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Results for “ANTIBODY FORMATION”

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At least 217 records · Page 12Linked to original sources
PubMed1990

Isolated human growth hormone deficiency due to the hGH-I gene deletion with (type IA) and without (the Israeli-type) hGH antibody formation during hGH therapy.

Three Japanese patients with isolated growth hormone deficiency from two different families were shown to be homozygous for deletion of the structural gene for human growth hormone (hGH-I gene). These three patients had the same restriction fragment length polymorphism haplotypes. In patient No. 1, the growth rate initially responded well to pituitary human growth hormone, but growth rapidly ceased concomitantly with the development of high levels of anti-hGH antibodies. He again responded well to recombinant methionyl hGH and recombinant hGH without the methionine residue, even though having high hGH antibodies. Two siblings (Patients No. 2 and 3) showed a rather good response to pituitary hGH treatment without hGH antibodies ever being detected (the Israeli-type). hGH-I gene deletions may not necessarily result in hGH antibody formation. Heterogeneity has been observed in isolated hGH deficiency due to hGH-I gene deletion. hGH-I gene analysis should not be limited to patients with hGH antibody formation and subnormal growth responses to hGH therapy.

Adolescent↗
PubMedDate not supplied

[Age-related changes in the immune response of mouse (CBA x C57BL)F1 hybrids. II. Effect of hydrocortisone on the specific immunosuppression phenomenon and the role of nonspecific suppressor cells in the antibody formation process in old animals].

The effect of hydrocortisone on the phenomenon of specific immunosuppression and on antibody formation was studied in old mice. The decrease of immune response in the old CBA X C57BL F1 mice appears to be due to a high suppressive activity of cells-regulators which are accumulated in the spleen with senescence. It is suggested that these cells-suppressors belong to the population of non-specific T-cells sensitive to hydrocortisone. The effector T-cells-suppressors participating in specific suppression of the immune response to sheep erythrocytes in young CBA X C57BL F1 mice are resistant against hydrocortisone.

Aging↗
PubMed1977

In vitro TNP-specific antibody formation by peripheral lymphocytes from patients with systemic lupus erythematosus.

Immunological reactivity in patients with systemic lupus erythermatosus (SLE) was assessed by investigating in vitro trinitrophenyl (TNP)-specific antibody formation by peripheral lymphocytes. Peripheral lymphocytes from 16 patients with SLE were cultured with TNP conjugated with horse erythrocytes (TNP-HRBC) in the presence of 2-mercaptoethanol. The hemolytic plaque assay was used to detect hapten (TNP)-specific antibody-forming cells. Peripheral lymphocytes from normal individuals failed to produce antibody to TNP, whereas SLE lymphocytes produced a significant number of plaque-forming cells. Co-culture experiments with SLE and normal lymphocytes suggested that patients with SLE have a defect in T lymphocytes, leading to abnormal antibody production.

Adolescent↗
PubMed1975

Reaginic antibody formation in the mouse. V. Adoptive antihapten IgE antibody response of dinitrophenyl-keyhole limpet hemocyanin-primed spleen cells cultured with dinitrophenyl heterologous carrier conjugates.

DBA/1 mice were primed with dinitrophenyl-keyhole lympet hemocyanin (DNP-KLH) included in aluminum hydroxide gel, and the adoptive anti-DNP IgE antibody response of their spleen cells was studied by transfer into irradiated syngeneic mice. As expected, depletion of T cells by anti-theta antiserum and complement abolished the response of the spleen cells to homologous antigen. If the same T-depleted spleen cells were cultured with DNP-KLH for 24 hr and then transferred into irradiated mice, anti-DNP IgE antibody response was obtained. It was also found that DNP-KLH-primed spleen cells were triggered for IgE antibody response if they were cultured for 24 to 48 hr with DNP heterologous carrier conjugate, such as DNP-bovine gamma-globulin or a copolymer of D-tyrosine, glutamine, and lysine. Transfer of the cells cultured with the antigen into irradiated recipients resulted in the formation of anti-DNP IgE antibody. The DNP-KLH-primed cells cultured for 24 hr in the absence of antigen and then treated with DNP-BGG at 0 degrees C, also gave an adoptive IgE antibody response. If the same DNP-KLH-primed cells were treated with the DNP heterologous carrier conjugate at 0 degrees C or injected into irradiated recipients together with the antigen, no IgE antibody response was obtained. The results indicated that T cell dependency of the IgE antibody response is diminished by culture of DNP-KLH-primed cell for 24 to 48 hr.

Animals↗
PubMed1981

Induction of immunological tolerance to the penicilloyl antigenic determinant. III. Suppression of benzylpenicilloyl-specific IgE antibody formation by cleavable penicilloylated dextran.

The suppressive effect of cleavable penicilloylated dextran (BPO-DEX), whose directly bound penicilloyl groups undergo hydrolytic cleavage within 3 days under physiological conditions, on murine IgE antibody formation against the benzylpenicilloyl (BPO) determinant was investigated in BALB/c and C3H mice. Intraperitoneal administration of BPO-DEX during either primary or secondary IgE responses to BPO ascaris produced a reversible suppression of BPO-specific IgE, while not affecting carrier-specific IgE antibody formation. Suppression of longer duration, at least 10 weeks, was achieved, however, by repeated administrations of BPO-DEX. BPO-DEX itself did not generate detectable BPO-specific IgE antibodies. These results suggest that BPO-DEX might be one of the promising tolerogens in the prevention of penicillin allergy.

