Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0153470 (Spleen)
 4,015 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Spleen cells, from BALB/c mice that had been infected with lactate dehydrogenase-elevating virus (LDV) for 6 days and that had or had not been previously immunized with glutaraldehyde-inactivated LDV, were fused with NS-1 myeloma cells. The fusion frequency was at least 10 times higher than with spleen cells of normal or chronically infected mice. Only 1 of 297 wells containing hybridomas prepared with spleens from unprimed 6-day-infected mice produced LDV-specific monoclonal antibodies (mAb). In contrast, when mice were immunized with inactivated LDV before infection, 33 of 73 hybridoma-containing wells screened were LDV-specific. The mAbs produced were mainly of IgG2a, IgM, and IgG1 subclasses and exhibited an identical characteristic staining pattern of LDV-infected cultured macrophages. A single mAb of IgG2b isotype yielded a different staining pattern. Western blotting showed that all of 12 mAbs analyzed in more detail were specific for the LDV glycoprotein, VP-3, but none of these neutralized the infectivity of the homologous strain of LDV. They also did not significantly protect immunosuppressed 10-month-old C58 mice against LDV-induced paralytic poliomyelitis, as does passive immunization with polyclonal mouse anti-LDV IgG.
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PMID:Characteristics of monoclonal antibodies to the lactate dehydrogenase-elevating virus. 361 May 72

Modified env gene or gp55 gene in Spleen Focus Forming Virus, polycythemic strain, K-1 was molecularly cloned and its structure was characterized gp55 is a fusion glycoprotein consisting of N terminal 2/3 of xenotropic virus-related gp70 and C terminal half of F-MuLV p15E. A unique structure at the 3' and of the gp55 gene with 6 base pairs + 1 base pairs insert was identified. Gp55 may be hooked by the lipid bilayer of the cell membrane of the SFFV-intected cells, and additional glycosylation on the cell surface may modify the growth regulation of the cells. Possible origin of SFFV-specific gp55 gene was discussed.
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PMID:[Modified env gene in Friend spleen focus forming virus--structure, origin, and its role in leukemogenesis]. 385 23

We describe a previously uncharacterised glycoprotein antigen of rat brain. The antigen was localised by immunofluorescence on 10 micron cryostat tissue sections, and was found to be present intracellularly in neurons. No other cell types or structures within the brain were stained. The antigen is recognised by a mouse monoclonal antibody called NGP41. The antibody was produced after immunising a mouse with glycoproteins purified by lentil lectin affinity chromatography of solubilised rat brain membranes. Spleen cells from the immunised mouse were fused with the myeloma P3X63Ag8. The antigen is expressed by neurons in all brain regions, and also in the dorsal root ganglion neurons of the peripheral nervous system. In all brain regions, the large projection neurons are the most intensely stained by immunofluorescence, but some small neurons also express the antigen. Although dendrites were not stained, sections of sciatic nerve were stained by NGP41, suggesting that the antigen is expressed by axonal processes. The cell bodies of neurons in the inferior olive were stained by NGP41, but their terminals on Purkinje cell dendrites in the cerebellar cortex were not stained, suggesting that the antigen is absent or expressed below the limit of detection in terminals. Both crude brain membranes and a lentil lectin affinity purified brain glycoprotein fraction absorbed the antibody, suggesting that the antigen is a membrane bound glycoprotein. In immunoblotting experiments, the antigen was detected in homogenates of brain and spinal cord membranes, where it appeared as a triplet of bands with molecular weights of 41K, 38K and 36K. Antigen was not detected by immunoblotting in homogenates of six different tissues of non-nervous origin. The antigen was enriched in glycoprotein fractions from adult and juvenile cerebellum as assessed by immunoblotting. Adult brain glycoprotein preparations had a triplet structure similar to that in the homogenates, although most of the antigenic activity of the juvenile preparation was found in a position corresponding to the upper two bands of the triplet.
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PMID:Recognition by a mouse monoclonal antibody of a glycoprotein antigen of rat brain which is expressed intracellularly by neurons. 608 6

