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Biomedical subjects

H M Grey

Publications and source records attributed to H M Grey.

At least 145 records · Page 8Linked to original sources
PubMed1976

Some biological properties of beta2-microglobulin and its antibody.

beta2-Microglobulin on the surface of lymphocytes exists in two molecular forms, first as part of the HL-A antigen complex, and second as a free molecule unbound to other membrane macromolecules. Quantitative determinations of the numbers of molecules of beta2-microglobulin per lymphocyte when compared to published values for the numbers of HL-A molecules per cell are consistent with an excess of beta2-microglobulin compared to HL-A antigens on the cell surface. Turnover studies of beta2-microglobulin from the lymphocyte surface indicated that both beta2-microglobulin and HL-A components are metabolized at similar rates. beta2-Microglobulin appears to be released in the free form. HL-A antigens, if released from the cell surface, appear to be released unbound to beta2-microglobulin. The effects of anti-beta2-microglobulin antibody on lymphocyte activation, namely on the mixed lymphocyte reaction and on antigen induced proliferative response, were studied. Anti-beta2-microglobulin completely inhibited the mixed lymphocyte reaction and the antigen induced proliferative response.

Antibodies↗
PubMed1975

Beta2 microglobulin and lymphocytic infiltration in Sjögren's syndrome.

We measured salivary beta2 microglobulin concentrations in 49 patients evaluated for Sjögren's syndrome with a labial salivary-gland biopsy. The salivary concentration was elevated and a significant correlation (P less than 0.001) was found between the concentration and the degree of inflammation seen in the biopsy. Serum concentrations were increased in 135 patients with Sjögren's syndrome. Striking elevations were seen in patients with associated renal or lymphoproliferative complications. Three patients have an increase in serum beta2 microglobulin concentration in association with exacerbation of their disease, and six a decrease after clinically efficacious therapy. These data indicate that determination of beta2 microglobulin in saiva may provide a simple, noninvasive technic for estimation of the degree of local inflammation in autoimmune disease.

Adrenal Cortex Hormones↗
PubMed1975

Elevated salivary and synovial fluid beta2-microglobulin in Sjogren's syndrome and rheumatoid arthritis.

Beta2-Microglobulin is normally present in low concentrations in serum and other bodily fluids. By use of a radioimmunoassay, elevated concentrations of beta2--microglobulin were found in saliva and synovial fluid from patients with Sjogren's syndrome and rheumatoid arthritis, autoimmune inflammatory diseases that attack and destroy the salivary glands and articular tissues, respectively. Elevated beta2-microglobulin concentrations decreased in the saliva of two patients who simultaneously showed a clinical response to systemic treatment. Measurement of beta2-microglobulin in inflammatory fluids may offer a simple method of quantifying local activity in autoimmune states.

Arthritis, Rheumatoid↗
PubMed1975

Activation of T and B lymphocytes in vitro: presence of beta2-microblobulin determinants on allogeneic effect factor.

The biologically acitve entity termed allogeneic effect factor, which is produced by alloantigen-activated T cells and has been shown to regulate triggering and differentiation of B lymphocytes in vitro, has previously been demonstrated to possess antigenic determinants coded by genes in the I region of the H-2 gene complex of the mouse. The studies presented here provide evidence that allogeneic effect factor also possesses antigenic determinants identical or cross-reactive with beta2-microglobulin. These observations suggest an important role for beta2-microglobulin in the mechanism of cell-cell interactions and the consequences of such interactions on lymphocyte triggering and differentiation.

Animals↗
PubMed1975

Inhibition by anti-beta2-microglobulin antisera of responder cells and not of stimulator cells in the mixed lymphocyte reaction.

Specific antisera directed against beta2-microglobulin (B2m) have been shown to inhibit completely the mixed lymphocyte reaction (MLR). However, the mechanism of inhibition has been unclear. In the present study, further experiments were performed to determine the effect of anti-B2m on both the stimulator and responder cells in an MLR. The experimental design used was that of a xenogeneic MLR, using mouse and human lymphocytes. The ffect of anti-human B2m was studied in this system. Anti-human B2m inhibited the xenogeneic MLR only when human lymphocytes were used as responder cells and did not inhibit the MLR when they were used as stimulator cells...

Animals↗
PubMed1975

Studies on the cytophilic properties of human beta2 microglobulin.

Human beta2 microglobulin is cytophilic for mouse, rat, and to a lesser extent guinea pig lymphocytes and polymorphonuclear leukocytes but not for human, rabbit, chicken, frog, and turtle cells, nor for any mature erythrocytes tested. Mouse splenic lymphocytes bind 5- 7-fold more beta2 microblobulin than thymocytes although hydrocortisone-resistant thymocytes resemble spleen cells in this regard. The beta2 microglobulin binding by B and T cells in mouse spleen is similar. The structure responsible for beta2 microglobulin binding to the surface of cells is distinct from the Fc receptor specific for aggregated IgG.

Animals↗
PubMed1975

Effect of anti-beta2-microglobulin on antigen and allogeneic lymphocyte-induced proliferation of human lymphocytes.

The effect of anti-beta2-microglobulin (beta2m) on the mixed lymphocyte reaction (MLR), and an antigen-induced proliferative response was studied. Anti-beta2m IgG and Fab' fragments completely inhibited the MLR. Preincubation of stimulator or responder cells with anti-beta2m suggested that the major effect of anti-beta2m may be on the responder cell population. A clear-cut effect on responder cells was demonstrated by showing that anti-beta2m completely inhibited a MLR in which the stimulator population was a beta2m negative lymphoblastoid cell line. Anti-beta2m also inhibited PPD-induced proliferation of sensitized lymphocytes. The kinetics of this inhibition indicated that anti-beta2m added within the first 18 hr of stimulation was effective in inhibiting the proliferative response. These data are discussed in light of the hypothesis that beta2m may be a subunit of an antigen receptor on T cells.

