Format

Send to

Choose Destination
Cell Mol Life Sci. 2018 Nov 29. doi: 10.1007/s00018-018-2978-6. [Epub ahead of print]

Identification of CD36 as a new interaction partner of membrane NEU1: potential implication in the pro-atherogenic effects of the elastin receptor complex.

Author information

1
UMR CNRS 7369 Matrice Extracellulaire et Dynamique Cellulaire (MEDyC), Team 2 "Matrix Aging and Vascular Remodelling", Université de Reims Champagne Ardenne (URCA), UFR Sciences Exactes et Naturelles, Moulin de la Housse, BP1039, 51687, Reims Cedex 2, France.
2
Fraunhofer Institute for Microstructure of Materials and Systems IMWS, Halle (Saale), Germany.
3
Institute of Pharmacy, Faculty of Natural Sciences I, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
4
Department of Pharmacy, University of Copenhagen, Copenhagen, Denmark.
5
PICT Platform, Université de Reims Champagne Ardenne (URCA), Reims, France.
6
Blizard Institute, Barts and the London School of Medicine, Queen Mary University of London, London, UK.
7
UMR CNRS 7369 Matrice Extracellulaire et Dynamique Cellulaire (MEDyC), Team 2 "Matrix Aging and Vascular Remodelling", Université de Reims Champagne Ardenne (URCA), UFR Sciences Exactes et Naturelles, Moulin de la Housse, BP1039, 51687, Reims Cedex 2, France. pascal.maurice@univ-reims.fr.

Abstract

In addition to its critical role in lysosomes for catabolism of sialoglycoconjugates, NEU1 is expressed at the plasma membrane and regulates a myriad of receptors by desialylation, playing a key role in many pathophysiological processes. Here, we developed a proteomic approach dedicated to the purification and identification by LC-MS/MS of plasma membrane NEU1 interaction partners in human macrophages. Already known interaction partners were identified as well as several new candidates such as the class B scavenger receptor CD36. Interaction between NEU1 and CD36 was confirmed by complementary approaches. We showed that elastin-derived peptides (EDP) desialylate CD36 and that this effect was blocked by the V14 peptide, which blocks the interaction between bioactive EDP and the elastin receptor complex (ERC). Importantly, EDP also increased the uptake of oxidized LDL by macrophages that is blocked by both the V14 peptide and the sialidase inhibitor 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (DANA). These results demonstrate, for the first time, that binding of EDP to the ERC indirectly modulates CD36 sialylation level and regulates oxidized LDL uptake through this sialidase. These effects could contribute to the previously reported proatherogenic role of EDP and add a new dimension in the regulation of biological processes through NEU1.

KEYWORDS:

Atherosclerosis; CD36; Elastin-derived peptides; NEU1; Sialylation

PMID:
30498996
DOI:
10.1007/s00018-018-2978-6

Supplemental Content

Full text links

Icon for Springer
Loading ...
Support Center