IgA: Difference between revisions

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At least two isotypes exist, termed IgA1 and IgA2. IgA2 can further be categorized into 2 allotypes: IgA2 m(1) and IgA2 m(2). While IgA2 is found in most mammalian species, IgA1 is found only in higher apes. An approximately equal ratio of secretory IgA1 (sIgA1) to secretory IgA2 (sIgA2) reside at the mucosal surface, with the exception of the colon, where the majority is sIgA2 <ref name="nineten" />. In the serum, about 90% of the IgA is monomeric IgA1 <ref name ="ten" />.

The receptors for IgA include the Fcα Receptor (FcαRI; CD89) and the polyimmunologlobulin receptor (pIgRI). When binding to FcαRI results in the dimerization, the consequent signaling results in effector functions, including respiratory burst, mucosal surface, phaocytosis, and eosinophil degranulation. Binding to the pIgR results in transoocytosis and IgA secretion <ref name="five" />. Unlike other antibody isotypes, IgA exists in mutiple oligomeric states <ref name="nineseven" />. The most common of which are the monomeric, dimeric, and secretory forms <ref name="ten" />, adding to the complexity of structural functions for IgA. Exploring IgA's structure and protein interactions illuminates the unique and critical function IgA plays in humoral immunity.

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Revision as of 16:51, 23 April 2009 view source Rebecca Martin (talk \| contribs) 123 edits New page: {{STRUCTURE_1iga \| PDB=1iga \| SCENE= }} == Introduction to IgA == The most extensive surface in contact with the external environment is not our skin, but the epithelial lining of ou...		Revision as of 17:22, 23 April 2009 view source Rebecca Martin (talk \| contribs) 123 edits No edit summary Newer edit →
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	At least two isotypes exist, termed IgA1 and IgA2. IgA2 can further be categorized into 2 allotypes: IgA2 m(1) and IgA2 m(2). While IgA2 is found in most mammalian species, IgA1 is found only in higher apes. An approximately equal ratio of secretory IgA1 (sIgA1) to secretory IgA2 (sIgA2) reside at the mucosal surface, with the exception of the colon, where the majority is sIgA2 <ref name="nineten" />. In the serum, about 90% of the IgA is monomeric IgA1 <ref name ="ten" />.		At least two isotypes exist, termed IgA1 and IgA2. IgA2 can further be categorized into 2 allotypes: IgA2 m(1) and IgA2 m(2). While IgA2 is found in most mammalian species, IgA1 is found only in higher apes. An approximately equal ratio of secretory IgA1 (sIgA1) to secretory IgA2 (sIgA2) reside at the mucosal surface, with the exception of the colon, where the majority is sIgA2 <ref name="nineten" />. In the serum, about 90% of the IgA is monomeric IgA1 <ref name ="ten" />.


	The receptors for IgA include the Fcα Receptor (FcαRI; CD89) and the polyimmunologlobulin receptor (pIgRI). When binding to FcαRI results in the dimerization, the consequent signaling results in effector functions, including respiratory burst, mucosal surface, phaocytosis, and eosinophil degranulation. Binding to the pIgR results in transoocytosis and IgA secretion <ref name="five" />. Unlike other antibody isotypes, IgA exists in mutiple oligomeric states <ref name="nineseven" />. The most common of which are the monomeric, dimeric, and secretory forms <ref name="ten" />, adding to the complexity of structural functions for IgA. Exploring IgA's structure and protein interactions illuminates the unique and critical function IgA plays in humoral immunity.		The receptors for IgA include the Fcα Receptor (FcαRI; CD89) and the polyimmunologlobulin receptor (pIgRI). When binding to FcαRI results in the dimerization, the consequent signaling results in effector functions, including respiratory burst, mucosal surface, phaocytosis, and eosinophil degranulation. Binding to the pIgR results in transoocytosis and IgA secretion <ref name="five" />. Unlike other antibody isotypes, IgA exists in mutiple oligomeric states <ref name="nineseven" />. The most common of which are the monomeric, dimeric, and secretory forms <ref name="ten" />, adding to the complexity of structural functions for IgA. Exploring IgA's structure and protein interactions illuminates the unique and critical function IgA plays in humoral immunity.