Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0019829 (Hodgkin's disease)
 30,247 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Studies with interference contrast microscopy reveal that platelets undergo a typical shape change within 30--60' after venepuncture, i.e. swelling, formation of large tentacles, tiny protrusions and vesicles at the platelet surface. This "shape change" can be observed in citrated blood and PRP, heparinized blood and EDTA-blood as well. It is enhanced by low incubation temperatures (4 degrees C, 10 degrees C) and delayed at 37 degrees C as compared with room temperature. An increased number of primarily shape changed platelets is found if platelets are strongly mechanically irritated at blood sampling. The shape change is partly reversible in vitro, it is completely or almost completely reversible in vivo. Some antiaggregating agents inhibit the in vitro shape change at varying degrees (Bencyclan, SH 869 greater than ASA greater than D-Propranolol). The shape change is partly inhibited after oral or i.v. administration of ASA. A typical transformation of platelets into "spheric" forms can be observed following the addition of Bencyclan, SH 869 and D-Propranolol to PRP in vitro. The spontaneous "primary shape change" which occurs in PRP or blood after blood sampling is probably different from the secondary ADP-induced shape change. The primary shape change may influence the results of different platelet function and aggregating tests. The shape change kinetics of "healthy" subjects and patients with Hodgkin's disease differ significantly. The described method may gain more clinical interest in the future.
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PMID:[Primary shape change of platelets in vitro (author's transl)]. 72 25

Immunohistochemistry was performed on paraffin sections of 169 bone marrow biopsies fixed in a buffered methanol-formalin solution and decalcified with EDTA. The biopsies included specimens with normal hematopoiesis, and specimens that were affected by various hematological disorders as well as some metastatic carcinomas. The results demonstrate that a wide spectrum of antigens was preserved in routinely processed bone marrow biopsies, even after long-term fixation up to 12 days. Markers for granulopoietic cells were lysozyme, elastase, DAKO-M 1, and MT 1. Megakaryopoiesis was stained with glycoprotein IIIa, von Willebrand factor, and Ulex europaeus agglutinin (UEA), and erythropoiesis with LN 1. Normal lymphocytes as well as lymphoma cells of all non-Hodgkin's lymphomas tested were positive for leukocyte common antigen (LCA), and at variable degree, for MB 1, 4 KB 5, LN 1, LN 2, UCHL 1, or MT 1. Reed-Sternberg and Hodgkin's cells in Hodgkin's lymphomas were reactive with Ber-H 2, LN 2 and Dako-M 1. In plasma cell disorders, staining for immunoglobulin light chains gave best results. Metastatic carcinomas showed predominantly staining with EMA, and KL 1. A selected panel of specific cell markers is proposed, which proved to be helpful in routine bone marrow diagnosis in most cases.
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PMID:Immunohistochemical examination of routinely processed bone marrow biopsies. 143 32

The properties of rosettes formed between the Hodgkin's cell lines, L428 and L591, and allogeneic peripheral blood mononuclear cell populations have been investigated. Immunocytochemical analysis showed that the majority of adherent cells were T-cells of both the CD4 and CD8 subsets. Only relatively few B-cells and monocytes were seen to adhere. However, when peripheral blood mononuclear cell populations were fractionated, it was found that monocytes were as good as T-cells at forming rosettes with both L428 and L591, though B-cells were shown to be poor at forming such associations. Treatment of both L428 and L591 with neuraminidase resulted in a significant reduction (P less than 0.01) in the mean number of adherent lymphocytes and in the numbers of Hodgkin's tumour cells which formed rosettes. Smaller, less significant effects were observed for Cytochalasin B and trypsin. EDTA (10(-2) M) at pH 7.2 had no significant effect on rosetting for L428 or L591. Adherence of allogeneic lymphocytes to L428 or L591 was pH dependent but did not appear to correlate with cell surface charge. Treatment of L428 cells with Fab fragments prepared from the IgG fraction of a hyperimmune rabbit anti-L428 antiserum, significantly (P less than 0.05) inhibited the adherence of allogeneic lymphocytes, but only when used at high concentration. The binding requirements of the Hodgkin's cell lines with allogeneic peripheral blood lymphocytes, as described in this study, appear to be quite different from those described for freshly isolated Hodgkin's tumour cells with autologous intratumoral lymphocytes. This suggests that the two phenomena may be unrelated. There would appear to be an absolute requirement for cell surface sialic acid for allogeneic lymphocyte attachment to the HD cell lines. This might suggest that the receptor-ligand system involved contains sialic acid as an integral part of the cell surface receptor structure involved in recognition of the appropriate ligand.
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PMID:The Reed-Sternberg cell/lymphocyte rosette. I. Properties of rosettes formed between Hodgkin's cell lines and allogeneic lymphocytes. 249 15

