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Related Experiment Videos

Growth-modulating plasma tripeptide may function by facilitating copper uptake into cells

L Pickart, J H Freedman, W J Loker

    Nature
    |December 25, 1980
    PubMed
    Summary

    The plasma tripeptide glycyl-L-lysine (GHL) binds copper and enhances its uptake into cells. This suggests GHL may function as a copper transport factor, influencing cellular processes.

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    Area of Science:

    • Biochemistry
    • Cell Biology
    • Molecular Biology

    Background:

    • Plasma tripeptide glycyl-L-lysine (GHL) exhibits diverse cellular effects at nanomolar concentrations.
    • GHL co-isolates with copper and iron, suggesting a potential interaction.
    • Similarities between GHL and copper-binding sites on albumin and alpha-fetoprotein hint at a role in metal transport.

    Purpose of the Study:

    • To investigate the role of glycyl-L-lysine (GHL) in cellular copper uptake.
    • To determine if GHL can act as a copper transport factor.
    • To explore the biochemical function of GHL in cultured systems.

    Main Methods:

    • Isolation and purification of GHL.
    • Structure-function studies of GHL analogs.
    • Copper-binding assays.

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  • Measurement of copper uptake in hepatoma cells (HTC4).

    • Main Results:

    • GHL readily forms complexes with copper(II).
    • GHL significantly enhances copper uptake into cultured hepatoma cells.
    • Tripeptides with a histidyl-lysyl linkage show activity similar to GHL.

    Conclusions:

    • Glycyl-L-lysine (GHL) functions as a copper transport factor.
    • GHL facilitates the cellular uptake of copper.
    • The findings suggest a fundamental role for GHL in cellular copper homeostasis and metabolism.