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Biomedical subjects

L KORNGOLD

Publications and source records attributed to L KORNGOLD.

At least 19 recordsLinked to original sources
PubMed1963

THE CELLULAR ORIGIN OF HUMAN IMMUNOGLOBULINS (GAMMA-2, GAMMA-1M, GAMMA-1A).

A study was made of the cellular origin of human immunoglobulins (gamma(2), gamma(1M), gamma(1A)). The results indicated that two closely related families of cells form immunoglobulins in human lymphoid tissue: germinal (reticular) centers and plasma cells. Thus their cellular origin in addition to their known antigenic relations further justifies placing the immunoglobulins in one family of proteins. Immunoglobulins were also formed to a small extent in primitive reticular cells which resembled those of germinal centers but were separated from them. Possibly such cells were undergoing transition to the much more numerous plasma cells with which they were commonly associated. The mantles of small lymphocytes which surrounded germinal centers did not contain detectable quantities of immunoglobulins. While in general only one type of immunoglobulin was present in an individual cell or germinal center, gamma(2)- and gamma(1M)-globulin were identified on occasion in the same plasma cell and germinal center. A peculiarity of the fetal thymus gland was the presence of immunoglobulin, mainly gamma(1M), in a small number of cells of small and intermediate size and primitive reticular appearance and in Hassall's corpuscles.

Cell Biology↗
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↗