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Biomedical subjects

T Uede

Publications and source records attributed to T Uede.

At least 199 records · Page 11Linked to original sources
PubMed1984

Suppression of IgE synthesis in mouse plasma cells and B cells by rat IgE-suppressive factor.

Rat IgE-binding factors were assessed for the ability to regulate the IgE response of mouse spleen cells. A rat-mouse T cell hybridoma, 23B6, produced two species, i.e., 15,000 (15K) daltons and 30K daltons, of rat IgE-binding factors upon incubation with rat IgE. The 15K IgE-binding factor selectively suppressed the in vitro IgE response of DNP-KLH-primed BALB/c spleen cells to homologous antigen without affecting the IgG1 response, whereas the 30K IgE-binding factor failed to affect both the IgE and IgG1 responses. Incubation of IgE-producing hybridoma cells with the 15K IgE-binding factor resulted in a parallel decrease in the proportion of IgE-secreting cells, cytoplasmic IgE-containing cells, and sIgE+ cells. The same IgE-binding factor suppressed IgE formation by mouse plasma cells in DNP-KLH-primed or KLH-primed BDF1 mice without affecting the IgG1-forming cells. In contrast, the 30K IgE-binding factor failed to affect the formation of IgE by the hybridoma and the plasma cells. It was also found that incubation of the splenic lymphocytes with the 15K IgE-binding factor resulted in a decrease in sIgE+ B cells; the 30K IgE-binding factor failed to do so. The results indicate that the binding of the 15K IgE-binding factor to plasma cells and to sIgE+ B cells results in suppression of IgE synthesis in these cells.

Animals↗
PubMed1984

Lymphoid cell subpopulations infiltrating into autologous rat tumors undergoing rejection.

Lymphoid cell subpopulations infiltrating into autografts of methylcholanthrene-induced sarcomas in rats immunized with autologous tumor cells were identified in terms of immunohistochemical and cytofluorographic techniques using various monoclonal antibodies raised against different classes of rat lymphohemopoietic cells. These antibodies included in this study directed to rat T-cell antigens corresponding to mouse Lyt-1 (RLyt-1) and Lyt-2,3 antigens (RLyt-2) and to W3/25 antigen expressed on a particular subset of rat T-cells with helper function, as well as to rat granulocyte-macrophage-specific antigen (RGM-1). Histological studies demonstrated that the autografts of highly antigenic tumors introduced to the primary hosts were completely rejected following massive immigration of lymphoid cells into the tumor sites, which was not observed in progressively growing, minimally antigenic tumors. These lymphoid cells found within regressing highly antigenic tumor autografts were identified mostly to be T-cells bearing RLyt-1 (approximately 70%), and more than two-thirds of these T-cells expressed RLyt-2 antigen. In contrast to T-cells, macrophages and B-cells, each of which could be recognized by the presence of either RGM-1 antigen or immunoglobulin on their cell surfaces, appeared to have a minimal role in the rejection of autochthonous tumors, as reflected by their less frequent appearance within the tumor tissues during the rejection process.

Animals↗
PubMed1983

IgE-binding factors from mouse T lymphocytes. I. Formation of IgE-binding factors by stimulation with homologous IgE and interferon.

Incubation of normal mouse spleen cells with homologous IgE resulted in the formation of soluble factors that inhibited rosette formation of mouse Fc epsilon R+ cells with IgE-coated ox erythrocytes. The soluble factors could be absorbed with mouse or rat IgE coupled to Sepharose and recovered from the beads by acid elution. However, the factors had no affinity for either human IgE or mouse IgG. The IgE-binding factors were derived from T cells. Production of the factors required Lyt1+ T cells and Fc gamma R+ cells, which suggests that the factors are derived from Fc gamma R+ Lyt 1+ T cells. The molecular size of IgE-binding factors was approximately 15,000 daltons. When IgE-binding factors were formed by BALB/c spleen cells, nearly one-half of the factors had affinity for lentil lectin, and the remaining half of the factors failed to bind to the lectin. The proportion of the two species of IgE-binding factors differed depending on mouse strains. The majority of the factors formed by B6D2F1 spleen cells had affinity for lentil lectin, but those formed by SJL spleen cells failed to bind to the lectin. The IgE-binding factors were also induced by incubation of normal spleen cells with polyinosinic-polycytidylic acid (pI:pC). The nucleotide stimulated splenic adherent cells to form "inducers" of IgE-binding factors, which in turn induced normal lymphocytes to form IgE-binding factors. The inducers of IgE-binding factors were inactivated (or neutralized) by antibodies specific for mouse Type I interferon. It was also found that purified mouse beta interferon could induce the formation of IgE-binding factors. IgE-binding factors induced by pI:pC consisted of two different molecules: one had a m.w. of 15,000 daltons, and another had a m.w. of between 40,000 and 60,000 daltons.

