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 expression of six different membrane markers by cells of the human B lymphocyte lineage has been studied, using monoclonal antibodies. B cells representing various stages of differentiation/maturation have been examined, using normal cells, leukaemia cells, and continuous cell lines. The expression of the six markers has been compared with maturation stages defined by immunoglobulin expression. The HLA/beta 2-microglobulin complex is present throughout the B cell lineage, whilst the Ia (p28,33) marker is present from the earliest stage that can be attributed to the B lineage, but is lost during plasma cell differentiation. A marker detected by monoclonal antibody FMC 1 is present only on mature B lymphocytes, being absent from pre-B cells or plasma cells. FMC 7 detects an antigen found on a relatively mature subpopulation, whereas FMC 8 detects early as well as mature B cells. FMC 3 expression is found on a proportion of cells at any maturation stage, suggesting that expression of this marker is controlled by factors unrelated to maturation.
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PMID:Maturation of human B lymphocytes--studies with a panel of monoclonal antibodies against membrane antigens. 619 92

Mouse monoclonal antibodies, GIN-2, -7 and -14, against adult T-cell leukemia virus (ATLV) were prepared by a hybridoma procedure. These antibodies belonged to different subclasses of IgG, but they reacted similarly with both ATLV-specific polypeptides p19 and p28. In the reaction with monoclonal antibodies and various ATLV-producer cell lines, it was found that MT-2 and MT-2-related T-cell lines produced both p19 and p28, whereas MT-2-unrelated cell lines produced p19, but not p28.
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PMID:Monoclonal antibody reactive with both p28 and p19 of adult T-cell leukemia virus-specific polypeptides. 619 27

Human breast cyst fluids were shown to contain low concentrations of IgA (15-78 micrograms/ml) and IgG (33-145 micrograms/ml). The IgA:IgG ratios in individual breast cyst fluids ranged from 1:0.6 to 1:4. These levels are considerably higher than their ratio in serum (1:7). IgA from 33% of the 40 fluids examined, and IgG from 10% of the fluids, reacted with the murine mammary tumor virus (MuMTV). The reactivity was detected by an enzyme-linked immunosorbent assay that measures antibody binding to both the envelope glycoprotein and core protein of the virus. In a second series of experiments. IgA from 28% of 40 breast cyst fluids reacted only with MuMTV while IgA from 30% of the fluids was reactive with both MuMTV and the Rauscher murine leukemia virus. Antigen reactive with antiserum to the 28,000-dalton MuMTV core protein (p28), was also identified in a 165,000-g pellet fraction from breast cyst fluids. In individual fluids, the extent of IgA binding to MuMTV was positively correlated (P less than or equal to 0.01) with the binding of anti-p28 antibody to the pellet of the breast cyst fluid. Fractions with the buoyant density of retroviruses (1.16-1.18 g/ml) or their cores (1.21-1.25 g/ml) were isolated from breast cyst fluids. These fractions contained a DNA polymerase capable of utilizing the reverse transcriptase-specific template, dG12-18 x poly rCm. In addition, they reacted with antiserum to MuMTV p 28 but not with antiserum to the 30,000-dalton Rauscher murine leukemia virus core protein.
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PMID:Antigens and antibodies cross-reactive to the murine mammary tumor virus in human breast cyst fluids. 625 13

Sera from normal mice and mice bearing murine mammary tumor virus (MTV)-induced tumors showed cytotoxic reactions to the MTV-producing Mm5mt/c1 cell line. The reaction could be blocked by the addition of MTV, but not of purified gp52 and p28. In sera from tumor bearers, cytotoxic responses ranged from 15 to 66%; reactivity was generally highest when the serum was diluted 32 to 128 times. The cytotoxic sera from the normal animals showed a much lower activity; again, there was a lack of cytotoxic response at lower serum dilutions. Low dilutions (1 to 64) of sera from tumor-bearing and normal mice were found to inhibit the MTV-specific cytotoxic activity of rabbit anti-MTV serum on the Mm5mt/c1 cell line. Specificity of this phenomenon was deduced from the fact that there was less inhibition by the mouse sera of anti-Rauscher leukemia virus-specific cytotoxic activity to Rauscher leukemia virus-infected cells and of anti-vaccinia virus serum to vaccinia virus-infected cells. Absorption of the mouse sera with rabbit anti-gp52 serum almost completely abolished the inhibition; after absorption with MTV, inhibition was somewhat reduced. The effect of free gp52 and MTV/anti-MTV immune complexes on the anti-MTV immune response is discussed.
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PMID:Virus-specific cytotoxic activity to mammary tumor cells of sera from normal and tumor-bearing mice with inhibition at low dilutions. 626 Jun 79

