Effects of glycyl-histidyl-lysyl chelated Cu(II) on ferritin dependent lipid peroxidation.
The copper binding tripeptide, glycyl-L-histidyl-L-lysine [GHK:Cu(II)] has a plethora of biological effects related to the wound healing process. The presence of iron complexes in damaged tissues is detrimental to wound healing, due to local inflammation, as well as microbial infection mediated by iron. To test if the wound healing properties of GHK:Cu(II) are due to an affect on iron metabolism, we examined the effects of GHK:Cu(II) on iron catalyzed lipid peroxidation. GHK:Cu(II) inhibited lipid peroxidation only if the iron source was ferritin. Whereas GHK:Cu(II) inhibited ferritin iron release it did not exhibit significant superoxide dismutase-like or ceruloplasmin-like activity. We propose that GHK:Cu(II) binds to the channels of ferritin involved in iron release and physically prevents the release of Fe(II). Thus, a biological effect of GHK:Cu(II), possibly related to wound healing, may be the inhibition of ferritin iron release in damaged tissues, preventing inflammation and microbial infections.
Miller
D M
DM
Biotechnology Center, Utah State University, Logan 84322-4430.
DeSilva
D
D
Pickart
L
L
Aust
S D
SD
D000818:Animals; D000975:Antioxidants; D002570:Ceruloplasmin / Q000494:pharmacology; D003300:Copper / Q000494:pharmacology*; D005293:Ferritins / Q000378:metabolism*; D066298:In Vitro Techniques; D007501:Iron / Q000378:metabolism; D015227:Lipid Peroxidation / Q000187:drug effects*; D008862:Microsomes, Liver / Q000187:drug effects / Q000201:enzymology; D009245:NADH Dehydrogenase / Q000378:metabolism; D009842:Oligopeptides / Q000494:pharmacology*; D051381:Rats; D013482:Superoxide Dismutase / Q000494:pharmacology; D014969:Xanthine Oxidase / Q000378:metabolism
D000975:Antioxidants; D009842:Oligopeptides; C020905:glycyl-histidyl-lysine; D003300:Copper; D005293:Ferritins; D007501:Iron; D013482:Superoxide Dismutase; D002570:Ceruloplasmin; D014969:Xanthine Oxidase; D009245:NADH Dehydrogenase