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

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 there...

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Bibliographic Details
Published in:Biological & pharmaceutical bulletin 2015/01/01, Vol.38(1), pp.116-121
Main Authors: Miki, Yuichi, Koyama, Keisuke, Kurusu, Haruna, Hirano, Kazuya, Beppu, Masatoshi, Fujiwara, Yasuyuki
Format: Article
Language:English
Subjects:
Animals
HEK293 Cells
Humans
macrophage
Macrophages, Peritoneal - metabolism
Macrophages, Peritoneal - physiology
Male
maleylated-bovine serum albumin
Mice
Nucleolin
Phagocytosis
Phosphoproteins - genetics
Phosphoproteins - metabolism
RNA-Binding Proteins - genetics
RNA-Binding Proteins - metabolism
scavenger receptor
Serum Albumin, Bovine - metabolism
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Summary: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 thioglycollate-elicited mouse peritoneal macrophages was weak, but that of maleylated-BSA was strong. Surface plasmon-resonance 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.
ISSN:0918-6158
1347-5215
DOI:10.1248/bpb.b14-00624