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Biomedical subjects

J Yodoi

Publications and source records attributed to J Yodoi.

At least 235 records · Page 13Linked to original sources
PubMed1988

Regulation of Fc epsilon receptor expression on a human monoblast cell line U937.

Fc epsilon receptor (Fc epsilon R) expression on several human cell lines (U937, RPMI 8866, HL 60, THP-1, and Molt 4) and its regulation were examined by immunofluorescent analysis using a monoclonal anti-human Fc epsilon R antibody, H107. Phorbol ester (PMA), recombinant gamma interferon (IFN-gamma) and H107 itself enhanced Fc epsilon R expression on a FC epsilon R positive cell line U937, whereas these reagents did not induce FC epsilon R expression on the Fc epsilon R negative cell lines, Molt 4, HL 60 and THP-1. Dexamethasone not only suppressed by 50% the spontaneous Fc epsilon R expression on U937 cells but also completely inhibited the enhancement of their Fc epsilon R expression on U937 cells induced by PMA, IFN-gamma or H107. Dexamethasone caused a little suppression of Fc epsilon R expression by RPMI 8866 cells. The results showed that Fc epsilon R expression on a human monoblast cell line U937 was up- or down-regulated by a variety of physiological or pharmacological agents. These experimental systems provide a good model for the investigation of the regulatory mechanisms of Fc epsilon R expression.

Antibodies, Monoclonal↗
PubMed1988

IL-2 receptor and Fc epsilon R2 gene activation in lymphocyte transformation: possible roles of ATL-derived factor.

Lymphocyte transformation/activation is accompanied by the induction of a variety of the inducible receptors associated with the activation antigens. The p55 chain of the interleukin-2 receptor (IL-2R/p55) recognized by anti-Tac monoclonal antibody (mAb) is expressed on activated T and B cells as well as natural killer (NK) cells. IL-2R/p55(Tac) is constitutively expressed on T4(+) T cells transformed by human T-lymphotropic virus I (HTLV-I), which is a causative agent for adult T-cell leukemia (ATL). Low affinity Fc receptor for IgE (Fc epsilon R2/CD23) is another inducible receptor binding IgE and is expressed on various hematopoietic cell types. While the physiological expression of Fc epsilon R2 and its soluble form (IgE Binding Factor; IgE BF) is variably regulated by cytokines and IgE, there is a constitutive expression of Fc epsilon R2 on Epstein-Barr virus (EBV) transformed B cell lines and some of HTLV-I (+) T cell lines. ATL-derived factor (ADF) has been characterized as an IL-2R/p55(Tac) inducing factor derived from HTLV-I(+) T cell lines. Purification of ADF protein and the cDNA cloning proved that ADF is closely related to the autocrine growth factor produced by an EBV(+) B cell line 3B6 (H. Wakasugi and T. Tursz) and belonging to the family of thiol reducing co-enzyme thioredoxin which is involved in many biological reactions. Recombinant ADF produced by COS cells and E. coli showed both IL-2R inducing and reducing activities. We will discuss the biological roles of ADF in viral and normal lymphocyte activation and transformation in relation to the receptor gene activation.

Amino Acid Sequence↗
PubMed1987

Impaired expression of high affinity interleukin 2 receptor on activated lymphocytes from patients with systemic lupus erythematosus.

Peripheral lymphocytes stimulated with phytohemagglutinin (PHA-blasts) were examined for their responsiveness to exogenous interleukin 2 (IL-2). The proliferative response of PHA-blasts to IL-2 was significantly lower in patients with systemic lupus erythematosus (SLE) than in normal subjects. To clarify the reason for this defect, the expression of IL-2 receptor (IL-2R) on PHA-blasts was investigated using anti-Tac antibody and purified IL-2. Cytofluorometric analysis showed no statistical differences in the Tac positivity of PHA-blasts among normal subjects and patients with active and inactive SLE. Scatchard analysis using 125I-labeled anti-Tac monoclonal antibody revealed that the number of Tac epitopes on PHA-blasts was also not different among them. Next, the affinity of IL-2R expressed on PHA-blasts was determined by Scatchard analysis using radiolabeled IL-2 as a ligand. The number of high affinity IL-2R on the PHA-blasts was significantly decreased in patients with active and inactive SLE, as compared with normal subjects. The responsiveness of PHA-blasts to exogenous IL-2 was well correlated to the number of high affinity IL-2R, but not to the number of Tac epitopes or total IL-2R. Inasmuch as high affinity components of IL-2R are functionally active, the defective expression of high affinity IL-2R may be responsible for the T cell dysfunctions in SLE.

Antibodies, Monoclonal↗
PubMed1987

Monoclonal antibody specific for T cell-derived human IgE binding factors.

