Jaime Prilusky at 11:33, 17 March 2013

2013-03-17T11:33:58Z

←Older revision		Revision as of 11:33, 17 March 2013
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	:: TCR: Crystal Structure of the G17E/A52V/S54N/Q72H/E80V/L81S/T87S/G96V variant of the murine T cell receptor V beta 8.2 domain [[2apv]]		:: TCR: Crystal Structure of the G17E/A52V/S54N/Q72H/E80V/L81S/T87S/G96V variant of the murine T cell receptor V beta 8.2 domain [[2apv]]
	* V-type immunoglobulin examples		* V-type immunoglobulin examples
-	:: Crystal Structure of a Ligand-Binding Domain of the Human Polymeric Ig Receptor, pIgR [[~~1XED~~]]	+	:: Crystal Structure of a Ligand-Binding Domain of the Human Polymeric Ig Receptor, pIgR [[1xed]]
	:: Crystal structure of human FcaRI [[10vz]]		:: Crystal structure of human FcaRI [[10vz]]

Rebecca Martin at 11:59, 23 April 2009

2009-04-23T11:59:22Z

(Difference between revisions)

Rebecca Martin at 04:55, 23 April 2009

2009-04-23T04:55:33Z

(Difference between revisions)

Rebecca Martin: New page: == Introduction to IgA == {{STRUCTURE_1iga | PDB=1iga | SCENE= }} The most extensive surface in contact with the external environment is not our skin, but the epithelial lining of our ...

2009-04-23T04:35:30Z

New page: == Introduction to IgA == {{STRUCTURE_1iga | PDB=1iga | SCENE= }} The most extensive surface in contact with the external environment is not our skin, but the epithelial lining of our ...

New page

== Introduction to IgA ==
{{STRUCTURE_1iga | PDB=1iga | SCENE= }}
The most extensive surface in contact with the external environment is not our skin, but the epithelial lining of our gastrointestinal, respiratory, and urogenital tracts <ref name="seven">PMID:17428798</ref>. As a first line of defense in maintainance the integrity our mucosa, the immune system manufatures and secretes dimeric IgA to neutralize pathogenic organisms <ref name="five">PMID:15111057</ref> and exclude the entry of commensals at the mucosal border <ref name="nineseven">PMID:19079336</ref>. In the serum, IgA functions as a second line of defense against pathogens that may breech the epithelial boundary <ref name="five" />. The body produces more IgA than any other antibody isotype <ref name="nineseven"/>. In fact, IgA is the most abundant antibody in the body, further illustrating IgA's critical role in immunity <ref name="ten">PMID:10064707</ref>.

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" />. At least two isotypes exist, termed IgA1 and IgA2. IgA2 can further be categorized into 2 allotypes: IgA2 m(1) and IgA2 m(2). 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 burstmucosal surface, 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" />, phaocytosis, and eosinophil degranulation. Binding to the pIgR results in transoocytosis and IgA secretion <ref name="five" />. Exploring IgA's structure and protein interactions illuminates the unique and critical function IgA plays in humoral immunity.

Rebecca martin/sandbox2 - Revision history

Jaime Prilusky at 11:33, 17 March 2013

Rebecca Martin at 11:59, 23 April 2009

Rebecca Martin at 04:55, 23 April 2009

Rebecca Martin: New page: == Introduction to IgA == {{STRUCTURE_1iga | PDB=1iga | SCENE= }} The most extensive surface in contact with the external environment is not our skin, but the epithelial lining of our ...