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Related Experiment Videos

Epidermal growth factor: uptake and fate.

P Cuatrecasas

    Ciba Foundation Symposium
    |January 1, 1982
    PubMed
    Summary

    Epidermal growth factor (EGF) receptors internalize continuously, with degradation essential for cell growth. Receptor dimerization may trigger long-term effects, independent of ligand binding.

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    Area of Science:

    • Cell Biology
    • Molecular Biology
    • Biochemistry

    Background:

    • Epidermal growth factor (EGF) receptors mediate cellular responses.
    • EGF receptor lateral diffusion and endocytosis are key processes.

    Purpose of the Study:

    • To investigate the dynamics and functional significance of EGF receptors.
    • To understand the role of receptor internalization and degradation in mitogenesis.

    Main Methods:

    • Fluorescence-labeled EGF analogues.
    • Fluorescence photobleaching recovery.
    • High image-intensified fluorescent microscopy.
    • Cell culture at 37°C and 4°C.

    Main Results:

    • EGF receptors diffuse laterally, form patches, and undergo endocytosis.
    • Internalization and lysosomal degradation of EGF receptors occur continuously.
    • Interference with degradation blocks mitogenesis.
    • Receptor dimerization may be necessary for long-term effects and endocytosis.
    • EGF receptors convert from low to high affinity states, requiring protein synthesis.

    Conclusions:

    • EGF receptor degradation is essential for mitogenesis.
    • Submicroscopic receptor aggregation (dimerization) is crucial for long-term signaling.
    • Ligand-independent mitogenic responses can be triggered by anti-receptor antibodies.
    • Intracellular accumulation of EGF-receptor complexes may regulate cellular growth and tumor promotion.

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