A B cell hybridoma secreting monoclonal antibody against human IgE binding factors was obtained by immunization of BALB/c mice with partially purified IgE binding factors, and fusion of their spleen cells with SP-2/0-AG14 cells. The monoclonal antibody bound all of the 60,000, 30,000, and 15,000 dalton IgE binding factors from two T cell hybridomas and those from activated T cells of a normal individual. The antibody bound both IgE-potentiating factors, which had affinity for lentil lectin, and IgE-suppressive factors, which had affinity for peanut agglutinin. However, the monoclonal anti-IgE-binding factor bound neither Fc epsilon R on RPMI 8866 cells nor IgE binding factors from the B lymphoblastoid cells. A monoclonal antibody against Fc epsilon R on B cells (H107) bound the 60,000 and 30,000 dalton IgE binding factors from both T cell hybridomas and RPMI 8866 cells but did not bind the 15,000 dalton IgE binding factors from either T cells or B cells. The results indicate that T cell-derived IgE binding factors have a unique antigenic determinant that is lacking in both Fc epsilon R on B cells and B cell-derived IgE binding factors. The anti-IgE binding factor and anti-Fc epsilon R monoclonal antibodies both failed to stain cell surface components of IgE binding factor-producing T cell hybridomas. However, both antibodies induced the T cell hybridoma to form IgE binding factors. The results suggest that the T cell hybridomas bear low numbers of Fc epsilon R that share antigenic determinants with IgE binding factors secreted from the cells.

Animals↗
PubMed1987

Activation of interleukin-2 receptor gene by forskolin and cyclic AMP analogues.

Forskolin (FK), a reversible activator of adenylate cyclase, markedly enhanced the expression of interleukin-2 receptor (IL-2-R) on a human natural killer (NK)-like cell line, YT. The FK-induced increase in IL-2-R on YT cells closely correlated with an increase in intracellular cyclic AMP (cAMP) level, and was mimicked by dibutyryl cyclic AMP (dbcAMP). FK induced both high and low affinity IL-2-R on the cells. Using a cDNA for the IL-2-R as a probe, the FK-induced IL-2-R expression was shown to be associated with an increase in IL-2-R mRNA. FK also enhanced the IL-2-R expression on a human T lymphotrophic virus I (HTLV-I) positive T-cell line (YTA-1H) and augmented the phorbol ester-induced expression of IL-2-R on HTLV-I negative T-cell lines (HSB-2 and HPB-ALL). These results suggest the possibility that the stimulation of adenylate cyclase may serve as a pathway leading to activation of the IL-2-R gene in certain types of lymphocytes.

Adenylyl Cyclases↗
PubMed1987

Transcription of IL-2 receptor gene is stimulated by ATL-derived factor produced by HTLV-I(+) T cell lines.

In HTLV-I transformed T-cell lines established from the patients with adult T-cell leukemia (ATL), there is a constitutive activation of the normal IL-2 receptor (IL-2-R) gene. These cell lines continuously produce an ATL-derived factor (ADF), an IL-2-R inducing factor without IL-2 activity. ADF enhances the expression of the IL-2-R through the augmentation of the IL-2-R mRNA in the HTLV-I(+) T-cell line (ED) as well as the NK cell line cells (YT). In YT cells, the transcriptional initiation of the promoter of the IL-2-R gene was enhanced by ADF but not by IL-2. Production of ADF by HTLV-I(+) T-cell lines may be involved in the abnormal expression of IL-2-Rs on these cells.

Cell Line↗
PubMed1987

Human lymphocyte Fc receptor for IgE: sequence homology of its cloned cDNA with animal lectins.

We have purified the human lymphocyte Fc receptor specific for IgE (Fc epsilon receptor) and its soluble form by using the anti-Fc epsilon receptor monoclonal antibody H107. Using an oligonucleotide probe corresponding to the partial amino acid sequence of the soluble Fc epsilon receptor related to IgE binding factor, we cloned, sequenced, and expressed a cDNA for the receptor. The Fc epsilon receptor has 321 amino acid residues with no NH2-terminal signal sequence. The receptor was separated into two domains by a putative 24-amino acid residue transmembrane region located near the NH2-terminal end. The Fc epsilon receptor showed a marked homology with animal lectins including human and rat asialoglycoprotein receptors, chicken hepatic lectin, and rat mannose binding proteins.

Amino Acid Sequence↗
PubMed1987

Interleukin 2 binding molecule distinct from the Tac protein: analysis of its role in formation of high-affinity receptors.