Animals↗
PubMed1983

Modulation of the biologic activities of IgE-binding factors. III. Switching of a T cell hybrid clone from the formation of IgE-suppressive factor to the formation of IgE-potentiating factor.

Incubation of rat-mouse T cell hybridoma cells, 23B6, with rat immunoglobulin E (IgE) results in the formation of the 15,000-dalton IgE-suppressive factor and the 30,000-dalton IgE-binding factor, which has neither potentiating activity nor suppressive activity on the IgE response. Another T cell hybridoma, 23A4 cells, produces the 30,000-dalton "inactive" IgE-binding factor upon incubation with IgE. Both the 15,000-dalton IgE-suppressive factor and the 30,000-dalton IgE-binding factor lacked affinity for lentil lectin but bound to peanut agglutinin. When the 23B6 cells were incubated with IgE in the presence of lysolecithin, the majority of the 15,000-dalton IgE-binding factor formed by the cells gained affinity for lentil lectin, and this factor selectively potentiated the IgE response. The glycosylation-enhancing factor, which was formed by stimulation of normal spleen cells with lymphocytosis-promoting factor (LPF or pertussigen), also switched 23B6 cells from the formation of IgE-suppressive factor to the formation of IgE-potentiating factor. It was also found that the 30,000-dalton "inactive" IgE-binding factor, formed by both 23B6 and 23A4 cells, gained the ability to potentiate the IgE response, when the cells were cultured with IgE in the presence of glycosylation-enhancing factor. The results indicate that IgE-potentiating factor and IgE-suppressive factor share common precursors, and that biologic activities of IgE-binding factors are decided by their carbohydrate moieties. Incubation of the two hybridoma cells with lysolecithin or glycosylation-enhancing factor results in an increase in the proportion of FC epsilon R+ cells, suggesting that the assembly of N-linked oligosaccharide to precursor molecules is intrinsic for the expression of FC epsilon R.

Animals↗
PubMed1983

B-cell malignancies and differentiation antigens defined with monoclonal antibodies.

Monoclonal antibodies directed to B-cell lineage were produced. They were characterized by their reactivity with a variety of human hematopoietic cell lines and normal lymphoid cells and by the immunohistological distribution of cells positive for the antibodies. Some of them were specific for B-cell lineage at various stages of B-cell differentiation and some were, in addition, cross-reactive with other cell lineages. These newly produced antibodies were utilized to dissect and characterize B-cell malignancies and were applied for classification of B-cell malignancies.

Animals↗
PubMed1983

Modulation of the biologic activities of IgE-binding factors. I. Identification of glycosylation-inhibiting factor as a fragment of lipomodulin.

Splenic T lymphocytes of rats treated with complete Freund's adjuvant (CFA) spontaneously release a lymphokine that inhibits the glycosylation of IgE-binding factors during their biosynthesis and provides the factors with biologic activity: selective suppression of the IgE response. The lymphokine, which is called glycosylation-inhibiting factor, also prevents IgE-induced increases in Fc epsilon R+ cells. The glycosylation inhibiting factor is formed by stimulation of BCG-primed spleen cells with PPD and participates in the selective formation of IgE-suppressive factors. The lymphokine is derived from OX 8+ T cells in both the CFA and BCG systems. The glycosylation-inhibiting factor is a 16,000-dalton peptide, as estimated by gel filtration, and specifically binds to monoclonal antibody against lipomodulin, a phospholipase inhibitory protein. Furthermore, "lipomodulin" was detected by radioimmunoassay in the 16,000-dalton fraction that contained glycosylation inhibiting factor. The fraction did not inhibit phospholipase A2 but after alkaline phosphatase treatment, the fraction did inhibit phospholipase A2. Furthermore, purified lipomodulin obtained from glucocorticoid-treated rabbit neutrophils had the same biologic activities as glycosylation inhibiting factors; i.e., it inhibited both protein glycosylation of IgE-binding factors and IgE-induced expression of Fc epsilon R. The results collectively indicate that glycosylation-inhibiting factor is a fragment of phosphorylated lipomodulin.

Animals↗
PubMed1983

Modulation of the biologic activities of IgE-binding factor. II. Physicochemical properties and cell sources of glycosylation-enhancing factor.

