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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] IgA1 is the predominant IgA subclass found in serum. Most lymphoid tissues have a predominance of IgA1-producing ...
IgA shows the same typical structure of other antibody classes, with two heavy chains and two light chains, and four distinct domains: one variable region, and three variable regions. As a major class of immunoglobulin in body secretions, IgA plays a role in defending against infection , as well as preventing the access of foreign antigens to ...
Secretory components wrap around two IgA units joined by a J chain protein fragment, resulting in a >--< configuration, with each of the two antigen binding regions of the two constituent y-shaped antibodies exposed. One identified function of secretory components is to protect IgA antibodies from degradation by the gastric acids and enzymes of ...
a variable region that differs between different B cells, but is the same for all immunoglobulins produced by the same B cell or B cell clone. The variable domain of any heavy chain is composed of a single immunoglobulin domain. These domains are about 110 amino acids long. [6]
The J chain regulates the multimerization of IgM and IgA in mammals. When expressed in cells, it favors the formation of a pentameric IgM and an IgA dimer. IgM pentamers are most commonly found with a single J chain, but some studies have seen as many as 4 J chains associated to a single IgM pentamer.
‘In IgA deficiency, B cells express IgA; however, they are of immature phenotype with the coexpression of IgM and IgD, and they cannot fully develop into IgA-secreting plasma cells’. [7] There is an inherited inability to produce immunoglobulin A (IgA), a part of the body's defenses against infection at the body's surfaces (mainly the ...
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The antigen receptor of T cells is the T-cell receptor (TCR), which is composed of two chains, either the TCR-alpha and -beta chains, or the TCR-delta and gamma chains. All TCR chains contain two Ig domains in the extracellular portion; one IgV domain at the N-terminus and one IgC1 domain adjacent to the cell membrane. Antigen presenting molecules