BALB/c mice were injected with an affinity-chromatography-purified placental transferrin receptor preparation. Spleen cells were fused with NS-1 myeloma cells. Sixteen hybrids producing monoclonal antibodies specific for the transferrin receptor and two hybrids specific for transferrin were identified by radioimmunoassay (RIA). Five hybrids were selected for cloning on the basis of antibody specificity and affinity. None of the antibodies inhibited the binding of transferrin to K562 cells. The binding of antibody ID9 to K562 cells was partially inhibited by transferrin or a polyclonal goat anti-transferrin receptor antiserum. Of the five antibodies, two (IIB6 and IIB2) reacted only with the purified receptor and solubilized cells and not with whole cells. The other three antibodies, when tested with normal human cells and leukaemia and tumour cell lines, showed identical reaction patterns. The antibodies precipitated a glycoprotein from K562 cells with an apparent molecular weight of 94,000, estimated from sodium dodecyl sulphate-polyacrylamide gel electrophoretograms run under reducing conditions, and a molecular weight of 188,000 when run under unreduced conditions. All antibodies have a high affinity with Ka values ranging from 1.44 X 10(9) to 3.56 X 10(10) (l/mol). The antigen precipitated by all five antibodies showed identical peptide maps after partial proteolytic digestion.
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PMID:Monoclonal antibodies to a purified human transferrin receptor. 609 40

Spleen cells from BALB/c mice immunized with human ovarian cystadenocarcinoma extract were fused with the mouse myeloma cell line P3/NSI/1-Ag 4 in the presence of polyethylene glycol (Mr 4000). Of the 46 hybrids obtained, four secreted antibodies preferentially reactive to the immunizing ovarian tumor extract. Two of these hybrids, which showed no reaction with normal controls, were selected for cloning by the limiting dilution method. The numerous clones obtained from each hybrid were screened against a panel of five ovarian tumor extracts, pooled normal ovary extracts, and pooled normal human sera. One clone from each hybrid that showed specificity for ovarian mucinous cystadenocarcinomas was recloned to assure monoclonality and to establish a permanent hybridoma cell line. The antibodies secreted by these cell lines were of IgG1 subclass with kappa light chains. These antibody-producing hybridomas were selected for further analysis of the antibody specificity by a solid-phase radioimmunoassay and quantitative absorption tests. The monoclonal antibodies recognized an antigenic determinant present only in mucinous cystadenocarcinomas of the ovary. These did not react with any other gynecological or nongynecological tumor thus far tested. The antigen was not demonstrable in any normal adult tissues tested. Among fetal tissues examined, only fetal intestine extract showed a positive reaction. The antigenic determinant recognized by these monoclonal antibodies was unrelated to carcinoembryonic antigen, normal glycoprotein, normal human serum components, or human ABO blood group materials. These antibodies, which have relatively high affinity and can be produced in large amounts, will be useful for the isolation and immunochemical characterization of this antigen. The purified antigen and the specific antibodies could be then combined in a sensitive radioimmunoassay for the early detection of the antigen in the sera and body fluids of patients with ovarian mucinous cystadenocarcinomas.
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PMID:Monoclonal antibodies recognizing tumor-associated antigen of human ovarian mucinous cystadenocarcinomas. 617 95