Interleukin 2 (IL-2) receptors on activated T cells exist in high- and low-affinity configurations, both of which share a ligand-binding component known as the Tac protein. Although almost all binding of IL-2 to such cells was inhibited by an antibody to Tac, the predominant component of binding on the natural killer (NK)-like cell line YT was resistant to this reagent. The ligand-binding component on YT cells also differed from Tac in its affinity constant (Kd approximately 8.2 X 10(-10) M vs. Kd approximately equal to 1.1 X 10(-8) M for low-affinity Tac sites) and in its susceptibility to inhibition by certain antibodies to IL-2. When the YT cells were stimulated in a manner that induced expression of the Tac protein, the IL-2 binding sites were converted to a high-affinity configuration (Kd approximately 1.8 X 10(-11) M). Thus, the original binding component on unstimulated YT cells appeared to combine with Tac and IL-2 to produce a high-affinity receptor complex. Use of bifunctional crosslinking agents following ligand binding to unstimulated YT cells yielded covalent IL-2-receptor complexes of 83 and 90 kDa. These complexes were similar in size to those derived from high-affinity receptors on activated T cells and shared a similar fragmentation pattern upon proteolysis. These results demonstrate the existence of a second IL-2 binding component in addition to the Tac protein and suggest that this component combines with Tac and IL-2 to form high-affinity receptor sites.

Antibodies↗
PubMed1987

Interleukin-2 receptor-inducing factor(s) in adult T cell leukemia.

The expression of the interleukin-2 receptor (IL-2-R) is regulated by transcriptional and post-transcriptional mechanisms. IL-2-R gene expression is induced by pharmacological agents including calcium ions, phorbol esters such as phorbol myristate acetate (PMA) and forskolin (FK), a direct activator of adenylate cyclase. HTLV-I(+) leukemic T cells and T cell lines from patients with adult T cell leukemia (ATL) continuously expressed IL-2-R without production of IL-2. However, there was no abnormality of the structural gene for IL-2-R in these cell lines as well as in fresh leukemic cells of ATL. We have detected that many HTLV-I(+) T4(+) T cell lines constitutively produce a non-IL-2 lymphokine named ATL-derived factor (ADF), which induced the expression of the high-affinity IL-2-R on a variety of cells including HTLV-I(+) T cells, myeloid leukemia cells and YT cells. IL-2-R-inducing agents such as ADF and FK were shown to induce elevation of the mRNA levels for IL-2-R through transcriptional enhancement of the IL-2-R gene. The possible involvement of IL-2-R-inducing cytokines in the physiological lymphocyte activation and the leukemogenesis in ATL and other T cell leukemias is discussed.

Antibodies, Monoclonal↗
PubMed1987

IgA binding factors and Fc receptors for IgA: comparative studies between IgA and IgE Fc receptor systems.

The expression of Fc receptors (FcR) for IgA (Fc alpha R) as well as for IgE (Fc epsilon R) on T lymphocytes (T cells) is enhanced or up regulated by the corresponding class of immunoglobulins (Ig). The production of class-specific regulatory factors binding to IgA and IgE (IgA binding factor [IgA-BF]; IgE binding factor [IgE-BF]) is also induced by these respective ligands. Murine IgA-BFs produced by a T hybridoma T2D4 and concanavalin A-activated spleen cells suppressed the in vitro IgA antibody responses of pokeweed mitogen-stimulated mouse spleen cells class-specifically. Human IgA antibody response was also suppressed by the murine IgA-BF. Similar suppressive IgA-BF is also produced by a human natural killer (NK)-like cell line (YT), which has no rearrangement of the T cell receptor beta-chain gene, indicating that non-T non-B/LGL cells may also be involved in the regulation of the class-specific antibody responses. It appears that, in human as well as murine systems, T- and NK-cells have the capacity to co-express multiple class-specific FcRs and to produce the corresponding immunoglobulin binding factors. While the Fc epsilon R expression is abnormally enhanced in the diseases with hyperimmunoglobulinemia E, disregulation of Fc alpha R is associated with certain human diseases involving the altered IgA regulation. In IgA nephropathy, which is characterized by increased serum IgA level and IgA deposition in the mesangium, there is an enhancement of the expression of Fc alpha R. In contrast, IgA failed to induce Fc alpha R significantly on the lymphocytes from the patients with selective IgA deficiency, indicating that Fc alpha R plays an important role in the IgA regulation in vivo.

Animals↗
PubMed1986

A human T cell line established from a patient with Sézary syndrome. Application for assay of human interleukin 2 (IL-2).

