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Query: UMLS:C0079731 (B-cell lymphoma)
 16,671 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We analyzed the overall structures of N-linked oligosaccharides on glycoproteins of various murine lymphocytic and lymphoma cells employing a newly developed method which was performed on high-performance liquid chromatography after derivatization of oligosaccharides with 2-aminopyridine. A total of 15 types of bi, tri- and tetra-antennary N-acetyllactosamine-type oligosaccharides with or without fucose and oligomannose-type oligosaccharides were identified on these cells in variable amounts depending on the type and maturation stage of the cells. It was found that all murine lymphocytic cells carry N-acetyllactosamine-type oligosaccharides with the additional alpha-linked galactose residue on the non-reducing ends. Thymocytes had exceptionally large amounts of oligosaccharides with one or even two alpha-galactose residues per molecule. In contrast, peripheral resting T cells possessed those oligosaccharides only in a small amount, although the cells produced more the oligosaccharides after stimulation with Con A. Two thymoma lines such as BW 5147 and EL-4 and one B cell lymphoma line WEHI231 contained relatively large amount of oligosaccharides with alpha-galactose residues. Significant change of the molar ratio of component carbohydrates by cell activation was observed also in oligommanose-type oligosaccharides which were few in resting T cells but were markedly increased in Con A activated cells. Molar ratio of triantennary oligosaccharides in total N-acetyllactosamine type oligosaccharides was high in thymocytes and low in resting T cells, but was increased in T cells after Con A activation. It was also very high in WEHI 231 B cell lymphoma. Although BW 5147 and EL-4 thymoma did not contain tri-antennary oligosaccharides in high proportion, they carried larger tetra-antennary oligosaccharides with an N-acetyllactosamine repeating unit in definitive amounts. It is suggested from these results that overall structures of oligosaccharides on cell surface proteins of lymphocytes are finely controlled with link to cell differentiation, activation and transformation.
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PMID:Cell type and maturation stage-dependent polymorphism of N-linked oligosaccharides on murine lymphocytes and lymphoma cells. 192 4

In order to investigate T cell-B cell interactions we constructed monoclonal, antigen-specific T- and B-cell populations. The Ia+ B-cell lymphoma A20-2J was transfected with trinitrophenyl (TNP)-specific heavy (mu) and light (kappa) chain Ig genes. A hapten-carrier complex (TNP-keyhole limpet hemocyanin (KLH)) bound to the surface Ig expressed on the transfectant and was presented to carrier-specific T-cell hybridoma clones at markedly low doses of antigen (0.01 microgram/ml) and in an Ia-restricted fashion. Two responses were elicited in the responding T-cell clones: (i) high levels of IL-2 secretion (320 units/ml), and (ii) cytotoxicity directed against the antigen-presenting B cell. This cytotoxicity was inhibited by D-mannose and was directed against innocent bystander cells, unlike cytotoxicity mediated by NK cells or alloreactive cytotoxic T lymphocyte. Helper and cytotoxic functions were often present in different T-cell hybridomas but some clones exhibited both activities. One representative T-cell hybridoma exhibited strong helper function for TNP-primed splenic B cells as detected in a plaque-forming cell assay, but was cytotoxic toward antigen-presenting B cells. Such monoclonal assay systems for studying cognate interactions of heterogeneous T cells and specific antigen-presenting cells will provide us with valuable new approaches for the study of antigen-specific T-cell regulation of B-cell activation in immune responses.
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PMID:Clonal analysis of antigen-specific interactions between T cells and genetically engineered B cells. 295 69

