Characterization of novel interactions with membrane NEU1 highlights new regulatory functions for the Elastin Receptor Complex in monocyte interaction with endothelial cells

Cell & Bioscience

Christine Terryn¹  Damien Rioult²  Dignê Tembely³  Pascal Maurice³  Laurent Duca³  Amar Bennasroune³  Olivier Bocquet³  Béatrice Romier³  Laurent Martiny³  Sébastien Blaise³  Hervé Sartelet³ 

[1] Plate-Forme Imagerie Cellulaire Et Tissulaire (PICT), Université de Reims Champagne Ardenne (URCA), UFR Médecine, Reims, France;Plateau Technique Mobile de Cytométrie Environnementale MOBICYTE, URCA/INERIS, Université de Reims Champagne Ardenne (URCA), UFR Sciences Exactes Et Naturelles, Reims, France;UMR CNRS 7369 Matrice Extracellulaire Et Dynamique Cellulaire (MEDyC), Université de Reims Champagne Ardenne (URCA), UFR Sciences Exactes Et Naturelles, Moulin de La Housse, BP1039, 51687, Reims cedex 2, France;

关键词: Elastin remodeling;    Elastin peptides;    Elastin receptor complex;    NEU1;    Desialylation;    Membrane glycoproteins;    Monocytes;    Endothelial cells;   

DOI  :  10.1186/s13578-021-00718-x

来源: Springer

【 摘 要 】

BackgroundVascular aging is associated with remodeling of elastin, one of the main extracellular matrix component of the arterial wall, and production of elastin-derived peptides (EDP). These extracellular matrix degradation products have been shown to trigger biological activities through the elastin receptor complex (ERC) and data from the last decade have brought significant insights on the critical role played by its NEU1 subunit in the biological effects mediated by EDP and the ERC in vascular and metabolic diseases.ResultsUsing a proteomic approach, we previously identified new potential interaction partners of membrane NEU1. Here, we validated the interaction between NEU1 and the β2 integrin in human monocytes and show that binding of EDP to the ERC leads to desialylation of β2 integrin through NEU1. A similar action mechanism was identified in human umbilical vein endothelial cells (HUVEC) for intercellular cell adhesion molecule-1 (ICAM-1). Importantly, these effects were associated with a significant increase in monocyte adhesion to endothelial cells and monocyte transendothelial migration.ConclusionsThese results demonstrate that membrane NEU1 sialidase interacts and modulates the sialylation levels of the β2 integrin and ICAM-1 through the ERC in monocytes and endothelial cells, respectively, and suggest that EDP and the ERC, through this newly identified common mode of action governed by NEU1, may be important regulators of circulating monocyte recruitment to inflamed vascular sites. Moreover, by its ability to interact with and to modulate the sialylation of key membrane glycoproteins through NEU1, new biological functions are anticipated for EDP and the ERC in elastin remodeling-associated disorders.

【 授权许可】

CC BY