Animals↗
PubMed1974

Receptors for aggregated IgG on mouse lymphocytes: their presence on thymocytes, thymus-derived, and bone marrow-derived lymphocytes.

An autoradiographic binding assay employing (125)I-labeled heat-aggregated mouse IgG2b myeloma protein (MOPC 141) was used to demonstrate receptors for IgG on 20-45% of Balb/c thymocytes and on 70-80% of splenocytes. Binding could also be shown with heat or BDB aggregates of another IgG2b (MOPC 195), with IgG1 and with human gamma-globulin, but not with aggregated chicken gamma-globulin, IgA, BSA, nor with aggregated Fab fragments of IgG2b. Optimum binding was obtained at 37 degrees C. Detection of binding was dependent upon aggregate size with complexes of more than 100 IgG molecules being optimal, aggregates of 6-25 detecting splenocytes but not thymocytes, and aggregates of less than 6 binding to a negligible extent. Comparison of grain counts on various cell types showed mastocytoma cells (P815) and macrophages averaging 40-50 grains/cell/day, allogeneically activated thymocytes 20-30, splenocytes 2-3, L5178 lymphoma cells 1, and positive thymocytes 0.6 grains/cell/day. Double labeling experiments for surface Ig, theta-antigen, and agg IgG receptor on mouse spleen cells indicated that a relatively high density of receptor was present on about 80% of B cells, 30% of T cells, and 60% of SIg(-), theta(-), null cells.

Animals↗
PubMed1974

Immunological identity of the small subunit of HL-A antigens and beta2-microglobulin and its turnover on the cell membrane.

A number of immunological methods have been employed to show that the small subunit of HL-A antigens, isolated either after papain treatment or after solubilization with detergent, is identical to beta(2)-microglobulin, a protein previously isolated from human urine and shown to be homologous in structure to constant region domains of immunoglobulins. Moreover, quantitative data indicate virtually total identity between the small subunit of HL-A antigens and beta(2)-microglobulin. Studies of the turnover of labeled HL-A antigens from the lymphocyte surface indicate that the two subunits turn over at similar rates, although only the small subunit could be detected in the culture medium. The significance of these observations is discussed.

Animals↗
PubMed1973

Two different complement receptors on human lymphocytes. One specific for C3b and one specific for C3b inactivator-cleaved C3b.

IN THE PRESENT STUDY IT WAS SHOWN THAT NORMAL PERIPHERAL LYMPHOCYTES HAVE TWO DIFFERENT COMPLEMENT RECEPTORS: one for C3b (the immune adherence receptor) and one for C3b subsequent to its cleavage by C3b inactivator. The two receptors are not cross-reactive and were shown by tests with various antisera to be antigenically distinct. Both the immune adherence receptor and the receptor for C3b inactivator-cleaved C3b were found on normal peripheral lymphocytes and on cultured lymphoblastoid cells. In 15 out of 18 chronic lymphatic leukemia patients, the immune adherence receptor was either partially or completely missing from the peripheral lymphocytes, while the lymphocyte receptor for C3b inactivator-cleaved C3b was retained. Normal erythrocytes, on the other hand, were found to have only the immune adherence receptor. Granulocytes from normal peripheral blood appeared to have only a receptor for C3b and did not have a receptor for C3b inactivator-cleaved C3b.

Antigen-Antibody Complex↗
PubMed1973

Combined studies of complement receptor and surface immunoglobulin-bearing cells and sheep erythrocyte rosette-forming cells in normal and leukemic human lymphocytes.

Human lymphocytes from normal peripheral blood, thymus, spleen, thoracic duct, and peripheral lymphocytes from patients with chronic lymphatic leukemia were studied for complement receptor sites (CRL), surface immunoglobulin (SIg), and for the ability to form rosettes with sheep erythrocytes (TRFC). The two B cell markers (CRL and SIg) were found to be in overlapping, but not totally identical populations, whereas cells that were able to form rosettes were found in a totally unrelated population of lymphocytes; TRFC is therefore probably a reliable marker for T cells. In peripheral blood 24% of lymphocytes had SIg, but only half of these were also CRL. Almost all of the non-SIg peripheral blood lymphocytes were TRFC. In the spleen and thoracic duct only a few lymphocytes were observed that had SIg and were not CRL. On the other hand, in two of three spleens studied 10-20% of cells were CRL that did not have SIg. In the thoracic duct all non-CRL that did not have SIg. In the thoracic duct all non-CRL, non-SIg cells were TRFC. In chronic lymphatic leukemia three findings were made: (a) The presence or absence of CRL was independent of the presence or absence of SIg so that in individuals whose cells were non-SIg. CRL were usually plentiful. (b) Leukemic cells were essentially negative for TRFC. (c) Leukemic cells reacted poorly with human C3 compared to mouse C3, EACmo detecting up to 20-fold more CRL than EAChu. This latter finding was in sharp contrast to normal CRL that reacted somewhat preferentially with EAChu. These data suggest that altered surface Ig receptors and complement receptors are present in chronic lymphatic leukemic cells. Since the cells obtained from all leukemic patients tested in this study had either the complement receptor or surface immunoglobulin in a high percentage of their cells and were essentially negative for TRFC, it is strongly suggested that leukemic lymphocytes are of B cell origin. The finding of lymphocytes with only one of the two B cell markers suggests that these markers are not uniformly present on all B cells and that depending on the source, one or the other may be deficient.

Animals↗