Publications by authors named "T Staehelin"

Jerne's success in developing the plaque-forming cell methodology for determining the number of specific antibody-producing lymphocytes during the immune response has prompted scientists to calculate the number of antibody molecules produced by a single cell. In this article, calculations of the rate of antibody production are made, and a special attention is called to the number of ribosomes in a cell, the rate of protein chain elongation and various other parameters. The generally accepted notion of 2000 IgM molecules or some 15,000 IgG molecules per second (per cell) remains an acceptable estimate.

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The efficacy, pharmacodynamics, and pharmacokinetics of CGP 51901, a recombinant monoclonal mouse-human chimeric anti-human immunoglobulin E (IgE) antibody were evaluated for 153 patients with seasonal allergic rhinitis treated with placebo or with 15, 30, or 60 mg CGP 51901 in six biweekly doses. Seasonal allergic rhinitis was chosen to validate the concept of anti-IgE therapy because the causal and temporal relation between allergen confrontation and IgE-mediated evocation of symptoms is firmly established. A sustained 85% or greater reduction of serum free IgE levels was shown to be effective in improving clinical symptoms.

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CGP 51901 is a non-anaphylactogenic mouse/human chimeric anti-human IgE antibody that binds to free IgE and surface IgE of IgE-expressing B cells but not to IgE bound to high affinity IgE receptors (Fc epsilonR1) on mast cells and basophils or low affinity IgE receptors (Fc epsilonR2) on other cells. A phase 1 double-blind, placebo-controlled, single dose study with doses of 3, 10, 30, and 100 mg of CGP 51901 was conducted in 33 pollen-sensitive subjects who had raised levels of serum IgE and received either intravenous CGP 51901 or placebo. The administration of CGP 51901 was well tolerated and resulted in a decrease of serum free IgE levels in a dose-dependent manner, with suppression after 100 mg of CGP 51901 reaching > 96%.

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We investigated in which form lipopolysaccharide (LPS) is released from live bacteria incubated with human serum and whether the released LPS can interact with high density lipoprotein (HDL), the main transport protein for purified LPS in circulation. Live biotinylated Salmonella abortus equi bacteria were incubated with fresh serum (37 degrees C; 2 h). The released LPS was isolated by immunoprecipitation or immunoabsorption using specific anti-O antibodies.

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