Clearance of CD43-Capped Cells by Macrophages: Capping Alone Leads to Phagocytosis

Oguri, Emiri; Miki, Yuichi; Hirano, Kazuya; Yamanaka, Masahiro; Beppu, Masatoshi

doi:10.1248/bpb.35.551

Cited by 5 publications

(10 citation statements)

References 55 publications

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“…8,27) These studies showed that the three-dimensional structure of the CD43 cap is critical for binding to nucleolin. Therefore, negative charges might have an important role in binding between maleylated-BSA and nucleolin.…”

Section: Discussionmentioning

confidence: 99%

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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Section: Discussionmentioning

confidence: 99%

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

et al. 2015

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“…[12][13][14][15][16][17][18][19][20][21][22][23]35) This study showed that Aβ42 is also a ligand for nucleolin. These observations support the idea that nucleolin on the surface of phagocytes has a general scavenger-like ability.…”

Section: Discussionmentioning

confidence: 99%

“…12,13) Previous studies have shown that macrophages utilize nucleolin to recognize and phagocytose apoptotic and oxidized cells 14,15) as well as living cells that have been treated with cytochalasin B and A23187. 16,17) Nucleolin-mediated recognition is therefore simple and powerful, as indicated by the indiscriminant removal of cells. Nucleolin is also a receptor for lipoproteins, 18) coxsackie B virus, 19) human immunodeficiency virus, 20) human parainfluenza virus type 3, 21) and enterohemorrhagic Escherichia coli O157 : H7.…”

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confidence: 99%

Shuttling Protein Nucleolin Is a Microglia Receptor for Amyloid Beta Peptide 1-42

Ozawa

Nakamura

Koike

et al. 2013

Biological & Pharmaceutical Bulletin

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Amyloid-beta peptide 1-42 (Aβ42) plays a key role in the neurotoxicity found in Alzheimer's disease. Mononuclear phagocytes in the brain (microglia), can potentially clear Aβ via phagocytosis. Recently, the shuttling-protein nucleolin has been shown to possess scavenger receptor-activity. Here, we investigated whether this receptor interacts specifically with Aβ type 1-42 and mediates its phagocytosis by microglia. While monomeric and fibril Aβ42 were phagocytosed by mouse microglial EOC2 cells, amyloid β peptide 1-40 (Aβ40) was only weakly phagocytosed. Surface plasmon-resonance analysis revealed that nucleolin strongly associates with Aβ42, but only weakly associates with Aβ40. Immunofluorescence staining of antinucleolin antibody revealed that EOC2 cells and rat primary microglia express nucleolin on their cell surfaces. Further, pretreating EOC2 cells with anti-nucleolin antibody, but not immunoglobulin G (IgG), inhibited phagocytosis of monomeric Aβ42 by microglia. Additionally, nucleolin-transfected HEK293 cells phagocytosed monomeric and fibril Aβ42 but not monomeric and fibril Aβ40. Moreover, AGRO, a nucleolin-specific oligonucleotide aptamer, inhibited phagocytosis of monomeric and fibril Aβ42, but not monomeric and fibril Aβ40. These results indicate that nucleolin is a receptor that allows microglia to recognize monomeric and fibril Aβ42.

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“…Cytoskeletal proteins may therefore play a critical role in ligand capping in cells with elevated calcium. Our previous research also suggests that active movement of cytoskeleton proteins may induce CD43 capping when caspases are activated (Eda et al, 2004;Oguri et al, 2012). Activated caspases can abrogate the link between CD43 and actin during the early stages of apoptosis (Kondo et al, 1997), and disrupting the actin bond presumably causes active movement of other cytoskeleton proteins that then induce capping of CD43 (Eda et al, 2004;Oguri et al, 2012).…”

Section: Discussionmentioning

confidence: 89%

“…Indeed, CD43 capping has been induced artificially using inhibitors that block actin and microtubule polymerization (Oguri et al, 2012;Seveau et al, 1997). CD43 may be conjugated to several cytoskeleton proteins, and disrupting the actin bond could cause active movement of other cytoskeleton proteins that then induce cap formation.…”

Section: Introductionmentioning

confidence: 99%

Macrophage Recognition of Cells with Elevated Calcium Is Mediated by Carbohydrate Chains of CD43

Miki

Oguri

Hirano

et al. 2013

Cell Struct. Funct.

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ABSTRACT. Macrophages remove deteriorating cells (those undergoing apoptosis and oxidation) via poly-Nacetyllactosaminyl chains on CD43 caps, a major cell-surface glycoprotein. Unusually high intracellular calcium levels are also deteriorating for cells and tissue. Here we artificially elevated calcium levels in cells and examined the mechanism by which this elevation was resolved by macrophages. Results showed that treatment with the calcium ionophore A23187 and ionomycin induces capping of CD43 on Jurkat cells, which are subsequently recognized and phagocytosed by macrophages, indicating that macrophages regard cells with elevated calcium as targets for removal. Further tests showed that A23187-and ionomycin-treated Jurkat cells did not induce apoptotic changes such as DNA fragmentation or phosphatidylserine expression, indicating that these cells were removed despite still being viable. Jurkat cells pretreated with anti-CD43 antibody or those with poly-Nacetyllactosaminyl chains containing oligosaccharides inhibited macrophage binding, indicating that macrophages recognize the poly-N-acetyllactosaminyl chains on CD43. Binding was also inhibited by treating macrophages with anti-nucleolin antibody, indicating that recognition occurs through nucleolin, a cell-surface receptor. Further, nucleolin-transfected HEK293 cells bound A23187-treated cells, and this binding was inhibited by in the presence of oligosaccharides. Taken together, these results show that elevated calcium levels induce CD43 capping, and macrophages remove the cells if their nucleolin receptors can bind to the poly-Nacetyllactosaminyl chains of capped CD43.

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Clearance of CD43-Capped Cells by Macrophages: Capping Alone Leads to Phagocytosis

Cited by 5 publications

References 55 publications

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

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

Shuttling Protein Nucleolin Is a Microglia Receptor for Amyloid Beta Peptide 1-42

Macrophage Recognition of Cells with Elevated Calcium Is Mediated by Carbohydrate Chains of CD43

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