scholarly journals Suitability of Commercial Human Rheumatoid Factor Rapid Tests for Detection of Rheumatoid Factors in Dog Serum

Author(s):  
C.N. Weber ◽  
J.O. Zeitz ◽  
E. Müller
1986 ◽  
Vol 164 (5) ◽  
pp. 1809-1814 ◽  
Author(s):  
V Agnello ◽  
J L Barnes

Evidence was obtained that both the WA and BLA crossidiotype (XId) groups are conformational antigens requiring both L and H chains and that with heat denaturation the antigens that define the XIds and antigen-binding activity are lost in parallel. In contrast, the primary structure-dependent crossreactive idiotype (CRI), PSL2, which is only weakly detected on native Wa and Bla monoclonal rheumatoid factors (mRFs), became prominently detected on the heated Wa and Bla mRFs. Heat denaturation may provide a simple method for distinguishing Ids determined by conformational antigen from primary structure-dependent Ids. In addition to heat denaturation, some acid conditions commonly used for preparation of RFs were also found to cause marked loss of Id antigen. The finding of PSL2-CRI on Bla mRF indicates that this Id is not unique to the WA XId.


The Lancet ◽  
1999 ◽  
Vol 353 (9149) ◽  
pp. 297 ◽  
Author(s):  
MP Grobusch ◽  
U Alpermann ◽  
S Schwenke ◽  
T Jelinek ◽  
DC Warhurst

1971 ◽  
Vol 134 (3) ◽  
pp. 286-295 ◽  
Author(s):  
R. J. Winchester ◽  
H. G. Kunkel ◽  
V. Agnello

γG globulin complexed in an unusual form has been demonstrated in the serum of many patients with rheumatoid arthritis. Such complexes have been detected and isolated principally through precipitation reactions with monoclonal γM rheumatoid factors. These monoclonal rheumatoid factors exhibited a greater sensitivity to react with small complexes or aggregates of γ-globulin than polyclonal rheumatoid factor from rheumatoid arthritis sera or isolated C1q. The serum complexes consisted in large part of high molecular weight but acid-dissociable 7S γG globulin molecules They however differed from the complexes in the joint fluid by not yielding precipitates with C1q and were not found in association with evidence of marked serum complement fixation or activation. A small number of systemic lupus erythematosus sera, primarily those forming cryoprecipitates, also gave reactions with monoclonal rheumatoid factor. Sera from patients with a variety of nonrheumatic diseases gave a low incidence of reactions. The exact nature of the complexes in the rheumatoid arthritis sera remains somewhat in doubt although γG rheumatoid factors appear partly involved.


1988 ◽  
Vol 1 (3) ◽  
pp. 211-218
Author(s):  
P. Peichl ◽  
G. Haberhauer ◽  
M. Scriba ◽  
H. Bröll

We compared antibodies (Ab) with both, antiviral and anti IgG properties in patients with rheumatoid arthritis with malignant progress, short remissions and no improvement to therapy. The selective binding of Rheumatoid Factor (RF) to antigen structures of CMV were tested in 180 patients by a newly established ELISA with antiidiotypic goat antibodies of CMV neutralizing human monoclonal Ab and against the virus antigen directly. Displacement reactions on the idiotypic bindingsite as well as comparative ELISA gave proof of the special RF activity. 24,2% of the patients suffering from RA, with IgM RF, showed selective binding to antigen structures of CMV and anti IgG activity. The evidence of the specific binding capacity of RF to the virus antigen in chronic CMV infection as well as their defined binding capacity to the Fc Fragment of IgG suggest CMV specific RF as the pathogenetic factor of malignant forms of inflammatory rheumatism.