Spleen cells from C57BL/10 mice injected with syngeneic B10 L-glutamic acid60-L-alanine30-L-tyrosine10 (GAT)-pulsed macrophages (GAT-M phi) within 18 h of birth were unable to respond to soluble GAT, GAT-methylated bovine serum albumin, or B10 GAT-M phi as adults. Spleen cells from these neonatally treated mice responded at control levels to GAT presented in allogeneic M phi and to sheep erythrocytes. Partially purified T cells from these neonatally treated mice suppressed responses by syngeneic virgin, but not primed, spleen cells in an antigen-specific manner and acted during the early phases of the response. These responder GAT-specific suppressor T cells (GAT-TSR) were sensitive to anti-Thy-1 + C and 500-rad irradiation and have the phenotype Ly-1-2+, I-J+; GAT-TSR cells can only suppress responses by spleen cells syngeneic with the GAT-TSR cells at the I-J subregion of H-2. Restimulation of these Ts cells with syngeneic GAT-M phi induces an antigen-specific suppressor factor within the supernatant fluid. The factor, GAT-TsFR, is a glycoprotein with a molecular weight between 48,000 and 63,000, as determined by gel filtration chromatography using isotonic buffers; it bears serologically detectable determinants encoded by the I-J subregion of the H-2 complex, has an antigen-binding site for GAT and L-glutamic acid50-L-tyrosine50, and shares idiotypic determinants with anti-GAT antibodies. The presence of GAT-TsFR in the first 36 h of in vitro culture is required for significant suppression. Furthermore, only responses by spleen cell syngeneic with the cells producing GAT-TsFR at the I-J subregion are suppressed. The fusion of GAT-TsFR-producing cells with BW5147 resulted in generation of two hybridomas with properties and characteristics identical to those of the conventional GAT-TsFR with one exception: conventional and hybridoma 372.D6.5 GAT-TsFR only suppress responses by spleen cells of the I-Jb haplotype, whereas suppression mediated by the second hybridoma GAT-TsFR (372.B3.5) is genetically unrestricted. These hybridoma GAT-TsFR are compared with nonresponder GAT-Ts factor (GAT-TsF) and these responder and nonresponder GAT-TsF are considered in the context of suppressor pathways.
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PMID:Antigen-specific suppression in genetic responder mice to L-glutamic acid60-L-alanine30-L-tyrosine10 (GAT). Characterization of conventional and hybridoma-derived factors produced by suppressor T cells from mice injected as neonates with syngeneic GAT macrophages. 618 35

The dolichol and dolichyl phosphate (Dol-P) content of various tissues and liver subcellular fractions obtained from rats have been measured directly using high pressure liquid chromatographic methods developed in this laboratory. Spleen contained the highest concentration of dolichol, while other tissues including serum had smaller amounts. Although considerable differences in homologue distribution patterns were observed among the tissues examined, a number of purified subcellular fractions obtained from liver (nuclei, mitochondria, cytosol, and microsomes) exhibited a single common pattern. Only some 5% of liver dolichol appeared in the microsomal compartment of the cell where glycoprotein formation occurs, while 50% of the dolichol in this tissue was found in a lysosome-enriched fraction. The concentrations of dolichol present in liver nuclei, mitochondria, whole microsomes (also rough and smooth, endoplasmic recticulum (RER and SER, respectively), and cytosol were considerably lower (on a protein basis) than those present in whole liver. Besides the lysosome-enriched fraction, only plasma membranes and Golgi contained dolichol at concentrations equal to or greater than those present in liver homogenates. The low concentrations of dolichol found in microsomes suggest that the amounts of dolichol available for Dol-P formation via the CTP-dependent kinase reaction may be rate limiting. Most of the Dol-P in liver could be recovered in the microsomal fraction. Dol-P accounted for 4 and 40% of the sum of alcohol + dolichyl fatty acyl ester + Dol-P forms present in whole liver and in microsomes, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Distribution and metabolism of dolichol and dolichyl phosphate in rat liver. 631 69

We used the hybridoma technique to characterize further the platelet glycoprotein abnormality in Glanzmann's thrombasthenia. Spleen cells from Balb/c mice immunized with human platelets were fused to mouse myeloma cell line Sp2/0-Ag14. Hybridoma lines producing a variety of antiplatelet antibodies were isolated by hypoxanthine-aminopterin-thymidine selection and cloned, and purified monoclonal IgG from six lines was prepared. One of these lines, 8aB5-9, produced an antibody, Tab, that binds to a protein on normal but not thrombasthenic platelets. We isolated this protein from Triton X-100 solubilized normal platelet membranes by affinity chromatography on Tab-Sepharose. As determined by SDS polyacrylamide gel electrophoresis, the isolated protein is a complex of glycoproteins IIb and IIIa, because the two subunits comigrate with glycoproteins IIb and IIIa of whole platelets and show identical changes in mobility after disulfide bond reduction. We prepared (125)I-Tab to determine the number of glycoprotein IIb-IIIa complexes on normal and thrombasthenic platelets by a direct binding assay. Platelets from 17 normal donors bound 39,000+/-4,600 (SD) Tab molecules/platelet. Platelets from four patients with thrombasthenia lacked Tab binding sites (<5%). Five obligate and four presumed heterozygotes for thrombasthenia bound 24,500+/-5,800 Tab molecules/platelet. The platelet alloantigen, Pl(Al), is not that recognized by Tab, because platelets from three Pl(Al)-negative subjects bound Tab normally. Studies with the Tab antibody have (a) enabled quantitation of the number of glycoprotein IIb-IIIa complexes on normal platelet membranes, (b) demonstrated that thrombasthenic homozygotes lack and heterozygotes have a partial deficiency of this complex, and (c) made possible the isolation of this membrane protein which may be required for normal platelet aggregation and clot retraction.
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PMID:Isolation and quantitation of the platelet membrane glycoprotein deficient in thrombasthenia using a monoclonal hybridoma antibody. 644 21

