Nucleolin Is a Receptor for Maleylated-Bovine Serum Albumin on Macrophages
| Autor: | Haruna Kurusu, Keisuke Koyama, Yasuyuki Fujiwara, Kazuya Hirano, Yuichi Miki, Masatoshi Beppu |
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| Rok vydání: | 2015 |
| Předmět: |
Male
Pharmacology biology Chemistry HEK 293 cells Serum albumin RNA-Binding Proteins Pharmaceutical Science Serum Albumin Bovine General Medicine Phosphoproteins Ligand (biochemistry) Molecular biology Mice HEK293 Cells Phagocytosis Macrophages Peritoneal biology.protein Animals Humans Macrophage Antibody Scavenger receptor Receptor Nucleolin |
| Zdroj: | Biological and Pharmaceutical Bulletin. 38:116-121 |
| ISSN: | 1347-5215 0918-6158 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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