Insights into the ligand binding specificity of SREC-II (scavenger receptor expressed by endothelial cells).

Autor: Wicker-Planquart C; CNRS, CEA, IBS, University of Grenoble Alpes, Grenoble, France., Tacnet-Delorme P; CNRS, CEA, IBS, University of Grenoble Alpes, Grenoble, France., Preisser L; CHU Angers, Inserm, CRCINA, SFR ICAT, Univ Angers, Université de Nantes, Angers, France., Dufour S; CNRS, CEA, IBS, University of Grenoble Alpes, Grenoble, France., Delneste Y; CHU Angers, Inserm, CRCINA, SFR ICAT, Univ Angers, Université de Nantes, Angers, France., Housset D; CNRS, CEA, IBS, University of Grenoble Alpes, Grenoble, France., Frachet P; CNRS, CEA, IBS, University of Grenoble Alpes, Grenoble, France., Thielens NM; CNRS, CEA, IBS, University of Grenoble Alpes, Grenoble, France.
Jazyk: angličtina
Zdroj: FEBS open bio [FEBS Open Bio] 2021 Oct; Vol. 11 (10), pp. 2693-2704. Date of Electronic Publication: 2021 Sep 12.
DOI: 10.1002/2211-5463.13260
Abstrakt: SREC-II (scavenger receptor expressed by endothelial cells II) is a membrane protein encoded by the SCARF2 gene, with high homology to class F scavenger receptor SR-F1, but no known scavenging function. We produced the extracellular domain of SREC-II in a recombinant form and investigated its capacity to interact with common scavenger receptor ligands, including acetylated low-density lipoprotein (AcLDL) and maleylated or acetylated BSA (MalBSA or AcBSA). Whereas no binding was observed for AcLDL, SREC-II ectodomain interacted strongly with MalBSA and bound with high affinity to AcBSA, a property shared with the SR-F1 ectodomain. SREC-II ectodomain also interacted with two SR-F1-specific ligands, complement C1q and calreticulin, with affinities in the 100 nm range. We proceeded to generate a stable CHO cell line overexpressing full-length SREC-II; binding of MalBSA to these cells was significantly increased compared with nontransfected CHO cells. In contrast, no increase in binding could be detected for C1q and calreticulin. We show for the first time that SREC-II has the capacity to interact with the common scavenger receptor ligand MalBSA. In addition, our data highlight similarities and differences in the ligand binding properties of SREC-II in soluble form and at the cell surface, and show that endogenous protein ligands of the ectodomain of SREC-II, such as C1q and calreticulin, are shared with the corresponding domain of SR-F1.
(© 2021 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)
Databáze: MEDLINE
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