期刊
PEPTIDES
卷 27, 期 2, 页码 431-437出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2005.03.062
关键词
MSH; melanocortin; inflammation; anti-inflammatory; NF-kappa B
资金
- Biotechnology and Biological Sciences Research Council [BB/D524983/1] Funding Source: Medline
- BBSRC [BB/D524983/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/D524983/1] Funding Source: researchfish
alpha-MSH is an anti-inflammatory peptide which signals by binding to the melanocortin-1 receptor (MC1R) and elevating cyclic AMP in several different cells and tissues. The carboxyl terminal peptides of a-MSH (KPV/GKPV) are the smallest minimal sequences that prevent inflammation, but it is not known if they operate via MC1R or cyclic AMP. The aim of this study was to examine the intracellular signaling potential of the GKPV peptide sequence when immobilized to polystyrene beads via a polyethylene glycol moiety. Beads containing an immobilized GKPV peptide were investigated for their ability to inhibit proinflammatory tumor necrosis factor-alpha (TNF-alpha) stimulated activation of NF-kappa B in HBL cells stably transfected with an NF-kappa B-luciferase reporter construct. Peptide functionalized beads were compared with the ability of soluble peptide alone (alpha-MSH or GKPV) or non-functionalized beads to inhibit TNF-a stimulated activation of NF-kappa B. GKPV peptide functionalized beads significantly inhibited NF-kappa B-luciferase activity in comparison to beads containing no peptide moiety in one of two growths conditions investigated. Soluble alpha-MSH and GKPV peptides were also confirmed to inhibit NF-kappa B-luciferase. The present study suggests that the carboxyl terminal MSH peptide acts via a cell receptor-based mechanism and furthermore may support the potential use of such immobilized ligands for anti-inflammatory therapeutic use. (c) 2005 Elsevier Inc. All rights reserved.
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