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Combined cupric- and cuprous-binding peptides are effective in preventing IL-8 release from endothelial cells and redox reactions
- Source :
- Biochemical and Biophysical Research Communications. 357:543-548
- Publication Year :
- 2007
- Publisher :
- Elsevier BV, 2007.
-
Abstract
- Copper mobilization and subsequent redox reactions have been implicated in the pathogenesis of numerous inflammation-based diseases. Reduction of the cupric ion (Cu(2+)) to the cuprous ion (Cu(+)) is necessary for the production of copper-induced reactive oxygen species (ROS). Peptides, designed to bind both Cu(2+) and Cu(+) and have the ability to prevent copper redox reactions, were studied. The peptides DAHGMTCANC and DAHKGMTCANC were effective at preventing the formation of thiobarbituric acid-reactive species (TBARS) in a copper/ascorbate solution at a 1:1 peptide/Cu ratio. This was observed in the reducing potential of the copper/ascorbate solutions containing these peptides at a 1:1 ratio based on oxidation-reduction potential (ORP) measurements. The peptide DAHGMTCARC was effective at a 2:1 ratio, but not at a 1:1 ratio in which an increase in the oxidation potential was observed. This suggests that a positively charged amino acid such as arginine (R) in the Cu(+)-binding motif interferes with metal chelation. All peptides tested were effective at preventing IL-8 release from phorbol 12-myristate 13-acetate (PMA)/copper-stimulated human umbilical vein endothelial cells (HUVEC). The use of Cu(+)/Cu(2+)-binding peptides might be beneficial in the treatment of ROS-related diseases associated with copper.
- Subjects :
- Arginine
Biophysics
chemistry.chemical_element
Peptide
Thiobarbituric Acid Reactive Substances
Biochemistry
Redox
chemistry.chemical_compound
TBARS
Humans
Molecular Biology
Cells, Cultured
chemistry.chemical_classification
Reactive oxygen species
Dose-Response Relationship, Drug
Interleukin-8
Endothelial Cells
Cell Biology
Copper
Amino acid
chemistry
Hydroxyl radical
Peptides
Reactive Oxygen Species
Oxidation-Reduction
Nuclear chemistry
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 357
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....9211074670c2508f0077f4d58562225f