Related Experiment Video
Updated: Feb 3, 2026

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
Published on: February 18, 2014
Acute-phase protein-like properties of endoplasmic reticulum aminopeptidase 1
Yoshikuni Goto1, Takahiro J Nakamura2, Kenji Ogawa3
1Faculty of Pharmaceutical Sciences, Teikyo-Heisei University, 4-21-2 Nakano, Nakano, Tokyo, Japan.
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.
More Related Videos
Related Concept Videos
Endoplasmic Reticulum
The Endoplasmic Reticulum
Directing Proteins to the Rough Endoplasmic Reticulum
Smooth Endoplasmic Reticulum
The ER provides optimal conditions for synthesizing steroid hormones and lipids, such as phospholipids and triglycerides. Traditionally, lipid metabolism was considered to be a smooth ER function. However, there is no direct evidence to prove that rough ER is completely excluded from lipid...
Phase Diagrams
Phase Transitions

