Clearance of oxidized erythrocytes by macrophages: Involvement of caspases in the generation of clearance signal at band 3 glycoprotein

Miki, Yuichi; Tazawa, Tomoki; Hirano, Kazuya; Matsushima, Hideki; Kumamoto, Shoko; Yamaguchi, Tomohiro; Beppu, Masatoshi

doi:10.1016/j.bbrc.2007.08.089

Cited by 27 publications

(22 citation statements)

References 13 publications

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“…Nucleolin as the Macrophage Receptor of Artificially Capped Jurkat Cells Sialylpolylactosaminyl chains on CD43-capped apoptotic cells are known to be recognized by nucleolin, 25,29,33) and we confirmed that this was the case in our healthy CD43-capped Jurkat cells. As shown in Fig.…”

Section: Cytochalasin B-induced Capping Of Cd43 On the Surface Of Jursupporting

confidence: 83%

“…Under apoptotic conditions, capping is induced by activated caspases 8,25) which can be detected by measuring the intensity of MCA florescence produced when they cleave certain molecules. Given that we previously observed the activation of caspase-3 in apoptotic cells recognized by macrophages, 25,33) we tested for activated caspase-3, and upstream caspase-9, finding that neither caspase was activated in Jurkat cells treated with cytochalasin B (Figs. 3A, B).…”

Section: Cytochalasin B-induced Capping Of Cd43 On the Surface Of Jurmentioning

confidence: 99%

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

Oguri

Miki

Hirano

et al. 2012

Biological & Pharmaceutical Bulletin

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Section: Cytochalasin B-induced Capping Of Cd43 On the Surface Of Jursupporting

confidence: 83%

Section: Cytochalasin B-induced Capping Of Cd43 On the Surface Of Jurmentioning

confidence: 99%

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

Oguri

Miki

Hirano

et al. 2012

Biological & Pharmaceutical Bulletin

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“…Here, we demonstrated that, in addition to other discarded elements, 4,[6][7][8][9]25) maleylated-BSA is also a ligand for nucleolin. This observation supports the notion that nucleolin on the surface of phagocytes has a general scavenger-like ability.…”

Section: Discussionmentioning

confidence: 79%

“…4,[6][7][8][9]25) Here, we showed that nucleolin expressed on the surface of macrophages is also a receptor for maleylated-BSA. These observations support the idea that phagocytes with cell-surface expression of nucleolin have a general scav- enger-like ability.…”

Section: Discussionmentioning

confidence: 84%

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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“…32) Interestingly, the optimal concentration of H 2 O 2 is 0.1 mM, and caspase inhibitors prevented erythrocyte change from unsusceptible to susceptible to macrophage recognition after oxidation, 32) which suggests that caspases present in erythrocyte cytosol 33) play a role in the "eat-me signal" generation, possibly clustering of band 3 glycoprotein. This observation also supports the present results that moderately oxidized Jurkat cells undergo apoptosis, and as a result of caspase-dependent proteolysis of cytoplasmic or/and membrane proteins, CD43 clustering may be induced.…”

Section: Discussionmentioning

confidence: 99%

Clearance of Oxidatively Damaged Cells by Macrophages: Recognition of Glycoprotein Clusters by Macrophage-Surface Nucleolin as Early Apoptotic Cells

Miki

Itoh

Hirano

et al. 2009

Biological & Pharmaceutical Bulletin

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Oxidative stress is known to cause various damages to cellular components such as nucleic acids, lipids, and proteins. [1][2][3] The damages to the cellular components are induced by free radical reactions including degradation, adduct formation, cross-linking, bond-breaking reactions, and so forth.1-3) Therefore oxidatively stressed cells are thought to undergo cell-membrane damages including membrane protein denaturation and cross-linking by free radicals.We previously studied the responses of macrophages to oxidatively damaged cells such as oxidized erythrocytes, 4,5) neutrophils, 6) and Jurkat T cells, 7) using various oxidants, and found that macrophages recognize and remove these oxidatively damaged cells. [4][5][6][7] The determinants on the oxidized cell surface that macrophages recognize were not chemically modified nor denatured membrane structure, but were preexisting carbohydrate chains containing sialyl residues and polylactosaminoglycan structures, possibly sialylpoly-N-acetyllactosaminyl chains, of membrane glycoproteins.4-7) Then, a question how macrophages discriminate the preexisting cellsurface carbohydrate chains of oxidized cells from those of unoxidized cells arose, and this was explained by the hypothesis that membrane glycoproteins aggregate to form clusters upon cell oxidation, presumably due to free radical-mediated protein cross-linking, and the resultant clusters of their extracellular polylactosaminoglycans provide multivalent and therefore high-affinity ligands for macrophage receptors. [4][5][6][7][8] However, there was no conclusive evidence for the membrane glycoprotein aggregation on oxidatively damaged cells [9][10][11][12] and for the presence of the putative macrophage receptors. [13][14][15] In another series of recent works on apoptotic cells, we found that CD43, a major membrane sialoglycoprotein of hematopoietic cells containing sialyl residues and poly-Nacetyllactosaminyl chains, of Jurkat cells aggregates to form clusters and caps at an early stage of apoptosis, and the early apoptotic Jurkat cells were recognized and taken up by macrophages through the clustered and capped CD43. 16) CD43 is a heavily sialylated membrane glycoprotein, 17) and the determinants on CD43 glycoprotein of early apoptotic cells were suggested to be sialylpoly-N-acetyllactosaminyl sugar chains 16) similarly to the determinants on oxidized cells for the macrophage recognition described above. In addition, we identified the macrophage receptor for sialylpoly-Nacetyllactosaminyl chains as nucleolin, 18) a multifunctional shuttle protein present in nucleus and cytoplasm and on the surface of some types of cells including macrophages, 19,20) and demonstrated that nucleolin expressed on cell surface recognizes early apoptotic cells but not non-apoptotic cells. 18)We also demonstrated that phosphatidylserine (PS), a wellinvestigated cell-surface marker for apoptotic cells, 21-23) is not exposed on the cell surface at the early stage of apoptosis, but is at relatively later stages. 24)Considering the s...

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Clearance of oxidized erythrocytes by macrophages: Involvement of caspases in the generation of clearance signal at band 3 glycoprotein

Cited by 27 publications

References 13 publications

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

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

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

Clearance of Oxidatively Damaged Cells by Macrophages: Recognition of Glycoprotein Clusters by Macrophage-Surface Nucleolin as Early Apoptotic Cells

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