The processing of murine invariant chain (Ii) to a cell surface form bearing complex N-linked oligosaccharides has been demonstrated in the B cell lymphoma, AKTB-1b. In addition, the rate of processing of pulse-labeled Ii has been determined relative to its rate of dissociation from the alpha/beta complex of I-Ak. Ii, alpha-, and beta-chains were immunoprecipitated with anti-I-Ak or anti-Ii monoclonal antibodies. The heretofore uncharacterized complex oligosaccharide form of Ii (Ii-c) was identified in gel-purified immunoprecipitates by peptide mapping with reverse-phase HPLC. Ii-c is resistant to deglycosylation by Endo H, which is specific for high-mannose N-linkages, but can be digested with Endo F, a glycosidase capable of cleaving both complex and high-mannose N-linked oligosaccharides. Immunoprecipitation of surface iodinated cells indicates that Ii-c is expressed on the plasma membrane. Pulse-chase metabolic labeling data show that the processing of Ii to Ii-c occurs with a t1/2 of about 120 min. In contrast, the processing of both alpha- and beta-chains of I-Ak to complex forms occurs with a t1/2 of 15 to 20 min. Our data show that Ii-hm begins to dissociate rapidly from the I-Ak complex after 100 to 120 min of chase. Only a small amount (less than 5% on a per mole basis) of Ii-c was found associated with the I-Ak complexes after 300 min of continuous metabolic labeling. These results are consistent with Ii serving as a carrier for Ia antigens as they are transported to the cell surface. In addition, they suggest that the processing of Ii to Ii-c, or a late processing event of the alpha- and beta-chains, such as their sialylation, may be a possible mechanism for inducing the dissociation of Ii from the I-Ak complex.
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PMID:Murine Ia-associated invariant chain's processing to complex oligosaccharide forms and its dissociation from the I-Ak complex. 387 94

The oligosaccharide side chains of the murine invariant chain (Ii) glycoprotein associated with the Ia antigens have been characterized. Affinity chromatography using a monoclonal antibody column was employed to purify the I-Ak antigen from lysates of the AKTB-1b B cell lymphoma. The invariant chain isolated by this procedure was subsequently digested with proteases, and the resulting glycopeptides were fractionated by reverse-phase high-pressure liquid chromatography (HPLC). The invariant chain appears to contain two glycosylation sites, both of which carry high-mannose oligosaccharides, each with a restricted size distribution and an average composition of Man6GlcNAc2 as judged by gel filtration and alpha-mannosidase digestion. These data, together with the observation that the invariant chain cannot be labeled metabolically with 3H-glucosamine, 3H-fucose, or 3H-galactose, allow the conclusion that the murine invariant chain does not contain complex oligosaccharides and is not O-glycosylated during its association with the Ia antigens.
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PMID:Characterization of the oligosaccharides from the invariant chain associated with murine Ia antigens. 640 79

The H-2Kk glycoprotein has been isolated by monoclonal antibody affinity chromatography, and an analysis of the asparagine-linked oligosaccharides present at the two major glycosylation sites has been performed. Antigen obtained from the AKTB-1b B-cell lymphoma that had been labeled with [2,6-3H]mannose for 5 or 21 h or for 5 h followed by a 5-h chase was digested exhaustively with trypsin. Each glycosylation site was then isolated by reverse phase high performance liquid chromatography using a C18 column. After removal from the peptide backbone by the almond emulsin peptide: N-glycosidase, the oligosaccharides from each isolated site were analyzed by gel filtration, ion exchange chromatography, concanavalin A affinity chromatography, and glycosidase treatment to assess the contribution of sialic acid and branching patterns of the oligosaccharide backbones to the overall microheterogeneity. The glycosylation of the H-2Kk antigen derived from several different AKTB-1b tumor preparations was examined during a period covering 1 year, during which time the tumor was passaged continuously in vivo in 2-week cycles. Our results conclusively demonstrate that the pattern of oligosaccharide microheterogeneity at the two glycosylation sites of the H-2Kk antigen derived from AKTB-1b cells is stable and that each site differs as to the specific array of oligosaccharide types found on the fully processed glycoprotein. In addition, this report describes an analytical scheme employing reverse phase high performance liquid chromatography to follow oligosaccharide processing and hydrolysis of the N-glycosidic bond by the peptide: N-glycosidase.
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PMID:Stable oligosaccharide microheterogeneity at individual glycosylation sites of a murine major histocompatibility antigen derived from a B-cell lymphoma. 660 28