Fibronectin was detected by immunofluorescence on the surface of one fraction of separated normal peripheral blood lymphocytes using FITC-conjugated anti-human fibronectin antibodies. Approximately one fifth of isolated B cells and 7% of O cells contained surface bound fibronectin but T cells failed to stain. There were no detectable free receptors for fibronectin on the surfaces of the lymphocytes in the different subsets isolated from healthy controls as studied using FITC-labelled purified fibronectin. The per cent of B and O cells bearing surface bound fibronectin was markedly decreased in patients with acute and chronic lymphocytic leukemias and non Hodgkin's lymphoma, only 1-4% of B and 1-2% of O cells stained with FITC-labelled antifibronectin immunoglobulins. FITC-conjugated fibronectin was not bound to the different lymphoblasts isolated from patients with leukemia and lymphoma. Treatment of cells with trypsin and EDTA removed fibronectin bound to the cell surfaces. Fibronectin attached to the surfaces of lymphocytes may have an immunoregulatory function.
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PMID:Cell surface fibronectin on peripheral blood lymphocytes in normal individuals and in patients with acute and chronic lymphocytic leukemia and non Hodgkin's lymphoma. 389 Apr 99

Kinetics of slow current carried by sodium ions through the potential-dependent calcium channels provided that EDTA is introduced into Ca-free external solution was studied in experiments on isolated internally dialyzed neurons of the mollusc Helix pomatia. Activation kinetics of this current was similar to that of initial calcium current. It can be described using the square power of the activation variable m in the Hodgkin-Huxley equations. Kinetics of decay (inactivation) of the induced sodium current is biexponential during prolonged depolarization of the membrane. On this basis it is suggested that the decay of the sodium current results from two independent processes: voltage-dependent inactivation to some steady-state level hoo with time constant tauh approximately 1 s and a decrease of the current due to accumulation of Na+ ions inside the cell and, consequently, to a change in electrochemical potential for Na+ ions (tau c approximately 10 s). It is concluded that modification of calcium channels resulting in ability for passing sodium ions does not affect gating mechanisms which open or close the channels.
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PMID:[Kinetics of through EDTA-modified calcium channels of the somatic membrane of mollusk neurons]. 631 78

Immune complexes (IC) present in sera from patients with Hodgkin's disease (HD) were isolated using three different affinity columns: C1q-degalan, anti-C1q sepharose and conglutinin (K)-degalan. The isolated IC were analysed by immunoprecipitation, SDS-PAGE and sucrose density gradients and compared with IC similarly isolated from patients with rheumatoid arthritis (RA), systemic lupus erythematosus (SLE) and in vitro prepared BSA-anti-BSA complexes. Isolated material from each disease, and BSA-anti-BSA complexes contained proteins compatible with true immune complexes--IgM, IgG, C1q and C3 breakdown components. Albumin, fibronectin and CRP, whose affinity for IgM, C1q and C3 are known, were co-isolated along with IC material. The size of isolated IC in HD ranged from 8-40S on sucrose density gradients. Despite the operational difference in detecting and isolating HD complexes via the C1q ligand (C1q-degalan or anti-C1q column) and C3bi (K-degalan), material purified by both methods showed remarkable similarity on SDS-PAGE and immunoprecipitation analysis. Although IC isolated from different diseases showed disparate banding patterns on SDS-PAGE this was attributed to a variation in the relative concentrations of constituent proteins--IgM, IgG and C3 breakdown products. IgM, IgG and C3 bind loosely, and non-specifically, to macromolecular aggregates formed around immune complexes. Using the anti-C1q column, most of this material could be eluted using 0.02M EDTA. Least protein, yet the most specific for antigen and antibody was eluted at pH 3.0.
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PMID:Immune complexes in Hodgkin's disease: isolation, immunochemical and physico-chemical analysis. 641 1

The activation marker CD30 is expressed on the cell surface of the malignant cells in Hodgkin's disease and a few non-Hodgkin lymphomas. We have analyzed the regulation of membrane-bound CD30 and found that the binding of a variety of anti-CD30 antibodies induced down-regulation of CD30 on cell lines. In addition, such down-modulation was also observed after treatment of the cell surface proteins with the sulfhydryl reagent iodoacetamide or after stimulation of the second messenger pathway with phorbol ester or calcium ionophore. This modulation was abolished at 4 degrees C and strongly inhibited by chelators like EDTA or 1,10-phenanthroline, whereas EGTA, a selective inhibitor of Ca(2+)-dependent proteinases and other inhibitors of serine, thiol and acid proteinases, showed no effect. The down-modulation was strengthened by Zn2+ or Cd2+, but not by other divalent cations such as Fe2+, Mn2+, Mg2+, Ca2+ or Co2+, thus indicating the involvement of a zinc metalloproteinase in CD30 modulation which can be activated by protein kinase C and by alkylation of sulfhydryl groups. Pulse-chase experiments, analysis of the CD30 glycosylation and specific measurement of the 90-kDa soluble form of CD30 (sCD30) with a sandwich radioimmunoassay revealed that CD30 down-modulation results from enhanced release of 90-kDa sCD30 by the site-specific cleavage of CD30 accomplished by a zinc metalloproteinase. This release occurs at the cell membrane without prior endocytosis.
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PMID:A zinc metalloproteinase is responsible for the release of CD30 on human tumor cell lines. 759 Dec 96

