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.

authors

Yamamoto H,Kuroda N,Uekita H,Kochi I,Matsumoto A,Niinaga R,Funahashi T,Shimomura I,Kihara S

doi

10.1016/j.bbrc.2016.01.023

subject

Has Abstract

pub_date

2016-02-05 00:00:00

pages

425-430

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(16)30023-7

journal_volume

470

pub_type

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