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Biomedical subjects

S B Taubman

Publications and source records attributed to S B Taubman.

5 recordsLinked to original sources

Screening tests for cell-mediated immunodeficiency diseases.

As our knowledge of immunology has become more sophisticated we have had to alter our ideas of the etiology of many immune deficiency diseases. Indeed, current concepts now prevalent have led to reclassification of a number of disease entities. In order to keep our diagnostic efforts abreast of the information being generated by the extensive immunology research programs now in progress, the clinical laboratory has been required to offer a new array of sophisticated tests on a relatively routine basis. This article is intended to serve as a brief review of immunobiology and immunodeficiency diseases with an indepth coverage of specialized tests generally available at the large centers. With an understanding of the principles, procedures, and pitfalls of the tests carried out the laboratory scientist is in a better position to assist the clinician in reaching the correct diagnosis. The detailed review is concerned with methods available to separate, classify, and subclassify lymphocytes and thereby allow a categorization of immune deficiency diseases. Toward that end there is a discussion of surface markers, rosetting, mitogenic and antigenic responsiveness as well as lymphokine production. With a view to present day research tests that might eventually find their way into the armamentarium of the clinical laboratory in the future, there is brief discussion of the methods presently used to classify T-cells as helper, suppressor, or effector cells, assays of some of the lymphokines, and measurement of antibody synthesis in cell culture.

Antigens, Surface

Interaction of C1s and C4. A binding phenomenon.

Addition of enzymatically active 125-I-labeled C1s (the esterase which is part of the activated complex protein of serum designated as the first component of complement or C1) to purified C4 (the naturally occurring fourth component of human serum complement) results in binding of a portion of the C1s to C4 as indicated by sucrose density gradient ultracentrifugation. Demonstration of binding requires hemolytically active C4, but not enzymatically active C1s. The latter was demonstrated by using DFP inactivated C1s as well as fragments of C1s produced by prior protease treatment of the C1s. While treatment of C1s with proteases (human leukocyte lysosomal enzymes, trypsin or plasmin) resulted in progressive inactivation of the enzymatic activity, the decline in esteratic activity occurred at a much slower rate than the decline in functional activity (inactivation of C4 in free solution). The data lead to the probable conclusion that C1s contains an enzymatic (or esteratic) site in addition to a binding site. The latter might be important for positioning a large molecule, such as C4, in order to effect proteolytic cleavage at the proper bond and hence prepare C4 to participate in the complement sequence.

Centrifugation, Density Gradient

Cell-detaching activity mediated by an enzyme(s) obtained from human leukocyte granules.

Granule proteins have been isolated from human peripheral blood leukocytes and their effects on intact tissue culture cells have been determined. Three hours after the addition of the mixture of granule hydrolases, both HeLa cells and human newborn fibroblasts were detached from one another and from their growth surface, but they seemed to remain viable, since cell-bound -51Cr was retained. Further studies with HeLa cells indicated that after as long as 24 hours in the presence of these enzymes the cells remained viable as judged by several independent criteria. The enzyme activity responsible for cell detachment was subject to inhibition by various protease inhibitors. Its molecular size, as determined by gel filtration, was approximately 20,000 daltons. In addition, the naturally occurring serum inhibitor of this enzyme activity was characterized as either alpha(1)-antitrypsin or another protein with similar properties.

Cell Adhesion

Inability of Ni++ and Co++ to release histamine from rat peritoneal mast cells.

Ni++ and Co++ concentrations from 10 minus 3M to 10 minus 6M were added to rat peritoneal mast cells. These metal ions, at the concentrations indicated, did not cause histamine release from the mast cells, and did not inhibit the histamine release mediated by compound 48/80. On the basis of these studies, anaphylactoid edema of the rat following injection of i++ or Co++ is on a basis other than a direct effect of the m-tal ion on mast cells.

Animals