We hypothesized that the phytosterols beta-sitosterol (BSS), beta-sitosterol glucoside (BSSG), and Moducare (MC; BSS:BSSG = 99:1) could modulate the growth of estrogen-dependent human breast cancer cells in vitro and in vivo. The present study evaluated the estrogenic and antiestrogenic effects of BSS, BSSG, and MC (0.001 to 150 micromol/L) on the proliferation of Michigan Cancer Foundation 7 (MCF-7) cells in vitro. Both BSS (>1 micromol/L) and MC (>50 micromol/L) increased MCF-7 cell proliferation. Treatment with 150 micro mol/L of BSS and MC increased cell growth by 2.4 and 1.5 times, respectively, compared to the negative control (NC) group. However, BSSG had no effect at the concentrations tested. The effects of dietary BSS, BSSG, and MC on the growth of MCF-7 cells implanted in ovariectomized athymic mice were also evaluated. Estrogenic effects of the phytosterols were evaluated in the NC, BSS, BSSG, and MC treatment groups, and antiestrogenic effects were evaluated in the 17 beta-estradiol (E(2)), E(2) + BSS, E(2) + BSSG, and E(2) + MC treatment groups. Mice were treated with dietary BSS (9.8 g/kg AIN93G diet), BSSG (0.2 g/kg diet), or MC (10.0 g/kg diet) for 11 wk. Dietary BSS, BSSG, and MC did not stimulate MCF-7 tumor growth. However, dietary BSS, BSSG, and MC reduced E(2)-induced MCF-7 tumor growth by 38.9% (P < 0.05), 31.6% (P = 0.08), and 42.13% (P < 0.05), respectively. The dietary phytosterols lowered serum E(2) levels by 35.1, 30.2, and 36.5% in the E(2) + BSS, E(2) + BSSG, and E(2) + MC groups, respectively (P < 0.05), compared to that of the E(2) treatment group. Estrogen-responsive pS2 mRNA expression in tumors did not differ among groups, but expression of the antiapoptotic marker B-cell lymphoma/leukemia-2 (bcl-2) in tumors from the E(2) + MC group was downregulated, compared to that of the E(2) treatment group. In summary, BSS and MC stimulated MCF-7 cell growth in vitro. Although BSSG comprises only 1% of MC, BSSG made MC less estrogenic than BSS alone in vitro. However, dietary BSS and MC protected against E(2)-stimulated MCF-7 tumor growth and lowered circulating E(2) levels.
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PMID:beta-Sitosterol, beta-Sitosterol Glucoside, and a Mixture of beta-Sitosterol and beta-Sitosterol Glucoside Modulate the Growth of Estrogen-Responsive Breast Cancer Cells In Vitro and in Ovariectomized Athymic Mice. 1511 61

Two novel lectins were purified from rhizomes of two sweet flag species, namely Acorus calamus (Linn.) and Acorus gramineus (Solandin Ait.) by affinity chromatography on mannose linked epoxy-activated Sepharose 6B. The apparent molecular mass of the lectins, as determined by gel filtration chromatography, was 56 kDa for ACL and 55 kDa for AGL. In SDS-PAGE, pH 8.3, both lectins migrated with a subunit molecular mass of 13.6 kDa and 13.5 kDa, respectively, under reducing and non-reducing conditions thus indicating the absence of disulphide linkages. Acorus lectins readily agglutinated rabbit, rat and guinea pig erythrocytes. Both ACL and AGL also reacted with RBCs from sheep, goat and human ABO blood groups after neuraminidase treatment. ACL and AGL were inhibited by mannose/glucose and their derivatives. The most effective inhibitor was methyl-alpha-D-mannopyranoside. Acorus lectins were stable up to 55 degrees C, did not require metal ions for their activity and were also affected by high concentrations of denaturants like urea, thiourea and guanidine-HCl. These lectins showed potent mitogenic activity towards mouse splenocytes and human lymphocytes. Both ACL and AGL also significantly inhibited the growth of J774, a murine macrophage cancer cell-line and to lesser extent WEHI-279, a B-cell lymphoma.
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PMID:Novel lectins from rhizomes of two Acorus species with mitogenic activity and inhibitory potential towards murine cancer cell lines. 1595 73

The use of monoclonal antibodies (MAbs) in cytotoxic conjugates (radionuclides, toxins, or drugs) for targeting tumor cells is restricted due to toxicity in vital organs. Through improved tumor targeting, it is possible to administer larger amounts of such labeled MAbs, thus improving the ability to eradicate tumor cells without increased normal organ toxicity. Extracorporeal affinity adsorption treatment (ECAT) has therefore been developed using an avidin-agarose (AA) adsorbent with high binding affinity for the biotinylated radiolabeled MAb, rituximab. During ECAT, excess radioimmunoconjugates, not bound to the tumor cells, can be removed improving tumor targeting. The present study was performed to estimate the biocompatibility of the AA adsorber. Seven patients with B-cell lymphoma not responding to conventional treatment were studied. During the ECAT procedure, blood (B) components, plasma (P) complement fragments C3a, C5a, and P-bradykinin were analyzed, and other laboratory tests were carried out. Slight decreases in B-hemoglobin (8.3%), B-thrombocytes (11.4%), and P-albumin (14.3%) were observed, and could be explained by the dilution of the blood with normal saline and acid citrate dextrose. The AA adsorbent had no effect on the blood cells, immunological status or P-bradykinin level. The AA adsorber demonstrated good hemocompatibility and biocompatibility, without any side effects in the patients.
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PMID:Biocompatibility of a novel avidin-agarose adsorbent for extracorporeal removal of redundant radiopharmaceutical from the blood. 1734 96

