Growth-modulating plasma tripeptide may function by facilitating copper uptake into cells
- Select a language for the TTS:
- UK English Female
- UK English Male
- US English Female
- US English Male
- Australian Female
- Australian Male
- Language selected: (auto detect) - EN
Play all audios:
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.
Anyone you share the following link with will be able to read this content: