Acute-phase protein-like properties of endoplasmic reticulum aminopeptidase 1.
Journal
Journal of biochemistry
ISSN: 1756-2651
Titre abrégé: J Biochem
Pays: England
ID NLM: 0376600
Informations de publication
Date de publication:
01 Feb 2019
01 Feb 2019
Historique:
received:
28
05
2018
accepted:
23
10
2018
pubmed:
27
10
2018
medline:
1
3
2019
entrez:
27
10
2018
Statut:
ppublish
Résumé
Endoplasmic reticulum aminopeptidase 1 (ERAP1) is a multi-functional enzyme. In this study, we analysed its role in lipopolysaccharide-induced inflammatory response in wild-type and ERAP1-knockout mice. Following lipopolysaccharide injection, ERAP1 was secreted into the blood, increasing leucine aminopeptidase activity and NO synthesis therein. Among the amino acids tested, arginine concentration was significantly increased in wild-type mice compared to ERAP1-knockout mice. These results suggest that ERAP1 behaves similar to acute-phase proteins, which are secreted into the blood in response to infectious/inflammatory stimuli and are involved in enhancing NO synthesis as a host defense mechanism.
Identifiants
pubmed: 30365037
pii: 5145134
doi: 10.1093/jb/mvy090
doi:
Substances chimiques
Acute-Phase Proteins
0
Lipopolysaccharides
0
Minor Histocompatibility Antigens
0
Nitric Oxide
31C4KY9ESH
Aminopeptidases
EC 3.4.11.-
ERAP1 protein, mouse
EC 3.4.11.-
Leucyl Aminopeptidase
EC 3.4.11.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM