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H R HOLMAN

Publications and source records attributed to H R HOLMAN.

17 recordsLinked to original sources
PubMed1962

Lupus nephritis.

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Humans↗
PubMed1959

The precipitin reaction between DNA and a serum factor in systemic lupus erythematosus.

The sera of certain patients with systemic lupus erythematosus contain an antibody-like substance capable of reacting with highly purified DNA preparations from widely divergent sources. Precipitin reactions have been demonstrated by double diffusion in agar and quantitative precipitin curves have been obtained. Complement was observed to be fixed in the reaction. Evidence was obtained that the serum factor possessed antigenic properties similar to those of gamma-globulins and migrated with this fraction on zone electrophoresis. The interaction of this factor with DNA exhibited certain specific characteristics which differ considerably from non-specific reactions between DNA and proteins in general. The DNA-precipitating factor appeared to be one of a number of related factors reacting with nuclear constituents of many different cells. It differed in certain respects from the "LE factor" which is responsible for the formation of "LE cells." The accumulated evidence, although not yet conclusive, favors the concept that the precipitating factor represents an antibody to DNA, and that it is one of a number of autoantibodies elicited in this disease.

Antibodies↗
PubMed1957

Role of gamma globulins in pathogenesis of renal lesions in systemic lupus erythematosus and chronic membranous glomerulonephritis, with an observation on the lupus erythematosus cell reaction.

Utilizing the fluorescent antibody method for the histologic demonstration of localized gamma-globulins, we have made the following observations (in contradistinction to the lack of such findings in a variety of normal and pathologic, control kidneys). In systemic lupus erythematosus (a) gamma-globulins were localized in the thickened capillary walls, the "wire-loop" lesions, and the so called "hyaline thrombi" in glomeruli; (b) these sites of localization of gamma-globulins were correlated to a considerable degree with the pattern of accentuated eosinophilia of the glomeruli, as seen in hematoxylin-eosin sections, or with the pattern of PAS-positive areas in the glomeruli in sections stained with the periodic acid-Schiff reaction; (c) and gamma-globulins were localized rarely in large cytoplasmic granules in tubular epithelium and occasionally in glomerular capsular crescents, tubular protein casts, and inflammatory cells, particularly in the cytoplasm of cells identified as immature and mature plasma cells. In nephrotic glomerulonephritis (a) gamma-globulins were localized in the glomerular basement membrane and appertaining structures in chronic membranous glomerulonephritis; (b) gamma-globulins were apparently localized in the altered mesangium in chronic lobular glomerulonephritis; and (c) in the tubular protein casts, presumably representing abnormal glomerular filtrates, gamma-globulins were present in a lesser concentration and other serum proteins in a greater concentration than found in the glomeruli. In positive lupus erythematosus preparations the nuclei of leukocytes, while undergoing transformation and subsequent phagocytosis to form lupus erythematosus cells, were the sites of localization of gamma-globulin (presumably the lupus erythematosus factor) whereas in control preparations no nuclear localization of gamma-globulin occurred. These observations are discussed in relation to the pathogenesis of renal lesions in systemic lupus erythematosus, chronic membranous glomerulonephritis, and amyloidosis.

Amyloidosis↗
PubMed1957

An unusual protein component of high molecular weight in the serum of certain patients with rheumatoid arthritis.

In the sera of a number of patients with rheumatoid arthritis an unusual, high molecular weight protein component could be detected by direct ultracentrifuge analysis of whole serum. This material sedimented more rapidly than the normal 19 S component and reached concentrations up to 340 mg. per cent. Similar components were not observed in a limited control series. The high molecular weight material was present in the gamma-globulin fraction of serum and joint fluid. It had an S20,(w) of approximately 22 S and could be dissociated into 2 fractions, one of which had a sedimentation coefficient of approximately 19 S. Evidence for a direct relationship between the 22 S component and the gamma-globulin precipitation test was obtained. The latter reaction was found to occur in the presence of altered, aggregated gamma globulin. Absorption of serum with altered gamma globulin removed the 22 S component. There also appeared to be a connection with the sheep cell agglutination reaction and the latex fixation test. The 22 S fraction was always observed in sera giving the most positive tests. Procedures of density gradient and repeated preparative ultracentrifugation demonstrated that each of these reactions was caused by a high molecular weight fraction. The relationship between the unusual protein complex and various 19 S gamma-globulins and 19 S antibodies is discussed.

Arthritis, Rheumatoid↗