IgA: Difference between revisions

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== Implications in Science and Medicine ==

~~[[Image:|thumb|Immunofluorescence detecting IgA in IgA glomerulonephritis]]~~

:IgA nephropathy is the most prebvalent cause of chronic glomerulonephritis in the world and is caused by polymeric IgA1 deposited @ kidney glomeruli <ref name="eight"/>. Notably, 90% of serum IgA is IgA1, mostly in the monomeric form.The observation that individuals with IgA myeloma [http://en.wikipedia.org/wiki/Multiple_myeloma] lack nephropathy suggests an abnormality in IgA structure, leading to an abnormal amount of polymerization. Steric hindrance of the fab segments normally limits the amount of polymerization of IgA. Bonner, et al proposes that a disturbance in the hinge region or an absence of fab. Similarly, decreased O-glycosylation might could destabilize the hinge region, allowing IgA to self associate. Likewise, destabilizing this region might make IgA susceptable to cleavage of fab fragments by bacterial proteases, leading to self aggregation and renal pathology. For more information on IgA nephropathy: [http://http://www.unckidneycenter.org/contact.html]. <ref name="sn">Falk, R. "IgA Nephropathy." UNC Kidney Center, from http://www.unckidneycenter.org/kidneyhealthlibrary/iganephropathy.html.</ref>.

:IgA nephropathy is the most prebvalent cause of chronic glomerulonephritis in the world and is caused by polymeric IgA1 deposited @ kidney glomeruli <ref name="eight"/>. Notably, 90% of serum IgA is IgA1, mostly in the monomeric form.The observation that individuals with IgA myeloma [http://en.wikipedia.org/wiki/Multiple_myeloma] lack nephropathy suggests an abnormality in IgA structure, leading to an abnormal amount of polymerization. Steric hindrance of the fab segments normally limits the amount of polymerization of IgA. Bonner, et al proposes that a disturbance in the hinge region or an absence of fab. Similarly, decreased O-glycosylation might could destabilize the hinge region, allowing IgA to self associate. Likewise, destabilizing this region might make IgA susceptable to cleavage of fab fragments by bacterial proteases, leading to self aggregation and renal pathology. For more information on IgA nephropathy: [http://http://www.unckidneycenter.org/contact.html].

:In other areas of science, studying mouse models of pathologies involving IgA1 introduces an added variable since IgA1 is found in higher apes only <ref name="ten"/>. Such complications in the experimental model must be taken into account when interpreting results.

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@@ Line 137: / Line 137: @@
 == Implications in Science and Medicine ==
-[[Image:|thumb|Immunofluorescence detecting IgA in IgA glomerulonephritis]]
+:IgA nephropathy is the most prebvalent cause of chronic glomerulonephritis in the world and is caused by polymeric IgA1 deposited @ kidney glomeruli <ref name="eight"/>. Notably, 90% of serum IgA is IgA1, mostly in the monomeric form.The observation that individuals with IgA myeloma [http://en.wikipedia.org/wiki/Multiple_myeloma] lack nephropathy suggests an abnormality in IgA structure, leading to an abnormal amount of polymerization. Steric hindrance of the fab segments normally limits the amount of polymerization of IgA. Bonner, et al proposes that a disturbance in the hinge region or an absence of fab. Similarly, decreased O-glycosylation might could destabilize the hinge region, allowing IgA to self associate. Likewise, destabilizing this region might make IgA susceptable to cleavage of fab fragments by bacterial proteases, leading to self aggregation and renal pathology. For more information on IgA nephropathy: [http://http://www.unckidneycenter.org/contact.html]. <ref name="sn">Falk, R. "IgA Nephropathy." UNC Kidney Center, from http://www.unckidneycenter.org/kidneyhealthlibrary/iganephropathy.html.</ref>.
-:IgA nephropathy is the most prebvalent cause of chronic glomerulonephritis in the world and is caused by polymeric IgA1 deposited @ kidney glomeruli <ref name="eight"/>. Notably, 90% of serum IgA is IgA1, mostly in the monomeric form.The observation that individuals with IgA myeloma [http://en.wikipedia.org/wiki/Multiple_myeloma] lack nephropathy suggests an abnormality in IgA structure, leading to an abnormal amount of polymerization. Steric hindrance of the fab segments normally limits the amount of polymerization of IgA. Bonner, et al proposes that a disturbance in the hinge region or an absence of fab. Similarly, decreased O-glycosylation might could destabilize the hinge region, allowing IgA to self associate. Likewise, destabilizing this region might make IgA susceptable to cleavage of fab fragments by bacterial proteases, leading to self aggregation and renal pathology. For more information on IgA nephropathy: [http://http://www.unckidneycenter.org/contact.html].
 :In other areas of science, studying mouse models of pathologies involving IgA1 introduces an added variable since IgA1 is found in higher apes only <ref name="ten"/>. Such complications in the experimental model must be taken into account when interpreting results.