apyrase and Burkitt-Lymphoma

B cell lymphomas' (BCL) current diagnosis is usually based on a combination of morphology, immunophenotype, recurrent cytogenetic aberration and clinical features. However, even with these diagnostic tools, a definitive diagnosis can be difficult to achieve. Therefore, the aim of this study was to assess the profile of CD39, CD43, CD81, and CD95 expressions in diffuse large B cell lymphoma (DLBCL), follicular lymphoma (FL), and Burkitt lymphoma (BL) cases.. To address this issue, we investigated the expression of CD39, CD43, CD81, and CD95 by eight-color flow cytometry in retrospective cases from 2014 to 2016.. The study included 27 adult patients diagnosed with DLBCL, FL, and BL during the study period. Four patients were diagnosed with germinal center B cell-like DLBCL (GCB DLBCL), seven with non-GCB DLBCL, nine with FL, and seven with BL. CD39 seems to be especially relevant to differentiate non-GCB DLBCL from BL and from FL. BL showed stronger expression of CD43 when compared to FL and GCB DLBCL. Moreover, CD43 may help to distinguish non-GCB DLBCL from GCB DLBCL. CD81 expression was much stronger in BL when compared to the other three groups of patients. Lastly, CD95 may also help to distinguish BL from the other subtypes, as BL cells expressed this antigen at low levels.. In combination, CD39, CD43, CD81, and CD95 expressions appear to be helpful to distinguish CD10

Topics: Adult; Aged; Aged, 80 and over; Apyrase; B-Lymphocytes; Biomarkers, Tumor; Burkitt Lymphoma; fas Receptor; Female; Flow Cytometry; Germinal Center; Humans; Immunophenotyping; Leukosialin; Lymphoma, Follicular; Lymphoma, Large B-Cell, Diffuse; Male; Middle Aged; Retrospective Studies; Tetraspanin 28

The A-myb gene is structurally related to the c-mby proto-oncogene, a transcription factor involved in the regulation of hemopoietic proliferation and differentiation. Recent evidence has shown that A-myb also functions as a transcriptional activator. We have previously demonstrated that A-myb RNA is not expressed in most mature human leukocytes at rest or after mitogenic or functional activation. We show here, by using cell sorting, PCR, and Western analyses that A-myb is most highly expressed in the subsets of human tonsillar B lymphocytes with the phenotypes CD38+, CD39-, and SIgM-. The preferential expression of A-myb in these populations was seen at both the RNA and protein levels. CD38 was consistently best at separating high from low A-myb-expressing cells, whereas other markers (CD10, 22, 23, 77, 11a, and 49d) did not correlate with A-myb expression. The CD38+ population expressing the highest levels of A-myb was shown to contain mostly cycling cells inasmuch as more than 95% were in the late G1, S, G2, and M phases of the cell cycle. In addition, A-myb expression always correlated with the percentage of cells in S/G2/M in the populations sorted with either CD38, CD39, or sIgM. Small resting tonsillar B lymphocytes induced to proliferate in vitro by several different polyclonal B cell activators did not, however, express detectable levels of A-myb, although these cells were demonstrated to express CD38 and enter the S/G2/M phases of the cell cycle. These data suggest that A-myb is a marker of in vivo-activated but not in vitro-activated B lymphocytes. Finally, A-myb was also found to be highly expressed in five of seven Burkitt's lymphoma lines and in none of three EBV lymphoblastoid cell lines. This finding is in agreement with the phenotype of the normal B cells that express high levels of A-myb in vivo and suggests that A-myb may be specifically induced within germinal center B cells.