Animals↗
PubMed1971

Antibody formation in rabbits adapted and nonadapted to high altitude.

Antibody formation in high-altitude-acclimatized and nonacclimatized rabbits was investigated at altitudes of 14,100 (Pikes Peak, Colo.) and 5,330 (Denver, Colo.). Serum pools representing samplings of primary response were titered before and after treatment with 2-mercaptoethanol. Peak titers of 2-mercaptoethanolresistant and -sensitive humoral antibodies were higher in the animals adapted to an altitude of 14,100 ft and in nonadapted animals than in animals maintained at 5,330 ft.

Journal Article↗
PubMed1987

Supplemental zinc (Zn2+) restores antibody formation in cultures of aged spleen cells. II. Effects on mediator production.

In vitro antibody production to T-dependent erythrocyte antigens is depressed as a function of age. Supplementation of antibody-forming cultures with the essential trace element zinc restores the capacity of cells from immunodepressed, aged mice to generate an antibody response. Zn2+ produces maximal enhancement of immune function when it is added to the cultures within the first 24 h. Supernatants obtained from cultures supplemented with zinc from 0-24 h contain soluble, nondialyzable factors which support enhanced antibody production in fresh cultures of cells from aged mice. Interleukin 2 levels in the supernatants from Zn2+-supplemented cultures were not increased. However, the levels of interleukin 1 were increased approximately 300% over nonsupplemented controls and these increases corresponded with the ability of the supernatants to support antibody formation. Further studies showed that, in addition to enhancing the production of interleukin 1, Zn2+ enhanced the ability of concanavalin A-activated T cells from aged mice to produce B cell stimulatory factor-1.

Aging↗
PubMed1976

[Mechanism of antibody formation suppression in high density suspension cultures].

There was a sharp decrease in the number of antibody producing cells formed in induction of primary immune reaction in vitro with increase of surface density (number of cells per 1 cm2 of the bottom of the incubation vessel); the cause of this phenomenon was studied. It was shown that depression of antibody formation in dense cultures was associated not with disturbance of the induction of the clone of antibody-forming cells, but with the inhibition of the subsequent proliferation of the cells of this clone. Disturbance of proliferation was reversible: a reduction of the density of the cultures 1 or 3 days after the beginning of the incubation led to the restoration of the growth of the number of antibody-producing cells. The depressive effect could not be transferred by humoral way from the cultures with a high density to the cultures with a low density; it could not be eliminated by daily replacement of the incubation medium in dense cultures for a fresh nutrient medium.

Animals↗
PubMed1988

Effect of a new antirheumatic drug (CGS10787B) on antibody formation and delayed-type hypersensitivity in BALB/c mice.

The effect of CGS10787B on antibody formation and cell-mediated (delayed-type) hypersensitivity in BALB/c mice was examined by using the haemolytic plaque-forming cell assay and the delayed-type footpad reaction with the assay of T-cell subsets. CGS10787B at doses of 5, 25 and 100 mg/kg p.o. enhanced spleen haemolytic plaque-formation on day 4, and spleen rosette-formation on day 5 after immunization. In the assay of T-cell subsets, CGS10787B at the dose of 100 mg/kg reduced the Lyt-23 positive cell subset. In type III hypersensitivity, CGS10787B at doses of 5, 25 and 100 mg/kg p.o. for 6 days reduced dose-relatedly the footpad swelling of the immunized mouse. In type IV hypersensitivity, CGS10787B at doses of 5, 25 and 100 mg/kg p.o. for 6 days diminished dose-dependently the footpad swelling augmented by cyclophosphamide pretreatment. In the assay of T-cell subsets, CGS10787B at doses of 25 and 100 mg/kg increased the Thy-1 positive cell subset. These findings suggest that CGS10787B has an influence on the immune systems, acting on the function of T lymphocytes as well as on the inflammatory process in immunized animals.

Animals↗
PubMed1997

The missense mutation Arg593 --> Cys is related to antibody formation in a patient with mild hemophilia A.

The development of inhibitory antibodies to factor VIII in patients affected by a mild form of hemophilia A (factor VIII > 0.05 IU/mL) is considered a rare event. In this study, we evaluated the relationship between genotype and anti-factor VIII antibody formation in a patient with mild hemophilia A. Mutation analysis showed that a missense mutation in the factor VIII gene leading to replacement of Arg593 by Cys in the A2 domain of factor VIII was associated with hemophilia A in this patient. The anti-factor VIII antibodies present in the patient's plasma were characterized using metabolically labeled factor VIII fragments expressed in insect cells. The anti-factor VIII antibodies, composed of subclasses IgG2 and IgG4, reacted with both the fragment corresponding to the factor VIII heavy chain and the A2 domain. The Arg593 --> Cys substitution was introduced into the cDNA encoding the A2 domain of factor VIII and the resulting construct was expressed in insect cells. Strikingly, the metabolically labeled A2 domain carrying the Arg593 --> Cys mutation was not recognized by the anti-factor VIII antibodies present in the plasma of the patient. These data indicate that the anti-factor VIII antibodies are exclusively directed against exogenous factor VIII. This strongly suggests that the Arg593 --> Cys substitution results in recognition of wild-type factor VIII as nonself and is thereby related to the formation of anti-factor VIII antibodies after factor VIII replacement therapy in this particular patient.

Adult↗