T lymphocytes of rats treated with Bordetella pertussis vaccine (BP) formed a soluble factor that enhanced the glycosylation of IgE-binding factors during their biosynthesis, and provided the latter factors with the biologic activity to potentiate the IgE response. The present experiments demonstrated that pertussigen (leukocytosis-promoting factor) from BP induced normal rat spleen cells to form the glycosylation-enhancing factor. The same factor was obtained by incubation of normal spleen cells with 5 micrograms/ml, but not 2 micrograms/ml, concanavalin A. When normal rat mesenteric lymph node cells were incubated with the glycosylation-enhancing factor together with IgE, IgE-binding factors formed by the cells selectively potentiated the IgE response. The IgE-binding factors formed by the same cells upon incubation with IgE alone neither enhanced nor suppressed the IgE response. The glycosylation-enhancing factor changed the nature of IgE-binding factors formed by the rat-mouse T cell hybridoma, 23A4. IgE-binding factors induced by IgE alone lacked affinity for lentil lectin, whereas those induced by IgE in the presence of the glycosylation-enhancing factor had affinity for the lectin. The cell source of the glycosylation-enhancing factor appeared to be W 3/25+ Fc gamma R+ T cells. The glycosylation-enhancing factor was protein in nature and had a m.w. of about 25,000. The factor had affinity for acid-treated Sepharose and could be recovered from the beads by elution with lactose. The factor was different from interleukin 2 with respect to both its affinity for galactose and its isoelectric point.

Animals↗
PubMed1983

[Hypothalamic histiocytosis X--report of a case].

Histiocytosis X is a non-neoplastic disorder of unknown etiology characterized by a mass of proliferating histocytes, plasma cells and inflammatory cells forming a granuloma within the reticuloendothelial elements of any organ system in the body. The three clinical syndromes of this condition, eosinophilic granuloma, Hand-Schüller-Christian disease and Letterer-Siwe disease were unified into a single nosological entity by Lichtenstein in 1953. The complication of the central nervous system is shown in the cerebrum, cerebellum, sella turcica, hypothalamus and so on. Hypothalamic histiocytosis X is often found in cases of disseminated histiocytosis X, but an isolated histiocytosis X of the hypothalamus is very rare. Including our case, 16 cases of hypothalamic histiocytosis X were reviewed in this paper. Age at onset was older than disseminated histiocytosis X. The sex ratio was almost equal. Diabetes insipidus was equally found as in other suprasellar masses and it was important as an initial symptom. The CT finding was shown as a homogeneously enhanced mass but no specific finding of CT was seen as suprasellar histiocytosis X. Therefore, differential diagnosis was very difficult. Treatments for this disease were variable. Chemotherapy, irradiation or combination of both were reported. The combination therapy was thought to be the most effective treatment. The relation between this disease and disseminated histiocytosis X is not known. But possibility of transformation of this disease into disseminated histiocytosis X was reported in some papers. Therefore, early diagnosis by biopsy of the hypothalamic lesion was stressed.

Adult↗
PubMed1982

Thy-1 antigen on rat bone marrow cells: immunochemical and fine morphological studies.

Immunochemical and fine morphological studies were conducted to clarify molecular characteristics of Thy-1 antigen on rat bone marrow cells and cell types expressing Thy-1 in rat bone marrow. For this purpose, a xenoantiserum highly specific for Thy-1 was prepared by immunizing rabbits with partially purified Thy-1 glycoprotein from rat brains. This antiserum reacted with approximately 90% of thymocytes, 10% of spleen cells, 30% of bone marrow cells and less than 2% of lymph node cells in normal rats, and the similar reactivity of this serum was also observed with spleen, lymph node and bone marrow cells obtained from congenitally athymic (rnu/rnu) rats. The anti-Thy-1 serum used in this study, as well as anti-asialo GM1, showed cytotoxic effect on natural killer (NK) cells in rats, suggesting that the NK cells, unlike those cells in mice, express both Thy-1 and asialo GM1. Immunoelectron microscopic observation performed on Thy-1 positive rat bone marrow cells showed that Thy-1 was expressed on immature cells ancestral to erythrocytes or granulocytes and on possible pluripotent hemopoietic stem cells as well as on bone marrow lymphocytes. It seems likely that an inverse relationship exists between Thy-1 expression and maturation of rat bone marrow cells including erythrocytic, granulocytic and lymphocytic cell series. Thy-1 antigen defined by our antiserum on rat bone marrow cells appears to be a sialoglycoprotein with 24 K molecular weight, which could be labeled by periodate-tritiated borohydride. The same antiserum precipitated a 27 K molecular weight sialoglycoprotein from rat thymocytes, which was regarded as the same molecular species as the 24 K molecular weight glycoprotein on rat bone marrow cells on the basis of data obtained from absorption studies.

