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Biomedical subjects

L KORNGOLD

Publications and source records attributed to L KORNGOLD.

At least 19 recordsLinked to original sources
PubMed1961

Rheumatoid factor and the pathogenesis of rheumatoid arthritis.

In analogy with the two categories of reactants which are used in the serological tests for the unusual category of macroglobulins called rheumatoid factor, two fluorescent reactants have been prepared for the detection of rheumatoid factor in situ in tissue sections: fluorescent antigen-rabbit antibody (immune) complex, in the present study, and fluorescent aggregated human gamma-globulin, in previous work. Plasma cells in the synovial membrane and germinal center cells and internodular plasma cells in lymph nodes are the sites of origin of rheumatoid factor in active rheumatoid arthritis, whether occurring in adults or children. Plasma cells and germinal center cells which form rheumatoid factor detectable with fluorescent immune complex are less numerous than those which contain factor demonstrable with fluorescent aggregate. In the same tissues, plasma cells and germinal center cells which contain macroglobulin (19S human gamma-globulin) detectable with fluorescent antibody-but not showing the reactivity of rheumatoid factor-are more abundant than those containing rheumatoid factor. While macroglobulin and rheumatoid factor are almost exclusively formed in the cytoplasm, these proteins are also detectable in the nucleus of an occasional plasma cell. Normal and pathological synovial and capsular tissues, lymph nodes, and connective tissues obtained from individuals without rheumatoid arthritis are not stained with fluorescent immune complex or, except for an unusual example of Waldenstrom's macroglobulinemia, with fluorescent aggregate. The cellular origin, as well as certain chemical and immunological attributes, of rheumatoid factor suggests an antibody-like nature and function. The observations cited are consistent with the behavior anticipated for cellular rheumatoid factor, were it primarily an antibody direct to an altered human gamma-globulin and cross-reacting with rabbit gamma-globulin. However, it is also possible that there are two or more cellular rheumatoid factors. Lesion-associated protein precipitates having the composition anticipated for rheumatoid factor-antigen complex are localized in the amyloid depositions in kidney and spleen of an individual who died with amyloidosis secondary to rheumatoid arthritis.

Adult↗
PubMed1959

Macroglobulinemia. III. The effect of mercaptoethanol on the antigenic structure of macroglobulins.

The monomers obtained by treating gamma(1)-macroglobulins with mercaptoethanol have proved to be antigenically different from normal 7S 7gamma-globulin. The depolymerization of the macroglobulins resulted in the loss of several antigenic determinants, although the monomers still cross-reacted with antisera against macroglobulins. Reaggregation of the monomers occasionally resulted in the reconstitution of some or all of the antigenic determinants that were lost during depolymerization. Repeated freezing and thawing of pathological macroglobulins in iodoacetate resulted in their complete antigenic destruction. Repeated freezing and thawing of one of the monomers in excess iodoacetate resulted in the degradation to a protein antigenically indistinguishable from Bence Jones protein. The other two monomers studied were stable under these conditions.

Antigens↗
PubMed1957

Macroglobulinemia. I. The antigenic relationship of pathological macroglobulins to normal gamma-globulins.

Highly purified pathological macroglobulins, which had been characterized electrophoretically and in the ultracentrifuge, were studied by the Ouchterlony gel diffusion technique. These macroglobulins were shown to be antigenically related to normal gamma(1)-macroglobulin (19S) as well as the 7S gamma-globulins. The pathological macroglobulins differ among each other and they are antigenically deficient when compared with the normal macroglobulin. There is no correlation between the macroglobulin's antigenic structure and its physico-chemical properties.

Antigens↗
PubMed1957

Macroglobulinemia. II. Antisera specific for pathological macroglobulins.

Rabbits were immunized with three highly purified macroglobulins, from patients with macroglobulinemia. The antisera reacted with two macroglobulins with sedimentation constants of 19S and 26S of homologous antigen, and cross-reacted with the 7S and 19S globulins of normal gamma(1)-globulin and the heterologous pathological 19S macroglobulins. Exhaustive absorption of these antisera with normal gamma-globulins rendered them specific for the homologous macroglobulins. The antigenic properties of the pathological macroglobulins indicate that these proteins are abnormal.

Animals↗