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Title: E-selectin ligand-1 (ESL-1) is a novel adiponectin binding protein on cell adhesion

Abstract

Background: Adiponectin (APN) is an adipocyte-derived bioactive molecule with anti-diabetic and anti-atherogenic properties. Although anti-diabetic effects are mostly mediated by the adiponectin receptors AdipoR1 and AdipoR2, the anti-atherogenic mechanisms have not been fully elucidated. Methods and Results: In this study, we identified E-selectin ligand (ESL)-1 as a novel APN-binding protein by mass spectrometry analysis of HepG2 cell-derived immunoprecipitant with an anti-APN antibody. Cell adhesion assays using fluorescence-labelled monocyte cell line THP-1 cells and human umbilical vein endothelial cells (HUVECs) revealed that APN-pre-treated THP-1 cells had reduced binding ability to HUVECs. This APN-mediated suppressive effect on monocyte binding to endothelial cells was partially abrogated by targeting ESL-1 with shRNA in THP-1 cells. In addition, serial mutagenesis analysis disclosed that five extracellular amino acids close to the N-terminus of ESL-1 were essential for binding with APN. Conclusion: Our results highlight the fact that interaction between APN and ESL-1 could provide a fundamental mechanism underlying the anti-atherogenic properties of APN. - Highlights: • E-selectin ligand (ESL)-1 was identified as an adiponectin (APN)-binding protein. • ESL-1 bound to APN at its N-terminal 6th-10th amino acids. • shESL-1 reduced the suppressive effect of APN on adhesion of THP-1 cells to HUVECs. • Interaction with ESL may be involved inmore » the anti-atherogenic effects of APN.« less

Authors:
; ; ; ; ;  [1]; ;  [2];  [1]
  1. Department of Biomedical Informatics, Division of Health Sciences, Osaka University Graduate School of Medicine, Osaka (Japan)
  2. Department of Metabolic Medicine, Osaka University Graduate School of Medicine, Osaka (Japan)
Publication Date:
OSTI Identifier:
22594226
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 470; Journal Issue: 2; Other Information: Copyright (c) 2016 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ANTIBODIES; ARTERIOSCLEROSIS; FLUORESCENCE; LIGANDS; MASS SPECTROSCOPY; MONOCYTES; MUTAGENESIS; RECEPTORS; VEINS

Citation Formats

Yamamoto, Hiroyasu, Kuroda, Nana, Uekita, Hiromi, Kochi, Ikoi, Matsumoto, Akane, Niinaga, Ryu, Funahashi, Tohru, Shimomura, Iichiro, and Kihara, Shinji. E-selectin ligand-1 (ESL-1) is a novel adiponectin binding protein on cell adhesion. United States: N. p., 2016. Web. doi:10.1016/J.BBRC.2016.01.023.
Yamamoto, Hiroyasu, Kuroda, Nana, Uekita, Hiromi, Kochi, Ikoi, Matsumoto, Akane, Niinaga, Ryu, Funahashi, Tohru, Shimomura, Iichiro, & Kihara, Shinji. E-selectin ligand-1 (ESL-1) is a novel adiponectin binding protein on cell adhesion. United States. doi:10.1016/J.BBRC.2016.01.023.
Yamamoto, Hiroyasu, Kuroda, Nana, Uekita, Hiromi, Kochi, Ikoi, Matsumoto, Akane, Niinaga, Ryu, Funahashi, Tohru, Shimomura, Iichiro, and Kihara, Shinji. Fri . "E-selectin ligand-1 (ESL-1) is a novel adiponectin binding protein on cell adhesion". United States. doi:10.1016/J.BBRC.2016.01.023.
@article{osti_22594226,
title = {E-selectin ligand-1 (ESL-1) is a novel adiponectin binding protein on cell adhesion},
author = {Yamamoto, Hiroyasu and Kuroda, Nana and Uekita, Hiromi and Kochi, Ikoi and Matsumoto, Akane and Niinaga, Ryu and Funahashi, Tohru and Shimomura, Iichiro and Kihara, Shinji},
abstractNote = {Background: Adiponectin (APN) is an adipocyte-derived bioactive molecule with anti-diabetic and anti-atherogenic properties. Although anti-diabetic effects are mostly mediated by the adiponectin receptors AdipoR1 and AdipoR2, the anti-atherogenic mechanisms have not been fully elucidated. Methods and Results: In this study, we identified E-selectin ligand (ESL)-1 as a novel APN-binding protein by mass spectrometry analysis of HepG2 cell-derived immunoprecipitant with an anti-APN antibody. Cell adhesion assays using fluorescence-labelled monocyte cell line THP-1 cells and human umbilical vein endothelial cells (HUVECs) revealed that APN-pre-treated THP-1 cells had reduced binding ability to HUVECs. This APN-mediated suppressive effect on monocyte binding to endothelial cells was partially abrogated by targeting ESL-1 with shRNA in THP-1 cells. In addition, serial mutagenesis analysis disclosed that five extracellular amino acids close to the N-terminus of ESL-1 were essential for binding with APN. Conclusion: Our results highlight the fact that interaction between APN and ESL-1 could provide a fundamental mechanism underlying the anti-atherogenic properties of APN. - Highlights: • E-selectin ligand (ESL)-1 was identified as an adiponectin (APN)-binding protein. • ESL-1 bound to APN at its N-terminal 6th-10th amino acids. • shESL-1 reduced the suppressive effect of APN on adhesion of THP-1 cells to HUVECs. • Interaction with ESL may be involved in the anti-atherogenic effects of APN.},
doi = {10.1016/J.BBRC.2016.01.023},
journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 2,
volume = 470,
place = {United States},
year = {2016},
month = {2}
}