Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0023418 (leukemia)
 93,477 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The radiological features of small intestinal lymphoma are described in 11 patients examined using the small bowel enema technique. The signs include luminal narrowing with mucosal destruction and occasionally shouldering of the margins and stricture formation, broad based ulceration, cavitation, non-specific thickening of the valvulae conniventes, discrete intraluminal filling defects, and a mass. In one patient, small nodules were scattered throughout the small intestine. Aneurysmal dilatation of a segment of intestine was seen in one case and an extraluminal mesenteric mass in another. A combination of different signs was a frequent finding and multiple intestinal lesions were present in four cases. Predisposing factors were present in five cases including coeliac disease, chronic lymphatic leukaemia, immunoproliferative small intestinal (alpha-chain) disease and previous extraintestinal lymphoma. In another patient there was evidence of extraintestinal lymphoma at the time of presentation.
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PMID:Lymphoma of the small intestine: radiological appearances. 324 56

A monoclonal antibody-secreting hybridoma cell line, VCD-1, was derived from the fusion of murine myeloma cells with splenocytes from a BALB/c mouse that had been immunised with chronic B-lymphocytic leukaemia cells. The cells came from a patient who had developed the leukaemia approximately 10 years after a course of radiotherapy for nodular sclerosing Hodgkin's disease. The antibody bound to a 30,000-dalton protein that was present in normal and malignant B cells, in monocytes, neutrophils, and interdigitating reticulum cells, and in malignant cells present in Hodgkin's disease lymph nodes. The reactive epitope was not accessible to antibody in viable intact cells; binding to peripheral blood cells could only be seen if the cells were fixed. The antibody recognises a determinant that probably resides on the alpha-chain of HLA class II molecules.
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PMID:A monoclonal antibody to an antigen present in cells from a patient with Hodgkin's disease. 331 34

Cell lines established from T-cell leukemias have recently been reported to exhibit a chromosome translocation t(8;14) involving proto-oncogene c-myc and the gene of the T-cell receptor alpha-chain(TcR-alpha). In this work, we have studied a case of T-cell leukemia presenting a t(8;14)(q24;q11) translocation that was found in fresh leukemic cells taken during relapse, but was absent in cells collected at diagnosis. Hybridization analysis showed that the breakpoint on chromosome 8 was located 3' to the c-myc exon 3. A TcR-alpha-specific original probe (D14S7, Mathieu-Mahul et al., 1985) revealed two differently rearranged patterns in DNA from leukemic cells obtained at diagnosis and during relapse. In contrast, the rearranged TcR-beta-gene DNA pattern did not change during the course of the disease, indicating that leukemic cells were clonally related. These data indicate that the chromosome breakpoint in 14q11 is situated in the TcR-alpha locus. These results suggest that translocations t(8;14) involving TcR-alpha and c-myc genes in T-cell malignancies are analogous to variant t(2;8) and t(8;22) translocations observed in Burkitt lymphoma. They also establish that the same types of molecular rearrangements due to a t(8;14)(q24;q11) translocation, at first described in T-cell lines established in culture, also exist in vivo and may play a role in the evolution of the leukemic process.
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PMID:A t(8;14)(q24;q11) translocation in a T-cell leukemia (L1-ALL) with c-myc and TcR-alpha chain locus rearrangements. 346 70

The antigen receptor expressed on most T lymphocytes is a disulphide-linked heterodimer (Ti) that is composed of alpha-chain and beta-chain subunits. On the surface of human T lymphocytes, Ti is non-covalently associated with three invariant proteins, designated CD3-gamma, -delta, and -epsilon. It has been suggested that Ti is obligatory for CD3 expression. But a T leukaemia cell line, IL-2 (interleukin 2) dependent T-cell clones established from fetal blood and IL-2 dependent cell lines established from immunodeficiency patients with bare lymphocyte syndrome and ectodermal dysplasia syndrome have recently been shown to express CD3, but not Ti (detected due to monoclonal antibody WT31). These lymphocytes may express the product of the T-cell antigen receptor gamma (TCR-gamma) gene, rather than the alpha/beta heterodimer, in association with CD3. Preliminary studies suggested that T cells expressing CD3 but lacking Ti are present in low frequency in normal lymphoid tissues. Here we show that in normal blood and thymus CD3+, WT31-T cells express neither CD4 nor CD8. The low frequency (less than 0.2-0.9% of total thymocytes) of CD3+, WT31- cells in the thymus suggests that this population does not represent a major stage of thymic development and may be a distinct lineage of T cells.
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PMID:Presence of Ti (WT31) negative T lymphocytes in normal blood and thymus. 349 23