1987 ◽  
Vol 165 (1) ◽  
pp. 263-267 ◽  
Author(s):  
V Agnello ◽  
F Goñi ◽  
J L Barnes ◽  
M T de la Vega ◽  
B Frangione

The amino acid sequence of the L-CDR2 (complementarity-determining region) of Bla mRF (monoclonal rheumatoid factor) is identical to that of the Wa mRFs. The PSL2-CRI (crossreactive idiotype), as determined by anti-PSL2, which has been shown to be present on all Wa mRFs, is also present on the Bla mRF and other monoclonal autoantibodies. PSL2-CRI is, therefore, not unique to Wa mRFs and may be present on most IgM kappa monoclonal autoantibodies. Whether PSL2-CRI is a crossidiotype (XId) that is selectively present on autoantibodies or represents an allotypic marker for a V kappa III gene is undetermined.


1989 ◽  
Vol 48 (6) ◽  
pp. 488-495 ◽  
Author(s):  
V R Bonagura ◽  
J F Wedgwood ◽  
N Agostino ◽  
L Hatam ◽  
L Mendez ◽  
...  

1980 ◽  
Vol 151 (6) ◽  
pp. 1514-1527 ◽  
Author(s):  
V Agnello ◽  
A Arbetter ◽  
G Ibanez de Kasep ◽  
R Powell ◽  
E M Tan ◽  
...  

Cross-reactivity of a monoclonal rheumatoid factor with an antigen present on IgG and DNA-nucleoprotein was demonstrated, and evidence presented that the combining site of the antibody was involved in the reaction. The antigen on the DNA-nucleoprotein was shown to involve both DNA and histone fraction H2A + H2B and was trypsin sensitive. The relative binding affinity of the antibody appeared to be greater for IgG than the DNA-histone antigen. Similar polyclonal cross-reactive rheumatoid factors were found in a variety of diseases. A high incidence was found among patients with rheumatoid arthritis and mixed connective tissue disease. None were detected in patients with systemic lupus erythematosus and idiopathic cryoglobulinemia. Studies on one representative isolated polyclonal rheumatoid factor demonstrated the same reactivity with DNA-histone H2A + H2B as the monoclonal antibody. Cross-idiotype studies using antigen-binding inhibition methods demonstrated the same cross-idiotype on the polyclonal and the monoclonal rheumatoid factor which reacted with DNA-histone. This cross-idiotype was shown to be distinct from the cross-idiotypes previously demonstrated on monoclonal IgM proteins with anti-gamma-globulin activity.


1993 ◽  
Vol 178 (6) ◽  
pp. 1903-1911 ◽  
Author(s):  
G B Knight ◽  
V Agnello ◽  
V Bonagura ◽  
J L Barnes ◽  
D J Panka ◽  
...  

The WA cross-idiotype (XId) is the major XId among human monoclonal rheumatoid factors (mRF) and is almost always associated with the light (L) chain XId, 17.109, and the heavy (H) chain XId, G6. A cell line, 35G6, was cloned that bears the WA XId, but shows no reactivity with immunoglobulin G (IgG) and is negative for the 17.109 and G6 XIds. The 35G6 L chain appears to be derived from the same VKIII-JKI genes as most WA mRFs L chains. In contrast to the WA mRFs H chains in which VH1 genes are used, the 35G6 IgM expresses a VH3 gene. Sequence comparisons with other WA XId-positive mRF suggested several common structural features that may be related to the WA XId and differences that may relate to lack of IgG reactivity. Cells similar to 35G6 have previously been described in pokeweed mitogen-stimulated cell lines of peripheral blood lymphocytes from normal individuals and patients with rheumatoid arthritis and type II mixed cryoglobulinemia. These observations were confirmed, and in addition, it was shown that the majority of WA XId-positive cells in these cultures were negative for the 17.109 and G6 XIds. The presence of the WA XId in the absence of IgG reactivity suggests that the WA XId is more directly associated with an antigen specificity other than IgG, and its association with RF activity may be incidental. It is postulated that these WA XId-positive RF-negative antibodies may serve a physiologic role as natural antibodies to a pervasive pathogen, and that IgG reactivity is a consequence of somatic diversification accompanying proliferation of the WA XId-positive RF-negative cell.


Sign in / Sign up

Export Citation Format

Share Document