Scavenger receptors in homeostasis and immunity

Canton, Johnathan; Neculai, Dante; Grinstein, Sergio

doi:10.1038/nri3515

Cited by 698 publications

(696 citation statements)

References 218 publications

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“…3,5) These findings suggest that SRs have a wide range of functions and that the identification of members of the scavenger receptor family might help characterize tissue homeostasis and diseases.…”

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confidence: 99%

“…Therefore, macrophages are critical for maintaining homeostasis and healthy tissues by clearing various discarded elements and reducing inflammation. [1][2][3][4] Scavenger receptors (SRs) consist of classes A to I and are expressed on the surfaces of macrophages, dendritic cells, and endothelial cells and initiate the removal of a large repertoire of discarded elements. SRs were identified by their ability to recognize and remove modified or damaged proteins (e.g.…”

mentioning

confidence: 99%

“…SRs have also been implicated in diseases as diverse as Alzhei mer's disease, atherosclerosis and type 2 diabetes mellitus. 3) In addition to modified endogenous molecules, SRs recognize conserved pathogen-associated molecular patterns (PAMPs) expressed on exogenous microbial surfaces, which results in the clearance of various microbial species and structures such as bacteria and bacterial lipopolysaccharides, lipoteichoic acid, CpG DNA and viruses.…”

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confidence: 99%

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Nucleolin Is a Receptor for Maleylated-Bovine Serum Albumin on Macrophages

et al. 2015

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Scavenger receptors have a broad range of functions that include pathogen clearance, and identification of the scavenger receptor family has been of great benefit to the field of physiology. The shuttling-protein nucleolin has recently been shown to possess scavenger receptor-like activity. We therefore investigated whether or not nucleolin is a receptor for maleylated-bovine serum albumin (maleylated-BSA), which is a common ligand for scavenger receptors. Binding and phagocytosis of native control-BSA by thioglycollateelicited mouse peritoneal macrophages was weak, but that of maleylated-BSA was strong. Surface plasmonresonance analysis revealed that nucleolin strongly associated with maleylated-BSA but not control-BSA or maleic anhydride. Further, co-treatment of macrophages with anti-nucleolin antibody, but not control-immunoglobulin G, inhibited binding of maleylated-BSA. In addition, antineoplastic guanine rich oligonucleotide (AGRO), a nucleolin-specific oligonucleotide aptamer, inhibited binding of maleylated-BSA. Further, binding of maleylated-BSA to nucleolin-transfected HEK293 cells was higher than that by control HEK cells. These results indicate that nucleolin is a receptor that enables macrophages to recognize maleylated-BSA.

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Nucleolin Is a Receptor for Maleylated-Bovine Serum Albumin on Macrophages

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“…7) SRs play a key role in the removal of a broad range of discarded elements and were initially identified by their ability to bind and remove modified or damaged endogenous and exogenous molecules, including maleylated protein, fibril amyloid-β, AcLDL, OxLDL, oxidized phosphatidylserine, apoptotic cells, bacteria, bacterial lipopolysaccharides, and viral components.…”

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confidence: 99%

“…7) Nucleolin is a multifunctional shuttling protein that is present in the nucleus, cytoplasm, and on the surface of macrophages. 8,9) We previously identified nucleolin as a scavenger receptor for apoptotic cells 10) and modified proteins such as fibril amyloid-β, 11) advanced glycosylation end products, 12) and maleylated-proteins.…”

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confidence: 99%

Nucleolin Acts as a Scavenger Receptor for Acetylated Low-Density Lipoprotein on Macrophages

Miki

Tachibana

Ohminato

et al. 2015

Biological & Pharmaceutical Bulletin

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Although macrophage phagocytoses modified low-density lipoprotein (LDL), excessive accumulation of modified LDL induces macrophage foam cell formation, which is a feature of atherosclerotic plaque. Thus, the identification of scavenger receptor for modified LDL will provide better understanding of an atherosclerotic event. We recently showed that nucleolin expressed on macrophages acts as a scavenger receptor for various endogenous discarded products. Here, we investigated whether or not nucleolin is involved in the uptake of acetylated LDL (AcLDL). In contrast to normal LDL, AcLDL directly bound to immobilized nucleolin. AcLDL exhibited a higher affinity for macrophages than normal LDL. This binding of AcLDL was inhibited by anti-nucleolin antibody and antineoplastic guanine-rich oligonucleotide (AGRO), a nucleolinspecific oligonucleotide aptamer. In addition, AcLDL exhibited a higher affinity for HEK cells transfected with nucleolin than those without. Further, intracellular accumulation of AcLDL was also inhibited by antinucleolin antibody. The results of this study suggest that nucleolin expressed on macrophages is a receptor for AcLDL.Key words nucleolin; macrophage; acetylated low-density lipoprotein (AcLDL); scavenger receptor Low-density lipoprotein (LDL) elevates cholesterol deposits in macrophage foam cells, which are involved in the development of atherosclerotic lesions.1) As the uptake of normal LDL via its receptor is controlled by feedback regulation, excess levels of LDL-derived cholesterol in macrophages might be attributed to modifications of LDL such as oxidation, acetylation, and aggregation.2) Scavenger receptors (SRs) and other unknown receptors account for up to 95% of the uptake of modified LDL.

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Cell wall glycopolymers of Firmicutes and their role as nonprotein adhesins

Schade

Weidenmaier

2016

FEBS Letters

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Cell wall glycopolymers (CWGs) of gram-positive bacteria have gained increasing interest with respect to their role in colonization and infection. In most gram-positive pathogens they constitute a large fraction of the cell wall biomass and represent major cell envelope determinants. Depending on their chemical structure they modulate interaction with complement factors and play roles in immune evasion or serve as nonprotein adhesins that mediate, especially under dynamic conditions, attachment to different host cell types. In particular, covalently peptidoglycan-attached CWGs that extend well above the cell wall seem to interact with glyco-receptors on host cell surfaces. For example, in the case of Staphylococcus aureus, the cell wall-attached teichoic acid (WTA) has been identified as a major CWG adhesin. A recent report indicates that a type-F scavenger receptor, termed SR-F1 (SREC-I), is the predominant WTA receptor in the nasal cavity and that WTA-SREC-I interaction plays an important role in S. aureus nasal colonization. Therefore, understanding the role of CWGs in complex processes that mediate colonization and infection will allow novel insights into the mechanisms of hostmicrobiota interaction.

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Scavenger receptors in homeostasis and immunity

Cited by 698 publications

References 218 publications

Nucleolin Is a Receptor for Maleylated-Bovine Serum Albumin on Macrophages

Nucleolin Is a Receptor for Maleylated-Bovine Serum Albumin on Macrophages

Nucleolin Acts as a Scavenger Receptor for Acetylated Low-Density Lipoprotein on Macrophages

Cell wall glycopolymers of Firmicutes and their role as nonprotein adhesins

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