Acute-phase protein-like properties of endoplasmic reticulum aminopeptidase 1

Abstract 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 le...

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Published in:Journal of biochemistry (Tokyo) Vol. 165; no. 2; pp. 159 - 165
Main Authors: Goto, Yoshikuni, Nakamura, Takahiro J, Ogawa, Kenji, Hattori, Akira, Tsujimoto, Masafumi
Format: Journal Article
Language:English
Published: England Oxford University Press 01-02-2019
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Summary:Abstract 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.
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ISSN:0021-924X
1756-2651
DOI:10.1093/jb/mvy090