The intracellular precursor polyproteins of simian sarcoma-simian-associated virus [SiSV(SiAV)] were compared to the intracellular proteins of the human retrovirus isolates. HL23V, HEL12V and A1476V, by radioimmunoprecipitation followed by SDS-polyacrylamide gel electrophoresis and tryptic peptide analysis. Cells infected with SiSV(SiAV) were characterized by polyproteins Pr200gag-pol, gPr80env, Pr80gag, Pr60gag and Pr40gag. Identical intracellular precursor polyprotein profiles were obtained from cells infected with HL23V, HEL12V and A1476V. Tryptic digest mapping of peptides containing [3H]leucine showed the structural composition of Pr60gag to be the virus core proteins, p28, p15/p12 and p10. The SiSV(SiAV) envelope precursor, gPr80env, contained the structural determinants of mature viral gp70 and a non-glycosylated protein termed p15E. The homology of the human isolate viruses, HL23V, HEL12V and A1476V, to the SiSV(SiAV)/GaLV (gibbon ape leukaemia virus) family of viruses was confirmed by mapping studies. Both gPr80env and Pr60gag of SiAV were identical by tryptic peptide mapping to the respective proteins from the three human retrovirus isolates examined. The potential significance of these results to considerations of the origins of SiAV and the SiAV-like human isolates is discussed.
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PMID:A comparison of the intracellular precursor polyproteins of simian sarcoma-associated virus [SiSV(SiAV)] and three human virus isolates: HL23V, HEL12V and A1476V. 629 May 96

The adult T-cell leukemia (ATL)-associated antigen complex (ATLA) is recognized by serum antibodies of carriers of ATL virus (ATLV). ATLA consists mainly of ATLV polypeptides and their precursors. The sera from 22 ATL patients, 21 healthy carriers and 9 healthy individuals were examined quantitatively by immunofluorescence assay (IF) for ATLA and by a newly developed radioimmunoprecipitation test with purified 125I-gp68, the putative env gene product of ATLV. More qualitative results were obtained by analysis on polyacrylamide gel (PAGE) of immunoprecipitates from lysates of 35S-cysteine-labelled cells producing ATLV, pelleted ATLV and cell-free culture supernatant. The two quantitative assays gave negative results with sera from all normal subjects and a few patients, but detected ATLA antibodies in all the healthy ATLV carriers. An important finding was that sera of patients that gave negative results in one assay gave positive results in the other, and vice versa. In contrast, all sera from ATL patients and healthy carriers, but not normal donors, precipitated ATLV-specific glycopolypeptides, gp68 and gp46 from 35S-labelled materials. But core polypeptides p28, p24, p19 and p15 were precipitated only by sera with IF titers of over 80. Thus, anti-ATLA antibodies in seropositive sera are predominantly directed against glycopolypeptides of ATLV, and the antibody reactivity to ATLA antigens does not differentiate between ATL patients at various stages of the disease and healthy ATLV carriers.
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PMID:Adult T-cell leukemia (ATL) virus-specific antibodies in ATL patients and healthy virus carriers. 660 32

We have identified previously a quantitatively minor membrane protein (p28) with an apparent reduced m.w. of 28,000, which is biosynthetically labeled in activated human lymphocytes. Rabbit antisera with activity directed against p28 (alpha-ATC) were prepared and p28 was identified by immunoprecipitation in NP-40 extracts of activated, extrinsically labeled lymphocytes. p28 was not expressed in appreciable amounts by unstimulated T cells, stimulated or unstimulated B cells, null cells, or adherent cells. Protein p28 was only minimally represented on resting thymocytes but was easily detected on 4-hr activated thymocytes and the T lymphoblastoid cell lines HSB2 and MOLT-4. Absorption and immunoprecipitation studies with alpha-ATC indicated that p28 was not present on erythrocytes, platelets, neutrophils, six B cell lines, six null cell lines, and seven other T lymphoblastoid cell lines. Protein p28 from HSB2 cells was absorbed by lentil lectin, concanavalin A, and wheat germ agglutinin affinity columns and was eluted with the appropriate sugars. Gel filtration column chromatography of unreduced p28 in the presence of 0.5% NP-40 or 0.1% deoxycholate gave elution characteristics consistent with a m.w. of approximately 60,000 to 100,000. In preparative isoelectric focusing (IEF) studies the isoelectric point (pI (p28) = 5.2 to 6.1) was similar or identical to that described for the reduced and denatured protein in two-dimensional polyacrylamide gels (pI = 5.5 to 6.2). Protein p28 was eluted from DEAE-cellulose (Whatman DE-52) ion exchange columns at 0.05 to 0.15 M NaCl. Experiments with monoclonal antibodies or heteroantisera specific for other T cell and B cell antigens and various lymphoblastoid cell lines and normal peripheral blood cells indicated that p28 is distinct from the human Ia-like antigens, from T3, T4, T5, T8, and from several other reported human T cell antigens that appear to correspond to Thy-1, the sheep erythrocyte receptor, and a human thymus-leukemia antigen.
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PMID:Properties of a surface antigen expressed on activated human thymus-derived lymphocytes. 680 Nov 23

