A Serologic Method Using Charcoal Particles from Commercial India Ink Application to Several Antigen-Antibody Systems with Special Reference to the Rheumatoid Factor

Pathobiology ◽  
1970 ◽  
Vol 36 (3) ◽  
pp. 173-178
Author(s):  
S. Erill ◽  
J. Gras
Keyword(s):  
Special Reference ◽  
Rheumatoid Factor ◽  
India Ink ◽  
Serologic Method ◽  
Antigen Antibody

Rate nephelometric measurement of rheumatoid factor in serum.

1979 ◽  
Vol 25 (11) ◽  
pp. 1909-1914 ◽  
Author(s):  
P R Finley ◽  
M J Hicks ◽  
R J Williams ◽  
J Hinlicky ◽  
D A Lichti
Keyword(s):  
Rheumatoid Factor ◽  
Control Level ◽  
Positive Control ◽  
Standard Curve ◽  
Graph Paper ◽  
Rate Of Increase ◽  
Human Sera ◽  
Reference Preparation ◽  
Level I ◽  
Antigen Antibody

Abstract We describe the measurement of rheumatoid factor in human sera with a rate nephelometer. The National Reference Preparation for Rheumatoid Factors is used to calibrate the assay in International Units. We used Hyland Positive Control, Level I, as a secondary standard. The standard curve is exponential, but is linear when plotted on log-log graph paper. Aggregated immune globulin (IgG) is the antigen used to detect rheumatoid factor (IgM-class antibody to IgG). The rate reaction measures the rate of increase in light-scatter by the antigen-antibody complexes; the reaction takes place in 17 to 20 s. Precision, linearity, and accuracy are excellent. Results agree well with those for a commonly used latex precipitation test. The advantages of speed, quantification in International Units, and superior discrimination of concentration as compared to serological titration provide a more reliable test for use in the diagnosis and treatment of rheumatoid arthritis.

scholarly journals STUDY ON CHRONIC BRONCHITIS WITH SPECIAL REFERENCE TO RHEUMATOID FACTOR

1971 ◽  
Vol 60 (8) ◽  
pp. 721-726
Author(s):  
Yukio NISHIMOTO ◽  
Shizutomo KATSUTA ◽  
Michio YAMAKIDO ◽  
Osami NISHIDA ◽  
Takuso SHIGENOBU ◽  
...  
Keyword(s):  
Special Reference ◽  
Rheumatoid Factor ◽  
Chronic Bronchitis

Application of Differential Light Scattering to the Latex Agglutination Assay for Rheumatoid Factor

1975 ◽  
Vol 21 (9) ◽  
pp. 1234-1237 ◽  
Author(s):  
Philip Blume ◽  
Leonard J Greenberg
Keyword(s):  
Rheumatoid Factor ◽  
Scattered Light ◽  
Polarized Light ◽  
Latex Agglutination ◽  
Antibody Assays ◽  
Potential Applications ◽  
Scatter Intensity ◽  
Antigen Antibody ◽  
Collimated Beam ◽  
Latex Agglutination Assay

Abstract When a suspension of particles is irradiated with a collimated beam of monochromatic polarized light of a wavelength close to the particle size and the intensity of the scattered light is measured as a function of angle, the scatter intensity is characterized by a series of relative maxima and minima. The nature of the signal depends on several significant variables that are characteristic of the particles. We have constructed a differential light scatter photometer and have applied the technique to analysis of rheumatoid factor by using latex particles coated with fraction II gamma-globulin. The results suggest that such a photometer may have potential applications in antigen-antibody assays based on the use of sensitized particles.

scholarly journals Rheumatoid factor (RF) production during anamnestic immune responses in the mouse. III. Activation of RF precursor cells is induced by their interaction with immune complexes and carrier-specific helper T cells.

