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 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.
School of Pharmacy, Tokyo University of Pharmacy and Life Sciences.
Yuichi
Y
Miki
Keisuke
K
Koyama
Haruna
H
Kurusu
Kazuya
K
Hirano
Masatoshi
M
Beppu
Yasuyuki
Y
Fujiwara
D000818:Animals; D057809:HEK293 Cells; D006801:Humans; D017737:Macrophages, Peritoneal / Q000378:metabolism* / Q000502:physiology; D008297:Male; D051379:Mice; D010587:Phagocytosis; D010750:Phosphoproteins / Q000235:genetics / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D000097796:Nucleolin
D010750:Phosphoproteins; D016601:RNA-Binding Proteins; D012710:Serum Albumin, Bovine; D000097796:Nucleolin; C049877:maleylalbumin