We recently experienced a case with uveitis suffering from fever of unknown origin suspected of being caused by sarcoidosis. Chest computed tomography showed right supraclavicular, bilateral mediastinal, and right hilar lymphadenopathy, and intensive abnormal uptake of 2-[18F]fluoro-2-deoxy-D-glucose (18F-FDG) was observed on positron emission tomography with 18F-FDG (FDG-PET). On the other hand, 67Ga scintigraphy showed almost no abnormal findings. Histopathological examination revealed the lesion to be a diffuse large B-cell lymphoma (DLBCL), namely, an aggressive non-Hodgkin lymphoma from a right supraclavicular lymph node biopsy specimen. Additional immunohistochemical analysis showed the negative expression of transferrin receptor (TfR) on the formalin-fixed paraffin-embedded specimen. Although DLBCL is generally considered to be a 67Ga-avid tumor, it does not always have a large number of TfRs and that leads to a discrepancy between the 67Ga scintigraphy and FDG-PET findings. FDG-PET should be more appropriate for the initial staging of DLBCL than 67Ga scintigraphy, whereas 67Ga scintigraphy might be able to provide additional information including prognostic factors and to support strategies that target TfR for cancer therapy.
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PMID:A 18F-FDG-positive, 67Ga-negative, and transferrin receptor expression-negative patient with diffuse large B-cell lymphoma. 1770 20

Positron emission tomography (PET) with [18F] fluoro-2-deoxy-D-glucose (FDG) is used for the diagnosis of various types of cancer. FDG-PET is used also for the assessment of therapeutic response as well as work-up of recurrence after therapy. Due to the characteristics of FDG-PET as an imaging tool, FDG-PET is supposed to be superior to the conventional imaging such as CT for the accurate assessment of the treatment response in patients with malignant lymphoma. Malignant lymphoma usually undergoes chemotherapy or chemoimmunotherapy as a treatment of stage III and IV patients. Recent advancement in the therapy of malignant lymphoma enables optional treatment strategies such as radioimmunotherapy with 90Y-labeled anti-CD20 monoclonal antibody or oral fludalabine for indolent non-Hodgkin's lymphoma and high-dose chemotherapy with autologous stem cell transplantation for aggressive non-Hodgkin's lymphoma. The purpose of the present study was to determine the clinical value of FDG-PET for the early assessment of therapeutic response of malignant lymphoma. Twenty-six patients with malignant lymphoma were enrolled in the study. The subject consists of 10 patients with follicular lymphoma, 9 diffuse large B-cell lymphoma, and others. Therapeutic regimens were rituximab plus cyclophosphamide, doxorubicin, vincristine, and prednisone (R-CHOP) for 19 patients, CHOP and ABVD (doxorubicin, bleomycin, vinblastine, dacarbazine) for 2 patients each, and others. FDG-PET was performed before the initiation of therapy in all patients and after the therapy of 1-2 courses in 5 patients; and 3-4 courses, 5-6 courses, and 7-8 courses in 7 patients each. Complete remission on the PET (CR(PET)) was defined as the FDG uptake lower than the background and compared with the final response assessment. CR(PET) was acquired in 4 of 5 patients at 1-2 courses, 6 of 7 at 3-4 courses, 4 of 7 at 5-6 courses, and 3 of 7 at 7-8 courses. In the group of 7-8 courses, final response assessment revealed 2 patients excess of CR. In patients who underwent multiple PET studies during the treatment, all 4 patients showed CR(PET) in its first assessment, and maintained CR thereafter. The present study revealed that most of the patients achieved CR(PET) up to 4 courses of therapy. The cases with remaining FDG uptake at this time were likely to be resistant to the therapy. The early assessment of therapeutic response may be accurately assessed by FDG-PET as early as 2 or 4 courses of therapy. Residual uptake of FDG in the lesion would be considered to be subject to the new therapeutic strategy. Clinical usefulness of the strategy based on the early response assessment with FDG-PET would be confirmed by the clinical trials.
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PMID:[Application of 18F-FDG PET for the assessment of early response to the treatment and prognosis of patients]. 1963 20


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