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beta-Endorphin: surface binding and internalization in thymoma cells.

L Schweigerer, W Schmidt, H Teschemacher

Proceedings of the National Academy of Sciences of the United States of America

|September 1, 1985

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The opioid peptide beta-endorphin binds to thymoma cell surface receptors and is internalized, suggesting intracellular modulation of T-lymphocyte proliferation.

Area of Science:

Immunology
Neuroendocrinology
Cell Biology

Background:

The opioid peptide beta-endorphin is known to interact with specific binding sites.
Thymoma cells possess surface receptors that bind beta-endorphin.

Purpose of the Study:

To investigate the binding and internalization mechanism of beta-endorphin on thymoma cells.
To explore the intracellular location and potential function of internalized beta-endorphin.

Main Methods:

Characterization of nonopioid binding sites (Mr 72,000) on thymoma cell surfaces.
Tracking the internalization of beta-endorphin within thymoma cells.
Assessing the regulation of Mr 72,000 binding sites following beta-endorphin exposure.

Main Results:

Related Experiment Videos

Beta-endorphin binds to specific Mr 72,000 nonopioid binding sites on thymoma cells.
Beta-endorphin is internalized into intracellular vesicular structures via these binding sites.
Internalization leads to the down-regulation of the Mr 72,000 binding sites.

Conclusions:

Beta-endorphin internalization suggests a role in intracellular signaling pathways.
The findings indicate that beta-endorphin may modulate cellular functions, like T-lymphocyte proliferation, intracellularly.
This intracellular action contrasts with typical cell surface receptor-mediated effects.