Monoclonal antibodies reactive with NIH/3T3 cell surface antigens were obtained from hybridomas of murine myeloma cells fused to spleen cells of rats immunized with NIH/3T3 cell plasma membranes. Four of the antibodies, of forty that have been studied, appeared to react with allospecific antigenic determinants: they bound to NIH/3T3 cells but not to BALB/ 3T3 cells. Each of these four antibodies immunoprecipitated a glycoprotein of about 80,000 daltons that migrated to an isoelectric point of about pH 5.0. Polypeptides of identical molecular weight and isoelectric points, and yielding the same proteolytic cleavage fragments, were present in BALB/3T3 cells, but were not antigenically reactive. The 80,000-dalton glycoprotein was a major constituent of the plasma membrane. It was a predominant lactoperoxidase iodinated component of intact NIH/3T3 cells, and saturation binding of 125I-labeled antibody indicated that there were about 10(6) antigenic sites/cell. Studies of the distribution of the immunoreactive glycoprotein among different strains of mice confirmed the polymorphic expression of the determinant: Spleen cells of BALB/c, DBA/1, DBA/2, and CBA mice did not bind anti-80,000-dalton glycoprotein monoclonal antibodies, whereas spleen cells of a large number of other strains of mice were positive for antibody-binding. The antigenic reactivity varied markedly among different cell lines and was greatest with the NIH/3T3 mouse embryo fibroblast, G8-1 Swiss Webster myoblast, and IC-21 SV40-transformed C57BL/6 mouse peritoneal macrophage. The properties of the 80,000-dalton glycoprotein characterized this molecule as a new cell surface differentiation alloantigen of murine mesenchymal cells.
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PMID:Murine cell surface glycoproteins. Characterization of a major component of 80,000 daltons as a polymorphic differentiation antigen of mesenchymal cells. 678 57

The gene encoding the Leishmania major (L. major) promastigote surface glycoprotein, gp63, was introduced into the Salmonella typhimurium (S. typhimurium) aroA- aroD- live oral vaccine strain BRD509 and expressed under the control of a constitutive tac promoter in plasmid pKK233-2. This construct (GID101) expressed gp63 in vitro and was used to immunize highly susceptible BALB/c mice by the oral route. The plasmid was relatively stably inherited by bacteria growing or persisting in the mesenteric lymph nodes of immunized mice. Mice immunized with GID101 developed significant resistance against a challenge infection with L. major compared to controls immunized with BRD509 alone. Spleen and lymph node cells from immunized mice developed a strong in vitro proliferative T-cell response to killed or live L. major. The activated T cells secreted interleukin-2 (IL-2) and interferon-gamma (IFN-gamma) which was abrogated by treatment with anti-CD4 but not with anti-CD8 antibody. The cells did not produce detectable levels of interleukin-4 (IL-4). The immunized mice also produced significant amounts of leishmanial specific IgG2a antibody but did not develop delayed-type hypersensitivity (DTH) to live parasites. No IgG1 antibody was detected. These data therefore demonstrate that gp63 gene delivered orally by a vaccine strain of S. typhimurium can preferentially induce the development of Th-1 subset of CD4+ T cells and protective immunity in the highly susceptible BALB/c mice.
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PMID:Protection against Leishmania major infection in genetically susceptible BALB/c mice by gp63 delivered orally in attenuated Salmonella typhimurium (AroA- AroD-). 763 11


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