Animals↗
PubMed1982

Formation of rat IgE-binding factors by rat-mouse T cell hybridomas.

Mesenteric lymph node (MLN) cells of rats infected with Nippostrongylus brasiliensis (Nb) were obtained 8 days after infection and were incubated overnight with rat IgE for the formation of IgE-binding factors. These cells were then fused with BW 5147 mouse T lymphoma cells. Two hybrid clones (A4 and B6) obtained by the fusion formed IgE-binding factors upon incubation with IgE. It was found that 1-hr incubation with 3 micrograms/ml of rat IgE was sufficient to induce hybridoma cells to form IgE-binding factors. Both hybrid clones express rat T cell markers; the A4 clone bears Fc epsilon R, whereas the B6 clone bears Fc gamma R on their surface. The IgE-binding factors formed by both clones bound to rat IgE-coated Sepharose and could be eluted from the beads at pH 3.0. The factors also have affinity for mouse IgE but not human IgE nor rat IgG. IgE-binding factors formed by the A4 clone had a m.w. between 26,000 and 30,000; the B6 clone formed IgE-binding factors of 26,000 and 13,000 daltons. The factors of both high and low m.w. failed to bind to lentil lectin and Con A, but had affinity for peanut agglutinin. Purified IgE-binding factors of 13,000 daltons selectively suppressed the IgE-forming cell response of DNP-ovalbumin-primed MLN cells to homologous antigen, whereas the factor of 26,000 to 30,000 daltons neither suppressed nor enhanced the IgE response.

Animals↗
PubMed1982

Formation of IgE-binding factors by rat T lymphocytes. V. Effect of adjuvant for the priming immunization on the nature of IgE binding factors formed by antigenic stimulation.

Rats were immunized with keyhole limpet hemocyanin (KLH) included in complete Freund's adjuvant (CFA) or with the same antigen absorbed to aluminum hydroxide gel. Incubation of their spleen and MLN cells with homologous antigen resulted in the formation of IgE-binding factors. The nature of IgE-binding factors formed by antigenic stimulation was different depending on the adjuvant employed for priming and the period after immunization. If the lymphoid tissues were obtained 2 to 4 wk after antigen priming, IgE-binding factors derived from lymphoid tissues of KLH-alum-primed animals selectively potentiated the IgE response, whereas those produced by the lymphoid tissues of KLH-CFA-primed animals suppressed the IgE response. Analysis of purified IgE-binding factors from KLH-primed spleen cells revealed that the factors were heterogeneous with respect to their m.w., and that IgE-binding factors of a m.w. of 13,000 were responsible for the biologic activities. Thus, the 13,000-dalton factors obtained from KLH-alum-primed spleen cells selectively potentiated the IgE response, and those from KLH-CFA-primed spleen cells suppressed the IgE response. The selective formation of either IgE-potentiating factors or IgE-suppressive factors by KLH-primed spleen cells was observed only when the cells were stimulated by specific antigen. When the same KLH-primed spleen cells were incubated with IgE, IgE-binding factors formed in the cultures neither potentiated nor suppressed the IgE response. It was also found that stimulation of a mixture of BCG-primed spleen cells and KLH-alum-primed spleen cells with PPD resulted in the formation of IgE-suppressive factors; the stimulation of the same mixed cell suspension with KLH resulted in the formation of IgE-potentiating factors. The results collectively indicate that the nature of IgE-binding factors is decided by antigen-primed cells.

Adjuvants, Immunologic↗
PubMed1982

Formation of IgE-binding factors by rat T lymphocytes. VI. Cellular mechanisms for the formation of IgE-potentiating factor and IgE-suppressive factor by antigenic stimulation of antigen-primed spleen cells.

