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Lectin‐like oxidized low density lipoprotein receptor‐1 (LOX‐1) supports cell adhesion to fibronectin
Author(s) -
Shimaoka Takeshi,
Kume Noriaki,
Minami Manabu,
Hayashida Kazutaka,
Sawamura Tatsuya,
Kita Toru,
Yonehara Shin
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02774-0
Subject(s) - scavenger receptor , fibronectin , chemistry , chondroitin sulfate , adhesion , cell adhesion , chinese hamster ovary cell , receptor , lipoprotein , biochemistry , low density lipoprotein , lectin , cd36 , biophysics , microbiology and biotechnology , extracellular matrix , cell , glycosaminoglycan , biology , cholesterol , organic chemistry
Lectin‐like oxidized lipoprotein receptor‐1 (LOX‐1) is a specific receptor for atherogenic oxidized low density lipoprotein (OxLDL) which belongs to the scavenger receptor family. In the present report, we show that LOX‐1 can also support cell adhesion to fibronectin (FN) in a divalent cation‐independent fashion. CHO‐K1 cells stably expressing bovine LOX‐1 (BLOX‐1‐CHO), but not untransfected CHO‐K1 cells, can adhere to FN‐coated plates, but not to collagen‐coated plates, in the presence of EDTA. BLOX‐1‐CHO adhesion to FN‐coated plates can also be suppressed by scavenger receptor ligands, such as OxLDL, polyinosinic acid (poly I), and dextran sulfate, but not by native LDL, acetylated LDL, polycytidylic acid (poly C), or chondroitin sulfate. Cultured bovine aortic endothelial cells can similarly adhere to FN‐coated plates, which was inhibited by OxLDL, poly I, and dextran sulfate in the presence of EDTA. LOX‐1 may play an important role in cell adhesion to FN in an integrin‐independent manner.