1985 ◽  
Vol 161 (1) ◽  
pp. 88-97 ◽  
Author(s):  
P G Coulie ◽  
J Van Snick
Keyword(s):  
T Cells ◽  
T Cell ◽  
Immune Responses ◽  
Rheumatoid Factor ◽  
Immune Complexes ◽  
Cell Activation ◽  
Precursor Cells ◽  
Protein Antigens ◽  
Antigen Antibody ◽  
Antibody Ratio

IgG1 immune complexes were identified as the humoral stimuli responsible for the synthesis of IgG1-specific IgM rheumatoid factor (RF), which occurs in the mouse during the early stages of secondary immune responses to protein antigens. The specificity of this phenomenon was illustrated by the fact that complexes made with IgG1 F(ab')2 fragments or with antibodies of a different isotype failed to induce significant anti-IgG1 RF synthesis. The importance of immune complexes in the induction of RF was further underscored by the substantial increase in the titers of isotype-specific RF observed in the serum of mice immunized with IgG1- or IgG2a-complexed antigen rather than with antigen alone. The RF-inducing capacity of the complexes varied with the antigen/antibody ratio: it was maximal in antibody excess or at equivalence, but dramatically reduced in large antigen excess. The importance of T cell priming in RF precursor cell activation by immune complexes was demonstrated by the failure of T cell-deprived spleen cells to reconstitute the capability of irradiated mice to produce RF, and by the optimal RF responses observed after reconstitution of irradiated recipients with primed T cells and naive B cells. The involvement of T cells in this process could not be explained by the release of nonspecific B cell activators, because antigenic stimulation of primed T cells failed to enhance the activation of RF precursor cells by immune complexes of unrelated antigen.

scholarly journals Historical observations contributing insights on etiopathogenesis of rheumatoid arthritis and role of rheumatoid factor

2016 ◽  
Vol 213 (10) ◽  
pp. 1937-1950 ◽  
Author(s):  
Eng M. Tan ◽  
Josef S. Smolen
Keyword(s):  
Rheumatoid Arthritis ◽  
Rheumatoid Factor ◽  
Inflammatory Mediators ◽  
Targeting Therapy ◽  
Initiation Phase ◽  
Novel Approach ◽  
Recurrent Inflammation ◽  
Antigen Antibody ◽  
Second Wave

When studies on rheumatoid arthritis (RA) that were made many decades ago and could be considered “historical” in nature are analyzed in the context of recent observations, important insights on RA and on the function of rheumatoid factor (RF) become apparent. RF in the role of antibody to immune complexes (ICs) appears to be involved in activation of the complement system and in the production of chemotactic and inflammatory mediators, creating a condition that can be sustained and reinitiated. In the synovial cavity, a state of nonresolving inflammation is produced with the formation of citrullinated protein antigen–antibody complexes or other forms of ICs. This is followed by a second wave of IC production in the form of RF acting as antibody reactive with the initial ICs. Both of these processes are associated with complement consumption and production of inflammatory mediators. We present a model of an initiation phase of RA that might represent an example of repetitive formation of ICs and complement-mediated inflammation. Targeting therapy at this phase of RA to break the cycles of recurrent inflammation might be a novel approach to aid in further control of the disease.

scholarly journals INTERACTION OF THE RHEUMATOID FACTOR WITH ANTIGEN-ANTIBODY COMPLEXES AND AGGREGATED GAMMA GLOBULIN

1958 ◽  
Vol 108 (1) ◽  
pp. 105-120 ◽  
Author(s):  
G. M. Edelman ◽  
H. G. Kunkel ◽  
E. C. Franklin
Keyword(s):  
Rheumatoid Factor ◽  
Gamma Globulin ◽  
Human Albumin ◽  
Heat Denaturation ◽  
Soluble Antigen ◽  
Cell Agglutination ◽  
Soluble Aggregates ◽  
Human Gamma Globulin ◽  
Ultracentrifugal Analysis ◽  
Antigen Antibody

