Binding and Activation of Plasminogen on Immobilized Immunoglobulin G

Harpel, Peter C.; Sullivan, Robert; Chang, Tsun-San

doi:10.1016/s0021-9258(17)31305-4

Cited by 35 publications

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

Some antiphospholipid antibodies recognize conformational epitopes shared by β₂‐glycoprotein I and the homologous catalytic domains of several serine proteases

Lin

Chen

Yang

et al. 2007

Arthritis & Rheumatism

View full text Add to dashboard Cite

Objective. To test the hypothesis that some antiphospholipid antibodies (aPL) in patients with the antiphospholipid syndrome (APS) recognize a conformational epitope shared by ␤ 2 -glycoprotein I (␤ 2 GPI; the major autoantigen for the antiphospholipid antibodies) and the homologous catalytic domains of several serine proteases (such as thrombin, activated protein C [APC], and plasmin) involved in hemostasis.Methods. We generated 4 new IgG monoclonal aPL (2 screened against ␤ 2 GPI, 1 against thrombin, and 1 against protein C) from 2 APS patients. The monoclonal antibodies (mAb) were analyzed for binding to ␤ 2 GPI, thrombin, APC, and plasmin, as well as for anticardiolipin antibody (aCL) activity. To demonstrate a shared epitope between ␤ 2 GPI and a serine protease, 1 mAb was studied by cross-inhibition analysis.Results. Both of the IgG anti-␤ 2 GPI mAb bound to thrombin, APC, and plasmin. On the other hand, the 1 anti-thrombin mAb and the 1 anti-protein C mAb also bound to ␤ 2 GPI. Moreover, the binding of 1 crossreactive mAb to ␤ 2 GPI was inhibited by ␣-thrombin (which contains only the catalytic domain of thrombin). All 4 mAb displayed aCL activity.Conclusion. Taken together with the findings that some aCL bind to several serine proteases that participate in hemostasis and share homologous catalytic domains, these data demonstrate that some aCL in APS patients recognize one or more conformational epitopes shared by ␤ 2 GPI and the catalytic domains of diseaserelevant serine proteases.

show abstract

Some antiphospholipid antibodies recognize conformational epitopes shared by β₂‐glycoprotein I and the homologous catalytic domains of several serine proteases

Lin

Chen

Yang

et al. 2007

Arthritis & Rheumatism

View full text Add to dashboard Cite

show abstract

Bacterial Complement Escape

Jongerius

Ram

Rooijakkers

2009

Pathogen-Derived Immunomodulatory Molecules

View full text Add to dashboard Cite

Analysis of autoantibodies to plasminogen in the serum of patients with rheumatoid arthritis

et al. 1996

View full text Add to dashboard Cite

Sera from patients with rheumatoid arthritis containing high titers of anti-streptokinase antibodies were found to contain anti-plasminogen antibodies of the IgG and IgA classes. High titers of anti-plasminogen autoantibodies of the IgA class were also found in sera from patients with systemic lupus erythematosus and Sjögren syndrome. Studies of the immune response to thrombolytic therapy with streptokinase in patients with no prior history of autoimmune disease suggest a strong correlation between streptokinase administration and the appearance of autoantibodies to plasminogen of the IgA class. The IgA anti-plasminogen autoantibody is specific for an epitope in a region of plasminogen which binds streptokinase and the IgG autoantibody reacts with an epitope in the C-terminal region corresponding to the catalytic domain of the plasminogen zymogen. Our findings suggest a different origin for the two classes of anti-plasminogen immunoglobulins in rheumatoid arthritis patients. Since plasminogen binding to rheumatoid synovial fibroblasts is enhanced, the high titers of both classes of anti-plasminogen autoantibodies may add to the localization and perpetuation of the immune response. We suggest that plasminogen may be a target of the immune response in autoimmune disease.

show abstract

Binding and Activation of Plasminogen on Immobilized Immunoglobulin G

Cited by 35 publications

References 31 publications

Some antiphospholipid antibodies recognize conformational epitopes shared by β₂‐glycoprotein I and the homologous catalytic domains of several serine proteases

Some antiphospholipid antibodies recognize conformational epitopes shared by β₂‐glycoprotein I and the homologous catalytic domains of several serine proteases

Bacterial Complement Escape

Analysis of autoantibodies to plasminogen in the serum of patients with rheumatoid arthritis

Contact Info

Product

Resources

About

Binding and Activation of Plasminogen on Immobilized Immunoglobulin G

Cited by 35 publications

References 31 publications

Some antiphospholipid antibodies recognize conformational epitopes shared by β2‐glycoprotein I and the homologous catalytic domains of several serine proteases

Some antiphospholipid antibodies recognize conformational epitopes shared by β2‐glycoprotein I and the homologous catalytic domains of several serine proteases

Bacterial Complement Escape

Analysis of autoantibodies to plasminogen in the serum of patients with rheumatoid arthritis

Contact Info

Product

Resources

About

Some antiphospholipid antibodies recognize conformational epitopes shared by β₂‐glycoprotein I and the homologous catalytic domains of several serine proteases

Some antiphospholipid antibodies recognize conformational epitopes shared by β₂‐glycoprotein I and the homologous catalytic domains of several serine proteases