Biomedical subjects
Publications and source records attributed to D Pressman.
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Cell membrane components that contain beta 2-microglobulin were purified from cells of a human T cell-type leukemia cell line, HPB-ALL. They contained membrane components that have the same molecular size and the same subunit structure as HLA(A,B,C) antigens but are separable from the typical beta 2-microglobulin-containing cell membrane components, i.e., the HLA (A,B,C) antigens, by xenoantibody reagents. A sensitive radioimmunoassay was constructed for detection of the T cell membrane components. The assay revealed that the cell membrane components are expressed exclusively on cells of T cell-type leukemia cell lines among the human lymphoid cell lines tested, predominantly in thymus, among the human organs and tissues tested. They were not present on cells of human B cell-type cell lines or on cells of nonlymphoid organs and tissues. No alloantibodies directed to the T cell membrane components, the putative human homologues of mouse TL antigens, were found in any of the human tissue typing sera tested.
Human Ia-like antigens in liver and kidney were shown by the immunofluorescence assay to be present mostly in the endothelial-mesenchymal cells of these organs. The parenchymal cells apparently contained no human Ia-like antigens. The antigens in liver and kidney were purified and shown to have the same subunit structure as human Ia-like antigens of cultured B-lymphoid cells. The human Ia-like antigens in non-lymphoid organs, not only in liver and kidney but also in testis, heart, muscle and brain, carried all the xenoantigenic characteristics of human Ia-like antigens expressed on lymphoid cells of B-cell lineage.
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The immunochemical analysis of Daudi Ia molecules by a variety of alloantisera led to the recognition of at least three molecular species carrying different antigenic determinants: DRw6, DC-1, and DC-2. Genetic as well as structural evidence indicates that DRw6 and DC-1 molecules are controlled by separate, HLA-linked loci, rather than by alleles at the same locus. The alloantigenic determinants appear to be expressed on the small Ia subunit. DC-1 and DC-2 determinants discussed had not been defined by serological analysis at the population level, but were demonstrated to be present by immunochemical analysis at the molecular level.
A human glycoprotein was isolated from the urine of a patient with plasma cell leukemia. It appears pure and homogeneous when examined by immunoelectrophoresis, sodium dodecyl sulfate (NaDodSO4)-polyacrylamide gel electrophoresis, gel filtration in 6 M guanidine hydrochloride (Gdn.HCl), and NH2-terminal amino acid sequence analysis. It has a brown color due to a tightly (most likely covalently) bound chromophore group(s) and migrates to the alpha1 region in immunoelectrophoresis. A molecular weight (mol wt) of 27 000 was obtained for the glycoprotein by gel filtration in 6 M Gdn.HCl. Its approximate mol wt determined by Na-DodSO4-polyacrylamide gel electrophoresis is 29 000 on 5% and 7.5% and 10% gels. Amino acid and hexosamine analyses showed that it is a glycoprotein and indicated that it contains four half-cystine residues per molecule. Based on the above observations we designated it "alpha1-microglycoprotein" (alpha1-MGP). Isoelectric focusing of alpha1-MGP showed a significant charge heterogeneity, although only a single NH2-terminal amino acid sequence was obtained for alpha1-MGP, i.e., Gly-Pro-Val-Pro-( )-Pro-Pro-Asx-Asx-Ile-Glx-Val-Glx-Glx-Asx-Phe-Phe-Ile-(Ser or Ala)-Arg. The alpha1-MGP was found in significant concentrations in the urine of many patients with neoplastic diseases.
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A rabbit antiserum raised against papain-solubilized H-2 antigens has been used to investigate the eventual expression of H-2 antigens and related molecules on embryonal carcinoma cells and on other types of mouse cells. No material reacting with this serum could be detected on cells carrying the F9 antigen. It is concluded that no H-2 antigen or cross-reacting material is expressed on these cell types.
Cell membrane components bound to beta2-microglobulin were isolated from Renex 30 (a nonionic detergent)-solubilized membrane materials of two human T cell-type cell lines, MOLT-4 and CCRF-CEM, by gel filtration and lectin affinity chromatography. The isolation was carried out by following the beta2-microglobulin activity by radioimmune inhibition assay. The T cell membrane components bound to beta2-microblogulin had a uniform molecular size of about 200,000 daltons and most of them showed an affinity to lentil lectin. The isolated membrane components were radioiodinated and examined for identity to HLA antigens by sequential precipitation with rabbit anti-HLA antiserum (specific to HLA large components) and with rabbit anti-beta2-microblogulin antiserum. In addition to HLA antigens, the beta2-microglobulin-bound components obtained from the MOLT-4 cells were found to contain certain membrane components that are the same in molecular size as the HLA large components but that are different antigenically from the HLA large components. On the other hand, the beta2-microglobulin-bound membrane components obtained from the CCRF-CEM cells were all HLA antigens. No other membrane components were involved in the binding.
The primary antibody response to dextran B1355 in BALB/c mice is largely a homogenous IgM antibody. This antibody appears to be similar if not identical to the myeloma protein, protein 104E, for the following reasons: a) isoelectric focusing of the 7S monomers, separately and together in co-isoelectric focusing, give the same pattern, both in the presence and absence of 4M urea; b) the inhibition of lysis of the dextran-coated SRBC by specifically purified anti-dextran antibody and by protein 104E required essentially the same concentration of dextran B1355. This similarity was further demonstrated by plaque assays with dextran-coated SRBC, in which the formation of plaques was inhibited by free dextran. Inhibition of plaques produced by both types of cells required essentially the same concentration of dextran B1355. On these bases, there appears to be no difference in properties (or in structure) between the myeloma protein and the induced antibody.
Rabbit immune sera against human cells of a non-T, non-B leukemia cell line bearing the Ph1 chromosome (NALM-1) were characterized. After proper and exhaustive absorption, the sera were tested by indirect membrane immunofluorescence on a panel of 19 human hematopoietic cell lines with T-, B-, or non-T, non-B cell surface characteristics. The absorbed sera reacted specifically with NALM-1 cells but not with cells of another Ph1-positive cell line, K-562. Four of the 6 leukemia T-cell lines, 2 of the 4 leukemia-lymphoma B-cell lines, all of 4 acute lymphoblastic leukemia (ALL) lines with non-T, non-B cell characteristics, and uncultured cells of all patients with non-T, non-B cell ALL were reactive with the antisera. A cross-absorption study of the antisera suggested that a single antigenic complex is involved in this antigen specificity. The antigen involved appears to be a common non-T, non-B ALL one that has been described previously.
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