The effect of highly purified rheumatoid factor on the precipitin reactions of various antigen-antibody systems was determined. The amount of nitrogen precipitated was increased over a broad range when the factor was added to ovalbumin, human albumin, or human gamma globulin, and the corresponding rabbit antibodies. In the zone of antigen excess, soluble antigen-antibody complexes were precipitated by rheumatoid factor. Soluble aggregates of human and rabbit gamma globulin, produced by heating at 63°C., treatment with urea plus mercaptoethanol or treatment with guanidine, also precipitated with rheumatoid factor. Ultracentrifugal analysis of dissolved specific precipitates showed the presence of aggregated gamma globulin. The sedimentation rate of reactive aggregates was greater than 20 S, and concentrated preparations free of the non-reactive 7 S gamma globulin could be prepared by various procedures of zone centrifugation. These aggregates showed a high inhibitory capacity in the sensitized sheep cell agglutination reaction. Solid gamma globulin, prepared by heat denaturation, also selectively adsorbed the rheumatoid factor, and removed or decreased the activity in the various precipitation and agglutination reactions. Elution of highly purified active preparations from the solid gamma globulin could be carried out with urea or acid buffers. Evidence for interaction between rheumatoid factor and low molecular weight gamma globulin without precipitation, was also obtained. This interaction appears to occur in the circulation of patients with rheumatoid arthritis. The question of whether the rheumatoid factor represents an antibody to gamma globulin was discussed. Points of similarity to the behavior of complement also were cited.

scholarly journals A mechanism for the induction of immunological tolerance by antigen feeding: antigen-antibody complexes.

1975 ◽  
Vol 142 (6) ◽  
pp. 1509-1519 ◽  
Author(s):  
C André ◽  
J F Heremans ◽  
J P Vaerman ◽  
C L Cambiaso
Keyword(s):  
Rheumatoid Factor ◽  
Immune Complexes ◽  
Immunological Tolerance ◽  
Antibody Activity ◽  
Previous Contact ◽  
Primary Type ◽  
A Site ◽  
Antigen Antibody

We have previously reported on the induction, in mice, of a systemic (splenic) immune response with IgA as the dominant antibody, as a result of a short (4 day) intragastric immunization course with foreign erythrocytes. This response was followed by a prolonged period of hyporesponsiveness to similarly administered antigen. Here it is shown that this hyporesponsiveness is also manifested towards antigen given intraperitoneally, and that one is therefore dealing with tolerance, not with failure to absorb antigen from the gut. In contrast, mice primed parenterally and then challenged intragastrically behaved as if never having any previous contact with the antigen, i.e., with a primary-type splenic response of predominant IgA character. This agrees with our former conclusion that splenic responses to enterically absorbed antigen reflect colonization of the spleen by cells sensitized locally in the gut wall, a site not readily primed by the parenteral route. Serum from intragastrically immunized mice contained a very active tolerogen. In vivo, it was capable of conferring tolerance to nonimmune recipient mice. In vitro, it paralyzed the activity of antibody-producing cells. Inhibitory sera has weak antibody activity, restricted to the IgA class, and contained immune complexes reacting with rheumatoid factor but not with C1q. Elimination of these complexes by means by insolubilized rheumatoid factor abolished the tolerogenic effect. In conclusion, the enterically induced tolerogen seems to consist of immune complexes with IgA as the antibody.

scholarly journals Efficient and selective presentation of antigen-antibody complexes by rheumatoid factor B cells.

1991 ◽  
Vol 173 (2) ◽  
pp. 487-489 ◽  
Author(s):  
E Roosnek ◽  
A Lanzavecchia
Keyword(s):  
T Cells ◽  
B Cells ◽  
Rheumatoid Factor ◽  
Factor B ◽  
Barr Virus ◽  
Membrane Immunoglobulin ◽  
Cell Clones ◽  
Lower Extent ◽  
Epstein Barr ◽  
Antigen Antibody

Using Epstein-Barr virus B cell clones and antigen-specific T cell clones, we asked how antigen-antibody complexes are handled by B cells. We found that the only B cells capable of efficient presentation of antigen-antibody complexes are those that bind the complexes via membrane immunoglobulin, i.e., rheumatoid factor-producing B cells and, to a lower extent, antigen-specific B cells. On the contrary, nonspecific B cells, although capable of binding antigen-antibody complexes, fail to present them to T cells. Thus, rheumatoid factor B cells can present any antigen in the context of an immune complex and be triggered by T cells specific for a variety of foreign antigens. These results demonstrate a mechanism of intermolecular help that may be responsible for the production of rheumatoid factor and possibly of other types of autoantibodies.

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