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Related Experiment Videos

Cyclosporin receptor on mouse lymphocytes

B Ryffel, P Donatsch, U Götz

    Immunology
    |December 1, 1980
    PubMed
    Summary

    This study characterized [3H]-cyclosporin C binding on mouse lymphocytes, finding saturable, high-affinity sites. Lymphocyte binding capacity varied by organ, with erythrocytes showing no specific binding.

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    Area of Science:

    • Immunology
    • Pharmacology
    • Cell Biology

    Background:

    • Cyclosporin C is an immunosuppressive oligopeptide.
    • Understanding its binding characteristics is crucial for therapeutic applications.

    Purpose of the Study:

    • To characterize the specific binding of [3H]-cyclosporin C on various mouse lymphocytes.
    • To determine the affinity and capacity of these binding sites.

    Main Methods:

    • Radioligand binding assays using [3H]-cyclosporin C.
    • Saturation, time-dependency, and reversibility studies.
    • Computerized data analysis to identify binding site populations.

    Main Results:

    • Specific binding of [3H]-cyclosporin C was saturable, time-dependent, and reversible.
    • High-affinity binding sites (KD = 1.5 x 10(-7) M) were identified on thymocytes.
    • Binding capacity (Bmax) varied across lymphocyte populations: thymus > spleen > mesenteric lymph node (T cells) > mesenteric lymph node (B cells).
    • Erythrocytes exhibited no specific binding.

    Conclusions:

    • Mouse lymphocytes possess specific, high-affinity binding sites for cyclosporin C.
    • The distribution and density of these sites differ among lymphocyte populations.
    • These findings contribute to understanding cyclosporin C's mechanism of action and distribution.

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