Analysis of cellular mechanisms of formation of IgE-binding factors by KLH-primed spleen cells revealed that the presentation of KLH to KLH-primed T cells by adherent cells resulted in the formation of lymphokines that in turn stimulated unprimed lymphocytes to form IgE-binding factors. Lymphokines released from KLH-alum-primed spleen cells induced normal lymphocytes to form IgE-potentiating factors, whereas those released from KLH-CFA-primed spleen cells induced the formation of IgE-suppressive factors. Fractionation of the lymphokines from KLH-primed spleen cells and analysis of cell sources of the lymphokines revealed that multiple factors are involved in the selective formation of one or the other IgE-binding factors. Thus, KLH-alum primed splenic T cells from "inducers" of IgE-binding factors and glycosylation-enhancing factors upon antigenic stimulation, and these factors in combination stimulate unprimed W 3/25+ Fc gamma R+ T cells to form IgE-potentiating factors. Antigenic stimulation of KLH-CFA-primed T cells results in the formation of the "inducers" and glycosylation-inhibiting factors, and these two lymphokines collectively stimulate unprimed W 3/25+ Fc gamma R+ T cells to form IgE-suppressive factors. Cell sources of "inducers" are W 3/25+ Fc gamma R- T cells, cells different from the source of IgE-binding factors. The glycosylation-enhancing factor is derived from W 3/25+ F gamma R+ T cells in KLH-alum-primed spleen; the glycosylation-inhibiting factor is derived from OX 8+ T cells in KLH-CFA-primed spleen. Evidence was obtained that these lymphokines, which modulate the protein glycosylation of IgE-binding factors during their biosynthesis, are derived from antigen-primed T cells and determine the nature of IgE-binding factors formed.

Animals↗
PubMed1982

[Antibodies against human lymphocytes].

The introduction of hybridoma technology has greatly contributed to the identification and the characterization of a variety of cell surface antigens present on human lymphoid cells. Rapid progress has recently been made in generating monoclonal antibodies against human lymphoid cells and extensive studies in clinical medicine have defined the potential application of these monoclonal antibodies. In this review, we summarize the main similarities and differences among these monoclonal antibodies.

Animals↗
PubMed1981

Human thymus antigen: characterization and its expression on human leukemias.

Specific anti-human thymus xenoantiserum (ATS) was utilized for characterizing a human thymus antigen (HTA) preferentially expressed on human thymocytes. Binding of ATS with different cell types was studied by immunofluorescence and immunoperoxidase techniques, as well as by radioimmunoprecipitation (RIP) followed by SDS-polyacrylamide gel electrophoresis (SDS-PAGE). ATS reacted selectively with the majority (87%) of human thymocytes among normal lymphoid cell populations tested. In the thymus, HTA was expressed largely on cortical thymocytes but not on those cells located in the thymic medulla. When 20 cases of different types of lymphatic leukemias were studied with ATS, HTA was found on acute lymphoblastic leukemia cells rosetting with sheep erythrocytes (T-ALL) but not on other lymphatic leukemia cases, including chronic lymphocytic leukemia cells rosetting with sheep red blood cells (T-CLL). SDS-PAGE analysis of immunoprecipitates formed between ATS and radiolabeled cell-surface components of human thymocytes demonstrated that ATS bound a 48,000-molecular-weight component that could be adsorbed to Sepharose 4B coupled with Les culinaris hemagglutinin and could be labeled by periodate-tritiated borohydride, indicating that HTA is a sialoglycoprotein. Similar antigen molecules were also precipitated by ATS from T-ALL cells but not from other lymphatic leukemia cells. Five T-ALL-derived cell lines were tested with ATS by immunofluorescence and by RIP and SDS-PAGE, but only two cell lines (MOLT-3 and P12/Ich) possessed HTA molecules on their cell membrane.

Animals↗
PubMed1981

Immunohistochemical study of lymphocytes in rat pineal gland: selective accumulation of T lymphocytes.

Morphologic and immunohistochemical studies were performed to examine the existence of lymphocytes in the brain of rats. Special attention was paid to the time course of the appearance of lymphocytes in and around the pineal gland. Rabbit anti-rat T cell and anti-rat immunoglobulin sera were used for identification of T and B cells in tissue sections. Immunoperoxidase and immunofluorescence techniques were employed to identify cells reacting with anti-T and anti-immunoglobulin sera. No lymphocytes were found in the brain of rats until 20 days after birth. Small clusters of lymphocytes appeared in the pineal region by 30 days of age, after which they gradually increased in number, forming massive clusters in the pineal region by 120 days. Along with an increase in the number of lymphocytic cells, there was a gradual increase of cells reacting with anti-T cell serum. These T cells were only a minority of pineal lymphocytes in younger animals, but 90% or more cells were stained by anti-T cell serum at 120 days after birth. The remaining cells did not react with anti-immunoglobulin sera either. These findings suggest that the gradual increase of T lymphocytes in the rat pineal region is a simple reflection of the normal course of maturation of T cells, and the pineal gland in the rat may have some role in immune responses within the brain.

Aging↗