blue; light chains are yellow. IgM scheme. Heavy chains are blue; light chains are yellow. Immunoglobulin M, or IgM for short, is a basic antibody that is present on B cells. It is the primary antibody against A and B antigens on red blood cells. IgM is by far the physically largest antibody in the human circulatory system. Contents 1 Structure and function 2 Expression 3 Clinical significance 4 Other points 5 See also 6 References 7 External links Structure and function IgM forms polymers where multiple immunoglobulins are covalently linked together with disulfide bonds, mostly as a pentamer but also as a hexamer. IgM has a molecular mass of approximately 900 kD in its pentamer form. Because each monomer has two antigen binding sites, a pentameric IgM has 10 binding sites. Typically, however, IgM cannot bind 10 antigens at the same time because the large size of most antigens hinders binding to nearby sites. The J chain is found in pentameric IgM but not in the hexameric form, perhaps due to space constraints in the hexameric complex. Pentameric IgM can also be made in the absence of J chain. At present, it is still uncertain what fraction of normal pentamer contains J chain, and to this extent it is also uncertain whether a J chain-containing pentamer contains one or more than one J chain. 1 Because IgM is a large molecule, it cannot diffuse well, and is found in the interstitium only in very low quantities. IgM is primarily found in serum; however, because of the J chain, it is also important as a secretory immunoglobulin. Due to its polymeric nature, IgM possesses high avidity, and is particularly effective at complement activation. Expression In germline cells, the gene segment encoding the μ constant region of the heavy chain is positioned first among other constant region gene segments. For this reason, IgM is the first immunoglobulin expressed by mature B cells. It is also the first immunoglobulin expressed in the fetus around 20 weeks and also phylogenetically the earliest antibody to develop.2 Clinical significance IgM antibodies appear early in the course of an infection and usually reappear, to a less extent, after further exposure. IgM antibodies do not pass across the human placenta. These two biological properties of IgM make it useful in the diagnosis of infectious diseases. Demonstrating IgM antibodies in a patient's serum indicates recent infection, or in a neonate's serum indicates intrauterine infection e.g. congenital rubella. Other points IgM in normal serum is often found to bind to specific antigens, even in the absence of prior immunization. For this reason IgM has sometimes been called a natural antibody. This phenomenon is probably due to the high avidity of IgM that allow it to bind detectably even to weakly cross-reacting antigens that are naturally occurring in nature. For example the IgM antibodies that bind to the red blood cell A and B antigens might be formed in early life as a result of exposure to A- and B-like substances that are present on bacteria or perhaps also on plant materials. IgM antibodies are mainly responsible for the clumping agglutination of red blood cells if the recipient of a blood transfusion receives blood that is not compatible with their blood type. See also Antibody IgA, IgD, IgE, IgG References ^ Erik J. Wiersma, Cathy Collins, Shafie Fazel, and Marc J. Shulman Structural and Functional Analysis of J Chain-Deficient IgM J. Immunol., Jun 1998; 160: 5979 - 5989. ^ Review of Medical Physiology by William Francis Ganong External links MeSH Immunoglobulin+M v d e Immune system / Immunology Systems Adaptive immune system vs. Innate immune system · Humoral immune system vs. Cellular immune system · Complement system Anaphylatoxins · Intrinsic immune system Antibodies and antigens Antibody Monoclonal antibodies, Polyclonal antibodies, Autoantibody · Allotype · Isotype · Idiotype · Antigen Superantigen · Polyclonal B cell response Immune cells/White blood cells Lymphoid: T cell · B cell · NK cell Myeloid: Mast cell · Basophil · Eosinophil · Macrophage Phagocytes: Neutrophil · Macrophage/Reticuloendothelial system Professional APCs: Dendritic cell · Macrophage · B cell Immunity vs. tolerance Immunity · Autoimmunity · Allergy · Tolerance Central · Immunodeficiency Immunogenetics Somatic hypermutation · VDJ recombination · Immunoglobulin class switching · MHC/HLA Substances Cytokines · Opsonin · Cytolysin Other Inflammation · Epitope Linear epitope and Conformational epitope · Hapten · Cross-reactivity · Diagnostic immunology · Immune complex v d e Immune system proteins Antibodies Light chain, Heavy chain, IgA, IgD, IgE, IgG, IgM Other MAC complex - Nanobodies - Perforin Retrieved from http://en..org/wiki/Immunoglobulin_M Categories: Immune system | Immunology | Glycoproteins | Antibodies Views Article Discussion this page History Personal tools Log in / create account Navigation Main page Contents Featured content Current events Random article Search Go Search Interaction Community portal Recent changes Contact Donate to Help Toolbox What links here Related changes Upload file Special pages Printable version Permanent link Cite this page Languages العربية Dansk Deutsch Español Français Italiano 日本語 Polski Português Suomi This page was last modified on 15 August 2008, at 01:03

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