A human T cell line, designated Sez 627, was established from a patient with Sézary syndrome. These clonal T cells have been cultured for more than 2 years in the presence of IL-2 without any antigen stimulation. The surface phenotype of Sez 627 was OKT3+, OKT4-, OKT8+, and Tac+, and infection with human T lymphotrophic virus type I (HTLV-I) was demonstrated by Southern blot hybridization analysis. In human IL-2 assay, Sez 627 cells were found to be superior to murine CTLL-2 cells with respect to their unresponsiveness to phorbol 12-myristate 13-acetate (PMA), and species specificity for human IL-2, as well as better cryopreservation, although they were less sensitive to IL-2 than CTLL-2 cells. Using Sez 627 cells, IL-2 production by lymphocytes from patients with systemic lupus erythematosus (SLE) was examined. Decreased IL-2 production was observed in the patients with active SLE but not in most patients with inactive SLE. These findings suggest that Sez 627 is a useful human T cell line for human IL-2 assay.

Antibodies, Monoclonal↗
PubMed1986

Down-regulation of interleukin 1 (IL 1) receptor expression by IL 1 and fate of internalized 125I-labeled IL 1 beta in a human large granular lymphocyte cell line.

The regulation of interleukin 1 (IL 1) receptor expression on a human large granular lymphocyte cell line, YT, and fate of internalized 125I-labeled IL 1 beta (125I-IL 1 beta) were studied. YT cells were selected for this study, because this cell line expresses a large number of specific high-affinity receptor for IL 1, responds biologically to exogenously added IL 1 by expressing high-affinity IL 2 receptors, and does not produce IL 1. YT cells constitutively express approximately 7 X 10(3) IL 1 receptors/cell with a Kd approximately 10(-10) M. Neither IL 2, phorbol myristic acid, nor lipopolysaccharide affected the total binding of 125I-IL 1 beta by YT cells. In contrast, the capacity of YT cells to bind 125I-IL 1 beta when incubated at 37 degrees C for 3 to 16 hr with a low dose of purified IL 1 beta (approximately 6 U/ml) was reduced by greater than 80%. The loss of binding capability gradually recovered by 16 hr after removal of IL 1 beta from cultured YT cells. The apparent loss of IL 1 receptor expression was accompanied by the internalization of 125I-IL 1 beta into cells. Acid treatment of YT cells to remove bound 125I-IL 1 beta at 4 degrees C showed that 50% of the 125I-IL 1 beta bound to cells could no longer be recovered after 30 min at 37 degrees C, and this increased to 80% after 3 hr at 37 degrees C. Fractionation of cell extracts on Percoll gradient additionally showed 125I-IL 1 beta to appear intracellularly after receptor binding on plasma membranes, and to be successively transferred to some membranous organelles (d approximately equal to 1.037) through an intermediate density organelle (d approximately equal to 1.050), and to finally end up in lysosomal cell fractions (d approximately equal to 1.05 to 1.08) after approximately 3 hr at 37 degrees C. Only approximately 5% of internalized 125I-IL 1 beta was released into culture media by 6 hr of incubation at 37 degrees C. However, the radioactivity in the TCA soluble fraction of the culture media increased gradually by 6 hr and a lysosomotropic enzyme, ethylamine, significantly inhibited both the transfer of internalized 125I-IL 1 beta to the lysosomal fraction and the degradation of 125I-IL 1 beta. This study represents the first evidence of autoregulation of IL 1 receptors by IL 1 and internalization of IL 1 molecules after binding to receptors.(ABSTRACT TRUNCATED AT 400 WORDS)

Cell Line↗
PubMed1986

Construction of rat-mouse T cell hybridomas that express regulatable rat interleukin 2 receptor.

Spleen cells obtained from Lewis rats were cultured with 4 micrograms/ml Con A for 96 hr, and activated cells were fused with BW5147 mouse T lymphoma cells. Seven clones obtained by fusion expressed rat IL 2R. The expression of rat IL 2R on those hybrid cells could be up-regulated by IL 2 itself, ATL-derived factor, and TPA and CA++ ionophore. Those IL 2R could be down-regulated by murine MoAb ART-18 that detects rat IL 2R. All hybrid clones produced IL 2 constitutively. IL 2 produced by hybrid cells bound to its receptor and promoted the proliferation of hybrid cells in some clones. Incubation of cells with exogenous IL 2 resulted in the proliferation of hybrid cells, whereas the proliferation of some clones was inhibited by exogenous IL 2, indicating that IL 2 had bifunctional properties on cell growth. Rat IL 2R from 6H2-F9 hybrid cells was studied by both one- and two-dimensional SDS-PAGE with ART-18. The IL 2R derived from 6H2-F9 cells had 72,000 to 77,000 and 40,000 to 48,000 m.w. major components under nonreducing conditions, and had 50,000 to 56,000 m.w. major and 35,000 to 38,000 m.w. minor components under reducing conditions. The 110,000 m.w. component, the third component of IL 2R, was constantly observed in 6H2-F9 hybrid cells.

Animals↗