The Origins, Specificity, and Potential Biological Relevance of Human Anti-IgG Hinge Autoantibodies

Human anti-IgG hinge (HAH) autoantibodies constitute a class of immunoglobulins that recognize cryptic epitopes in the hinge region of antibodies exposed after proteolytic cleavage, but do not bind to the intact IgG counterpart. Detailed molecular characterizations of HAH autoantibodies suggest that...

Full description

Saved in:
Bibliographic Details
Main Authors: Randall J. Brezski, David M. Knight, Robert E. Jordan
Format: Article
Language:English
Published: Wiley 2011-01-01
Series:The Scientific World Journal
Online Access:http://dx.doi.org/10.1100/tsw.2011.107
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1832562909650092032
author Randall J. Brezski
David M. Knight
Robert E. Jordan
author_facet Randall J. Brezski
David M. Knight
Robert E. Jordan
author_sort Randall J. Brezski
collection DOAJ
description Human anti-IgG hinge (HAH) autoantibodies constitute a class of immunoglobulins that recognize cryptic epitopes in the hinge region of antibodies exposed after proteolytic cleavage, but do not bind to the intact IgG counterpart. Detailed molecular characterizations of HAH autoantibodies suggest that they are, in some cases, distinct from natural autoantibodies that arise independent of antigenic challenge. Multiple studies have attempted to define the specificity of HAH autoantibodies, which were originally detected as binding to fragments possessing C-terminal amino acid residues exposed in either the upper or lower hinge regions of IgGs. Numerous investigators have provided information on the isotype profiles of the HAH autoantibodies, as well as correlations among protease cleavage patterns and HAH autoantibody reactivity. Several biological functions have been attributed to HAH autoantibodies, ranging from house-cleaning functions to an immunosuppressive role to restoring function to cleaved IgGs. In this review, we discuss both the historic and current literature regarding HAH autoantibodies in terms of their origins, specificity, and proposed biological relevance.
format Article
id doaj-art-d38bfd3b0c8d41999ae9a0d0ce75aa52
institution Kabale University
issn 1537-744X
language English
publishDate 2011-01-01
publisher Wiley
record_format Article
series The Scientific World Journal
spelling doaj-art-d38bfd3b0c8d41999ae9a0d0ce75aa522025-02-03T01:21:29ZengWileyThe Scientific World Journal1537-744X2011-01-01111153116710.1100/tsw.2011.107The Origins, Specificity, and Potential Biological Relevance of Human Anti-IgG Hinge AutoantibodiesRandall J. Brezski0David M. Knight1Robert E. Jordan2Biologics Research, Centocor R&D Inc., Radnor, PA, USABiologics Research, Centocor R&D Inc., Radnor, PA, USABiologics Research, Centocor R&D Inc., Radnor, PA, USAHuman anti-IgG hinge (HAH) autoantibodies constitute a class of immunoglobulins that recognize cryptic epitopes in the hinge region of antibodies exposed after proteolytic cleavage, but do not bind to the intact IgG counterpart. Detailed molecular characterizations of HAH autoantibodies suggest that they are, in some cases, distinct from natural autoantibodies that arise independent of antigenic challenge. Multiple studies have attempted to define the specificity of HAH autoantibodies, which were originally detected as binding to fragments possessing C-terminal amino acid residues exposed in either the upper or lower hinge regions of IgGs. Numerous investigators have provided information on the isotype profiles of the HAH autoantibodies, as well as correlations among protease cleavage patterns and HAH autoantibody reactivity. Several biological functions have been attributed to HAH autoantibodies, ranging from house-cleaning functions to an immunosuppressive role to restoring function to cleaved IgGs. In this review, we discuss both the historic and current literature regarding HAH autoantibodies in terms of their origins, specificity, and proposed biological relevance.http://dx.doi.org/10.1100/tsw.2011.107
spellingShingle Randall J. Brezski
David M. Knight
Robert E. Jordan
The Origins, Specificity, and Potential Biological Relevance of Human Anti-IgG Hinge Autoantibodies
The Scientific World Journal
title The Origins, Specificity, and Potential Biological Relevance of Human Anti-IgG Hinge Autoantibodies
title_full The Origins, Specificity, and Potential Biological Relevance of Human Anti-IgG Hinge Autoantibodies
title_fullStr The Origins, Specificity, and Potential Biological Relevance of Human Anti-IgG Hinge Autoantibodies
title_full_unstemmed The Origins, Specificity, and Potential Biological Relevance of Human Anti-IgG Hinge Autoantibodies
title_short The Origins, Specificity, and Potential Biological Relevance of Human Anti-IgG Hinge Autoantibodies
title_sort origins specificity and potential biological relevance of human anti igg hinge autoantibodies
url http://dx.doi.org/10.1100/tsw.2011.107
work_keys_str_mv AT randalljbrezski theoriginsspecificityandpotentialbiologicalrelevanceofhumanantiigghingeautoantibodies
AT davidmknight theoriginsspecificityandpotentialbiologicalrelevanceofhumanantiigghingeautoantibodies
AT robertejordan theoriginsspecificityandpotentialbiologicalrelevanceofhumanantiigghingeautoantibodies
AT randalljbrezski originsspecificityandpotentialbiologicalrelevanceofhumanantiigghingeautoantibodies
AT davidmknight originsspecificityandpotentialbiologicalrelevanceofhumanantiigghingeautoantibodies
AT robertejordan originsspecificityandpotentialbiologicalrelevanceofhumanantiigghingeautoantibodies