The antimicrobial activity of chemerin-derived peptide p4 requires oxidative conditions.
Animals
Anti-Bacterial Agents
/ pharmacology
Chemokines
/ metabolism
Female
Humans
Intercellular Signaling Peptides and Proteins
/ metabolism
Methicillin-Resistant Staphylococcus aureus
/ drug effects
Mice
Mice, Inbred C57BL
Microbial Sensitivity Tests
Oligopeptides
/ pharmacology
Oxidation-Reduction
Oxidative Stress
/ drug effects
Skin
/ drug effects
Skin Diseases, Bacterial
/ drug therapy
Staphylococcal Infections
/ drug therapy
MRSA
Staphylococcus aureus (S. aureus)
adipokine
antimicrobial peptide (AMP)
bacteria
chemerin
chemotaxis
epidermis
host defense
host–pathogen interaction
skin
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
25 01 2019
25 01 2019
Historique:
received:
22
08
2018
revised:
22
11
2018
pubmed:
7
12
2018
medline:
30
4
2019
entrez:
4
12
2018
Statut:
ppublish
Résumé
Chemerin is a leukocyte attractant, adipokine, and antimicrobial protein abundantly produced in the skin epidermis. Despite the fact that most of the bactericidal activity present in human skin exudates is chemerin-dependent, just how chemerin shapes skin defenses remains obscure. Here we demonstrate that p4, a potent antimicrobial human chemerin peptide derivative, displays killing activity against pathogenic methicillin-resistant
Identifiants
pubmed: 30504221
pii: S0021-9258(20)38864-5
doi: 10.1074/jbc.RA118.005495
pmc: PMC6349111
pii:
doi:
Substances chimiques
Anti-Bacterial Agents
0
Chemokines
0
Intercellular Signaling Peptides and Proteins
0
Oligopeptides
0
RARRES2 protein, human
0
peptide P4
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1267-1278Références
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