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ABSTRACT The plasma tripeptide glycyl-L-histidyl-L-lysine (GHL), when added at nanomolar concentrations to a wide group of cultured systems, produces a disparate set of responses ranging

from the stimulation of growth and differentiation to outright toxicity1–3. Such diverse actions imply that this tripeptide mediates some basic biochemical function common to many types of

cells and organisms. During the isolation of GHL we found the compound to co-isolate through a number of steps with approximately equimolar copper and about 1/5 molar iron1. Maximal effects

on hepatoma cells (HTC4) were seen when the peptide was added with copper and iron to the growth medium1. Structure–function studies revealed that several tripeptides with a histidyl-lysyl

linkage were nearly as active as GHL1. The association of GHL with copper and a homology similarity between the tripeptide and the copper transport sites on albumin and _α_-fetoprotein,

where the cupric atom is bound to a histidyl residue adjacent to a basic residue, suggested that GHL may act as a copper transport factor4. We report here that the tripeptide readily forms

complexes with copper(II) and enhances the uptake of the metal into cultured hepatoma cells. Access through your institution Buy or subscribe This is a preview of subscription content,

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IRON MOBILIZATION BY SMALL MOLECULES Article 25 April 2024 A C-PEPTIDE COMPLEX WITH ALBUMIN AND ZN2+ INCREASES MEASURABLE GLUT1 LEVELS IN MEMBRANES OF HUMAN RED BLOOD CELLS Article Open

access 15 October 2020 STRUCTURE OF HEPCIDIN-BOUND FERROPORTIN REVEALS IRON HOMEOSTATIC MECHANISMS Article 19 August 2020 REFERENCES * Pickart, L. & Thaler, M. _Nature new Biol._ 243,

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(1979). Article  CAS  Google Scholar  Download references AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Virginia Mason Research Center, Seattle, Washington, 98101 Loren Pickart * Department

of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York, 10461 Jonathan H. Freedman & Jack Peisach * Department of Chemistry, University of Washington, Seattle,

Washington, 98195 W. John Loker, Christopher M. Perkins & Boris Weinstein * Department of Biological Structure, University of Washington, Seattle, Washington, 98195 Ronald E. Stenkamp

Authors * Loren Pickart View author publications You can also search for this author inPubMed Google Scholar * Jonathan H. Freedman View author publications You can also search for this

author inPubMed Google Scholar * W. John Loker View author publications You can also search for this author inPubMed Google Scholar * Jack Peisach View author publications You can also

search for this author inPubMed Google Scholar * Christopher M. Perkins View author publications You can also search for this author inPubMed Google Scholar * Ronald E. Stenkamp View author

publications You can also search for this author inPubMed Google Scholar * Boris Weinstein View author publications You can also search for this author inPubMed Google Scholar RIGHTS AND

PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Pickart, L., Freedman, J., Loker, W. _et al._ Growth-modulating plasma tripeptide may function by facilitating

copper uptake into cells. _Nature_ 288, 715–717 (1980). https://doi.org/10.1038/288715a0 Download citation * Received: 30 July 1980 * Accepted: 16 October 1980 * Issue Date: 18 December 1980

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