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

Yoshikuni Goto, Takahiro J. Nakamura, Kenji Ogawa, Akira Hattori, Masafumi Tsujimoto

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)159-165
Number of pages7
JournalJournal of Biochemistry
Volume165
Issue number2
DOIs
Publication statusPublished - 1 Feb 2019

Fingerprint

Aminopeptidases
Acute-Phase Proteins
Endoplasmic Reticulum
Knockout Mice
Lipopolysaccharides
Blood
Leucyl Aminopeptidase
Arginine
Amino Acids
Injections
Enzymes

Keywords

  • Acute phase
  • Amino acid
  • Aminopeptidase
  • Lipopolysaccharide
  • Nitric oxide

Cite this

Goto, Yoshikuni ; Nakamura, Takahiro J. ; Ogawa, Kenji ; Hattori, Akira ; Tsujimoto, Masafumi. / Acute-phase protein-like properties of endoplasmic reticulum aminopeptidase 1. In: Journal of Biochemistry. 2019 ; Vol. 165, No. 2. pp. 159-165.
@article{ed8380eec869460e9fe5a3eb03d2aa15,
title = "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 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.",
keywords = "Acute phase, Amino acid, Aminopeptidase, Lipopolysaccharide, Nitric oxide",
author = "Yoshikuni Goto and Nakamura, {Takahiro J.} and Kenji Ogawa and Akira Hattori and Masafumi Tsujimoto",
year = "2019",
month = "2",
day = "1",
doi = "10.1093/jb/mvy090",
language = "English",
volume = "165",
pages = "159--165",
journal = "Journal of Biochemistry",
issn = "0021-924X",
publisher = "Oxford University Press",
number = "2",

}

Acute-phase protein-like properties of endoplasmic reticulum aminopeptidase 1. / Goto, Yoshikuni; Nakamura, Takahiro J.; Ogawa, Kenji; Hattori, Akira; Tsujimoto, Masafumi.

In: Journal of Biochemistry, Vol. 165, No. 2, 01.02.2019, p. 159-165.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Acute-phase protein-like properties of endoplasmic reticulum aminopeptidase 1

AU - Goto, Yoshikuni

AU - Nakamura, Takahiro J.

AU - Ogawa, Kenji

AU - Hattori, Akira

AU - Tsujimoto, Masafumi

PY - 2019/2/1

Y1 - 2019/2/1

N2 - 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.

AB - 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.

KW - Acute phase

KW - Amino acid

KW - Aminopeptidase

KW - Lipopolysaccharide

KW - Nitric oxide

UR - http://www.scopus.com/inward/record.url?scp=85060144997&partnerID=8YFLogxK

U2 - 10.1093/jb/mvy090

DO - 10.1093/jb/mvy090

M3 - Article

C2 - 30365037

AN - SCOPUS:85060144997

VL - 165

SP - 159

EP - 165

JO - Journal of Biochemistry

JF - Journal of Biochemistry

SN - 0021-924X

IS - 2

ER -