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Biomedical subjects

E R Abney

Publications and source records attributed to E R Abney.

27 records · Page 2Linked to original sources
PubMed1976

Identification of a high molecular weight protein on the surface of murine thymus and thymus-dependent cells.

Rabbit anti-mouse Ig reacted with mouse thymocytes resulting in the formation of caps which were shed into the medium and subsequently injected into rabbits. The antiserum from these animals (AMTP) reacted strongly with thymocytes and peripheral T cells and weakly with B cells. The antiserum did not react via the Thy-1 antigen and could be made specific for T lymphocytes by absorption with B lymphocytes. By surface labeling of lymphocytes with 125I, it could be shown that the major T lymphocyte antigen recognized by AMTP was one, or possibly two, large, single chain molecules with a molecular weight of approximately 200000. This molecule was not Ig and, furthermore, the AMTP did not react with cell surface Ig of B lymphocytes. The implications of this finding for previous reports on the existence of immunoglobulin on T lymphocytes are discussed.

Animals↗
PubMed1976

Immunoglobulin M receptors on memory cells of immunoglobulin G antibody-forming cell clones.

The memory cells of two antibody-forming cell clones had receptors of the IgM class, even though the clones had been producing IgG1 or IgG2a anti-2,4-dinitrophenyl antibodies for 9-15 months previously (on exposure to antigen). Thus a phenotypic switch in heavy chain constant region evidently occurred after re-exposure of these memory cells to antigen. To show that, we first removed the clonal cells' surface immunoglobins by "capping" and "stripping", with class- or subclass-specific antisera. Then, to assay their remaining receptor activity, the cells were incubated with antigen in vitro, washed and transferred (together with carrier primed cells) to irradiated recipients, and their antibody responses to this in vitro boost were assayed by iselectric focusing. Pretreatment with anti-mu serum, as well as with anti-Fab(kappa), prevented the responses of the IgG1 and IgG2a clones to an in vitro boost, while anti-gamma1 and anti-gamma2a antisera had no effect. An antiserum to the putative mouse IgD also had no effect. The anti-mu serum failed to react with the IgG1 and IgG2A clonal serum antibodies in the test tube. Some other contaminating clones were suppressed completely only by the anti-Fab serum. This result strongly suggests that switching in class commitment may occur during the differentiation of memory cells to antibody producers, and may therefore be antigen-dependent. It also implies that some apparently naive cells with surface IgM may, in reality, be B memory cells.

Animals↗
PubMed1976

Location of nucleotide pyrophosphatase and alkaline phosphodiesterase activities on the lymphocyte surface membrane.

1. Isolated mouse spleen lymphocytes hydrolysed UDP-galactose added to the medium. Nucleotide pyrophosphatase activity that accounted for this hydrolysis was enriched to a similar extent as alkaline phosphodiesterase and 5'-nucleotidase in a lymphocyte plasma-membrane fraction. 2. The cell surfaces of mouse spleen and thymus lymphocytes were iodinated with 125I by using the lactoperoxidase-catalysis method. Detergent extracts of the cells were mixed with a purified anti-(mouse liver plasma-membrane nucleotide pyrophosphatase) antiserum and the immunoprecipitates analysed by polyacrylamide-gel electrophoresis. Only one major radioactive component, similar in size (apparent mol.wt 110000-130000) to the liver enzyme, was observed. 3. Electrophoresis of an iodinated spleen plasma-membrane fraction indicated peaks of radioactivity, including one of apparent mol.wt 110000-130000. 4. When detergent extracts of spleen lymphocytes were passed through a Sepharose-bead column containing covalently attached anti-(nucleotide pyrophosphatase) antiserum, the nucleotide pyrophosphatase activity was retained by the beads, whereas protein and leucine naphthylamidase activity were eluted. 5. The results indicate that nucleotide pyrophosphatase and alkaline phosphodiesterase activities are due to the location of the same or similar enzymes at the outer aspect of the lymphocyte plasma membrane. Some possible functions of enzymes at this location are discussed.

Animals↗
PubMed1976

Heterogeneity of surface immunoglobulin on murine B lymphocytes.

Surface IgM on murine splenic lymphocytes was capped using a rhodamine-coupled anti-mu chain system. The cells were then reacted with a polyspecific, fluorescein-coupled anti-mouse immunoglobulin (Ig) under non-capping conditions. A large number (31-41% of total Ig-bearing cells) which gave red caps with anti-mu subsequently stained green peripherally with anti-Fab under the non-capping conditions. The remaining stained cells were divided between those showing only red caps (17-29% of Ig-bearing cells) and those showing only green rings (37-45% of Ig-bearing cells). These data are interpreted by assuming that most of the staining with the second reagent (fluorescein-coupled anti-mouse Ig) is due to the presence of surface associated IgD.

Animals↗