Tumor-specific transplantation antigens unique to each of MM2, MM46 and Ehrlich mouse ascites tumor cells (cell line-specific antigens) were released from the cells into the medium during incubation in 0.12M saline at 37 degrees for 30 min. The released antigens were purified by identical procedures which consisted of ultracentrifugation, affinity chromatography using Sepharose 4B conjugated with Ricinus communis lectin, and DEAE-cellulose column chromatography. The recovery was about 700 micrograms (protein) from 100 g (wet weight) cells. The recovered materials induced specific immunity in C3H/He mice against transplantation of the corresponding tumor cells only when they were administered after treatment with the corresponding tumor-regressor C3H/He mouse serum. Single injection into the peritoneal cavity of 10 mcrograms of each of the pretreated materials inhibited transplantation of 5 x 10(3) corresponding tumor cells. Spleen cells from mice immunized by repeated injections of the pretreated antigen neutralized transplantability of the tumor cells. Specific humoral antibody was also detected. The specific antigens obtained from these cells were similar to each other with respect to sedimentation coefficient (16S), electrophoretic characteristics and xenogeneic antigenicity, and were free of beta-2 microglobulin, murine leukemia virus major structural proteins such as gp70 or p30 and murine mammary tumor virus proteins such as gp55 and p28.
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PMID:Purification of cell line-specific transplantation antigens from mouse ascites tumor cells. 711 55

An HTLV-I-associated case of adult T-cell leukemia (ATL) was described in a 51-year-old white man, native from Georgia, the former U.S.S.R. Clinical manifestation of the disease (enlarged lymph nodes, bone marrow and peripheral blood changes, CNS-involvement, cutaneous lesions and hypercalcemia) as well as laboratory findings were recognized to be very similar to those frequently observed in ATL patients from endemic regions. Mature T-helper surface phenotype detected on peripheral blood lymphocytes of the patient (OKT3-, OKT4+ and OKT8-) and aggressive course of the disease were also in favour of classical type ATL developed in the patient. The HTLV-I antibody presence in an ATL patient was repeatedly confirmed by serological tests (Abbott HTLV-I EIA and Serodia HTLV-I), immunofluorescence and Western blot assay. The latter revealed the presence of a large spectrum of HTLV-I-specific antibodies (to p19, p24, p26, p28, p32, p36, pr53, gp21, gp46, gp62 and gp68 of HTLV-1). The HTLV-I-specific antibodies have also been detected in serum samples of the patient's wife and son. The presence of HTLV-I provirus in the primary ATL patient's PBL was clearly demonstrated by PCR and Southern blot analysis. This case, with the HTLV-I infections detected in two other family members, suggests that in Europe, HTLV-I-positive cases of ATL can occur in virus-infected local people with much wider distribution than that hitherto supposed.
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PMID:Clinical, morphological and virological features of an HTLV-I-positive case of ATL in a white man from the Caucasus. 832 44

The AMV v-Myb oncoprotein causes oncogenic transformation of myelomonocytic cells in vivo and in vitro. Its transforming capacity is strictly dependent upon the N-terminal DNA binding domain, the central transactivation region, and on the C-terminal domain containing a putative leucine zipper motif. Here we show that the v-MybL3,4A mutant, in which Leu325 and Leu332 of the leucine zipper have been replaced by alanines, failed to induce leukemia in virus infected chicken. This demonstrates that the leucine zipper domain is indispensable for v-myb induced leukemogenesis in vivo. v-MybL3,4A was, however, still able to transform myelomonocytic cells from chicken bone marrow in vitro. Yet, while v-mybL3,4A transformed cells were impaired in growth at 37 degrees C, they failed to grow at 42 degrees C, the physiological body temperature of avian species. This might explain the loss of v-MybL3,4A leukemogenic potential in vivo. We also demonstrate that the v-Myb leucine zipper domain interacts in vitro with two host cell proteins, p26 and p28. This interaction is compromised in v-MybL3,4A indicating that binding of v-Myb to p26 and p28 might be important for the leukemogenic potential of v-Myb.
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PMID:The Myb leucine zipper is essential for leukemogenicity of the v-Myb protein. 941 37


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