The incidence of malignancies in recipients of renal transplants was compared to that in non-grafted patients on maintenance dialysis as reported to the EDTA-ERA Registry and in the general population as recorded by the cancer registries of England and Wales, of Sweden, of the (former) German Democratic Republic, and of Lombardy and Varese in Northern Italy. For tumours known to be associated with immunosuppression, namely Kaposi's sarcoma, non-Hodgkin lymphoma and the common malignancies of the skin (except melanoma), an increased incidence was confirmed for the transplanted population. Thyroid carcinoma and hepatoma were found to be more frequent in non-grafted patients on dialysis as well as after renal transplantation. An increased incidence of cancer of the cervix and of the body of the uterus was recorded only for young cohorts with a functioning graft but not for women after menopause. Most of the other malignancies had similar incidences in grafted and non-grafted populations which did not differ from those in the general populations of the cancer registries except cancer of the colon which was slightly more frequent, particularly at 10-20 years after the first transplant operation. Survival after diagnosis of cancer at the most frequent sites, such as bronchopulmonary, breast, oesophagogastric and colorectal cancer, did not differ between non-grafted patient groups on dialysis and those who developed the tumour while carrying a functioning renal transplant.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Malignancies after renal transplantation: the EDTA-ERA registry experience. European Dialysis and Transplantation Association-European Renal Association. 761 85

The human BCL-6 gene, which is rearranged in approximately 30% of diffuse large B cell lymphomas, encodes a 706-amino-acid nuclear protein of the Kruppel-type zinc finger transcription factors mainly expressed in normal germinal center B cells and related lymphomas. Four monoclonal antibodies (PG-B6, PG-B6a, PG-B6p, and PG-B6m), specifically directed against the human BCL-6 protein, were generated by immunizing BALB/c mice with a recombinant protein corresponding to the BCL-6 amino-terminal region (amino acids 3 to 484). The PG-B6 monoclonal antibody reacted with a BCL-6 epitope sensitive to fixatives and preserved in all mammalian species. PG-B6a (a is for avian) recognized the most evolutionarily conserved BCL-6 epitope (expressed in all animal species including avian). PG-B6p (p is for paraffin) recognized a fixative-resistant epitope of BCL-6 that was detectable on paraffin sections after microwave heating in 1 mmol/L EDTA buffer. PG-B6m (m is for mantle) was the least specific monoclonal antibody as, in addition to BCL-6, it reacted with a yet undefined antigen selectively located in the cytoplasm of mantle and marginal zone B cells. All monoclonal antibodies detected strong nuclear expression of BCL-6 in follicular lymphomas, diffuse large B cell lymphomas, Burkitt's lymphomas, and nodular, lymphocyte-predominance Hodgkin's disease. In diffuse large B cell lymphomas, BCL-6 expression was independent of BCL-6 gene rearrangements and did not correlate with expression of other markers or the proliferation index. BCL-6 was not expressed in B-CLL, hairy cell leukemia, mantle-cell- and marginal-zone-derived lymphomas. Labeling of paraffin sections with PG-B6p proved useful for differentiating proliferation centers in B-CLL (BCl-2+/BCL-6-) from trapped germinal centers in mantle cell lymphomas (BCL-2-/BCL-6+) and for identifying neoplastic cells in cases of nodular, lymphocyte-predominance Hodgkin's disease. Because of their high specificity, wide reactivity in humans and animal species including avians (PG-B6a), and suitability for labeling routine paraffin sections (PG-B6p), the reagents described in this paper should prove valuable in both research and diagnostics.
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PMID:Monoclonal antibodies PG-B6a and PG-B6p recognize, respectively, a highly conserved and a formol-resistant epitope on the human BCL-6 protein amino-terminal region. 862 23

Storage-related differences in C3 level of blood complement and its hydrolized form--C3(H2O)--were identified in Hodgkin's disease patients and healthy donors, by immunoenzymatic analysis using murine monoclonal antibodies. Both C3 and C3(H2O) levels in blood serum of patients varied with time and were significantly different from those in health subjects; they correlated with EDTA concentration. After a second thawing of plasma in patients, there were no traces left of C3(H2O).
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PMID:[Conformational changes in C3 levels of complement during storage of blood from Hodgkin's disease patients and from healthy people]. 1078 25


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