Topics: Adenosine Triphosphatases; ADP-ribosyl Cyclase; ADP-ribosyl Cyclase 1; Antigens, CD; Antigens, Differentiation; Apyrase; B-Lymphocytes; Base Sequence; Burkitt Lymphoma; Cell Cycle; Gene Expression; Humans; Immunoglobulin M; Lymphocyte Activation; Membrane Glycoproteins; Molecular Sequence Data; Oncogenes; Palatine Tonsil; Proto-Oncogene Mas; Proto-Oncogene Proteins; Receptors, Antigen, B-Cell; RNA, Messenger

A human monoclonal IgM antibody, referred to as TU223, has been produced. The reactivity of TU223 was tested in various cells and cell lines by complement-dependent microcytotoxicity test and fluorescence-activated cell sorter analysis. The antigen defined by TU223 was expressed on Epstein-Barr virus-transformed B-cell lines and on some Burkitt's lymphoma cell lines, but was not expressed on normal T cells, B cells or erythrocytes. In addition, expression of the antigen defined by TU223 was also induced on B cells activated by Epstein-Barr virus or pokeweed mitogen, and on T cells activated by phytohemagglutinin, concanavalin A, pokeweed mitogen or recombinant interleukin-2. However, no expression of the antigen detected by TU223 was induced at all on recombinant interleukin-4-treated B cells or macrophage-like cell line U937. When the ability of TU223 and various mouse monoclonal antibodies to bind to human differentiation antigens was compared, interestingly, the reactivity of TU223 was found to be very similar to that of mouse monoclonal antibody CD23 (H107), which reacts with Fc epsilon receptor II. Two-color analysis revealed that the antigen defined by TU223 is expressed on the cell surface of certain lymphoid cells expressing CD23 antigen. However, it can be concluded that the antigen defined by TU223 is clearly distinct from Fc epsilon receptor II, based on assay of cross-blocking between H107 and TU223. The surface antigen on B85 cells recognized by TU2232 had the molecular size of 80-82 kiloDaltons as determined by immunoblotting analysis.(ABSTRACT TRUNCATED AT 250 WORDS)

Topics: Adenosine Triphosphatases; Animals; Antibodies, Monoclonal; Antibody Specificity; Antigens, CD; Apyrase; B-Lymphocytes; Burkitt Lymphoma; Cell Line, Transformed; Cytotoxicity Tests, Immunologic; Flow Cytometry; Herpesvirus 4, Human; Humans; Immunoglobulin M; Interleukins; Lymphocyte Activation; Mice; Mitogens; Recombinant Proteins; T-Lymphocytes; Tumor Cells, Cultured

We demonstrate a differential platelet in vitro proaggregating activity in three Burkitt's lymphoma--derived human B cell lines, i.e. Daudi, Raji and P3H-R1. Functional and ultrastructural findings indicated the ability of Daudi cells to induce a marked secondary irreversible platelet aggregation, while the Raji cells only induced a primary-type reversible platelet response; no evidence of proaggregating activity has been obtained for P3H-R1 cells. Luminometric assays indicated that contact of Daudi and Raji, but not P3H-R1, cells with platelet rich plasma (PRP) or platelet poor plasma (PPP) was followed by ADP release, in the range of 2,2-3,5 microM and 0.4-0.6 microM respectively for Daudi and Raji cells. After preincubation of PRP with apyrase Daudi cells induced a reversible platelet response similar to that obtained with the use of Raji cells: then, the irreversible complete platelet response induced by Daudi cells was to be related to ADP release from degranulating platelets. Experiments in gel-filtered platelet systems showed that the plasma co-factor inducing ADP release from Daudi and Raji cells was not fibrinogen. Specific inhibition of platelet thrombin receptors, as well as of cycloxygenase and lipoxygenase pathways, did not modify the proaggregating activity of Daudi and Raji cells. Work is in progress to characterize the plasma factor interacting with Daudi and Raji, but not P3H-R1 cells, and the differences between the three cell lines which support this differential interaction.

Topics: Adenine Nucleotides; Amino Acid Sequence; Apyrase; Burkitt Lymphoma; Cell Communication; Humans; Microscopy, Electron; Molecular Sequence Data; Platelet Aggregation; Sonication; Thrombin; Tumor Cells, Cultured