Similar to the immunoglobulin (Ig) gene rearrangements in B-lineage cells, identification of T-cell receptor (TCR) gene rearrangements is a novel clonal marker and necessary to establish a T-cell lineage. The function of T-cell gamma-chain (T gamma) gene is still unknown, but because of its shared properties with T-cell alpha-chain (T alpha) and T beta genes, we analysed T gamma gene organization in 10 patients with T-lineage leukemia/lymphoma as well as in non-T lineage leukemias. All 10 cases of T-lineage leukemia/lymphoma, whose phenotypes were different, demonstrated T gamma gene rearrangements as well as T beta gene rearrangements. In contrast, among the non-T-lineage leukemias, the emergence of T beta and/or T gamma gene rearrangements was varied. Based on these findings, concomitant rearrangements of T beta and T gamma genes are characteristic in childhood T-lineage leukemia/lymphoma regardless of their phenotypic differences. Furthermore, no obvious developmental hierarchy was observed between T beta and T gamma gene arrangements in these leukemia/lymphoma cells.
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PMID:Concomitant rearrangements of T-cell beta- and gamma-chain genes in childhood T-lineage leukemia/lymphoma. 349 98

Chromosomal rearrangements in malignant T-cell disease frequently involve the chromosome bands containing the T-cell receptor genes. The RPMI 8402 cell line, which was established from the leukemia cells of a patient with T-cell acute lymphoblastic leukemia, is characterized by a translocation involving chromosome 14 (band q11) and chromosome 11 (band p15) [t(11;14)(p15;q11)]. By using in situ chromosomal hybridization and Southern blot analysis to examine RPMI 8402 cells, we determined that the break at 14q11 occurs within the variable region sequences of the T-cell receptor alpha-chain gene (TCRA); the break at 11p15 occurs between the HRAS1 gene and the genes for insulin and the insulin-like growth factor 2. These results suggest that the TCRA sequences activate a cellular gene located at 11p15 in malignant T-cell disorders.
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PMID:T-cell receptor alpha-chain gene is split in a human T-cell leukemia cell line with a t(11;14)(p15;q11). 354 Sep 49

We studied the effect of polyethylene glycol (PEG) on the solubility of the receptor for immunoglobulin E (IgE) in non-ionic detergent extracts of rat basophilic leukemia (RBL) cells. We found that the precipitation patterns of free and IgE-bound receptor were identical but differed from that of unbound IgE. Thus, 85 to 95% of the free receptor and the IgE-receptor complexes precipitated at 13% PEG in the presence of 0.5% Nonidet P-40, whereas 95% of the unbound IgE remained soluble. A similar degree of differentiation between the precipitation of receptor-bound and unbound IgE was found when we used extracts and PEG solutions prepared with several non-ionic and/or neutral detergents. The intact IgE-receptor complex with the full complement of subunits (alpha, beta, gamma) precipitated more efficiently than the IgE-alpha-chain-complex. The presence of phospholipids, which were previously shown to be important for preservation of the association between the receptor subunits, enhanced the efficiency of precipitation of the IgE-receptor complex. The presence of PEG also had an effect on the solubility of cellular phospholipids and some of the detergents, although the effect of PEG on either could not be directly related to its effect on the solubility of the IgE-receptor complex. The radioiodinated receptor for IgE, much like other radioiodinated RBL cell membrane proteins, was soluble (greater than or equal to 95%) at approximately 7% PEG but could be specifically and efficiently precipitated from crude cell extracts, in the presence of 7% PEG upon the addition of anti-receptor immunoglobulins alone. Using mouse anti-dinitrophenyl IgE antibody, we found that unlike unbound antigen (DNP-BGG) or the IgE-receptor complex, the detergent-solubilized DNP-BGG-IgE-receptor complex was insoluble at 7% PEG. Consequently, PEG can be employed in assays to quantitate the soluble receptor, and to immunoprecipitate it specifically and directly. Moreover, the use of PEG can facilitate the distinction between unbound antigen and antigen-IgE-receptor complex as well as between the latter and IgE-receptor complex.
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PMID:The behavior of the solubilized receptor for immunoglobulin E in polyethylene glycol-detergent solutions: characterization and potential applications. 620 83

Although the receptor with which T cells bind specific antigen can, like immunoglobulin, distinguish between antigens which differ only slightly in structure, it is unique in recognizing antigen only in conjunction with one of the self proteins of the major histocompatibility complex (MHC restriction). The receptor was identified and characterized in mouse and man by using monoclonal antibodies to receptor idiotypes, and consists of two disulphide-linked polypeptides, and acidic alpha-chain and a neutral to slightly basic beta-chain. Peptide maps have shown that, like immunoglobulin, both chains vary for receptors of different specificities. T-cell-derived cDNA clones have recently been identified in mouse and man encoding immunoglobulin-like molecules. These were identified as derived from beta-chain genes through a partial N-terminal protein sequence of the beta-chain isolated from a human T-cell tumour. We have now purified the alpha- and beta-chains of the receptor of the human T-cell leukaemia line HPB-MLT, and have determined the amino acid sequence of several tryptic peptides derived from each chain. Our results further confirm that the previously reported cDNA clones encode beta-chains. The sequence of the alpha-chain peptides identify this as another immunoglobulin-like polypeptide chain. Particularly striking was an alpha-chain peptide with high homology to the conserved portion of the immunoglobulin J segment and T-cell receptor beta-chains. Surprisingly, the alpha-chain peptides show little similarity to the sequence predicted by two overlapping putative murine alpha-chain cDNA clones.
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PMID:Immunoglobulin-like nature of the alpha-chain of a human T-cell antigen/MHC receptor. 633 42

The T-cell receptor has been studied intensely over the past 10 years in an effort to understand the molecular basis for major histocompatibility complex (MHC) restricted antigen recognition. The use of anti-receptor monoclonal antibodies to isolate and characterize the receptor from human and murine T-cell clones has shown that the protein consists of two disulphide-linked glycopeptides, alpha and beta, distinct from known immunoglobulin light and heavy chains. Like immunoglobulin light and heavy chains, however, both the alpha- and beta-chains are composed of variable and constant regions. Molecular cloning has revealed that the beta-chain is evolutionarily related to immunoglobulins, and is encoded in separate V (variable), D (diversity), J (joining) and C (constant) segments that are rearranged in T cells to produce a functional gene. We report here cDNA clones encoding the alpha-chain of the receptor of the human T-cell leukaemia line HPB-MLT. Using these cDNA probes, we find that expression of alpha-chain mRNA and rearrangement of an alpha-chain V-gene segment occur only in T cells. The protein sequence predicted by these cDNAs is homologous to T-cell receptor beta-chains and to immunoglobulin heavy and light chains, particularly in the V and J segments.
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PMID:Primary structure of human T-cell receptor alpha-chain. 644 30

Mutagenesis of a region of human interleukin (IL)-6 which is important for triggering signal transduction via the IL-6 receptor beta-chain (gp130) has lead to the isolation of a variant of human IL-6 (IL-6.Q160E/T163P), which could antagonize the biological activity of wild type IL-6 on the human EBV transformed B cell line CESS and the human hepatoma cell line HepG2. Surprisingly this antagonistic IL-6 variant had an agonistic effect on the human myeloma cell line XG-1, albeit at a 1000-fold higher concentration than wild type IL-6. This residual activity of the mutant arose from triggering gp130, because it could be inhibited by a gp130 specific mAb. Extensive mutagenesis of residues between Q153 and H165 of human IL-6, a region which is partly homologous in cytokines which also signal via gp130 (oncostatin M, ciliary neurotrophic factor, leukaemia inhibitory factor, IL-11), did result in the isolation of a second antagonist for IL-6 activity on CESS and HepG2 cells. However on XG-1 cells this variant was active as well. These results suggest that (an) additional region(s) of the IL-6 molecule might be involved in gp130 triggering. Recently we indeed found that residues Lys42-Ala57 are also important for gp130 triggering. Inhibition experiments with neutralizing IL-6R alpha-chain specific mAb show that this region can be functionally separated from the Q153-H165 region. These findings have important implications for the development of receptor antagonists of IL-6 and IL-6 family members.
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PMID:Functional distinction of two regions of human interleukin 6 important for signal transduction via gp130. 757 77


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