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Aminoacyl‐tRNA synthetase‐interacting multi‐functional protein, p43, is imported to endothelial cells via lipid rafts
Author(s) -
Yi JaeSung,
Lee JiYeon,
Chi SungGil,
Kim JiHyun,
Park Sang Gyu,
Kim Sunghoon,
Ko YoungGyu
Publication year - 2005
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.20632
Subject(s) - lipid raft , microbiology and biotechnology , cholera toxin , biology , angiogenesis , biochemistry , chemistry , signal transduction , cancer research
An aminoacyl‐tRNA synthetase subunit, p43, was previously demonstrated to be released from mammalian cells, and to function as an extracellular regulator of both angiogenesis and inflammatory responses (Ko et al., [2001] J Biol Chem, 276; 23028; Park et al.[2002], J Biol Chem 277; 45243). Here, we report that p43 is internalized to the endothelial cells via lipid rafts. Exogenous p43 was co‐localized on bovine aorta endothelial cells with cholera toxin B (CTB), which binds to cholesterol‐enriched lipid rafts. The p43 was rapidly internalized to the cells, as early as 5 min after binding to the surfaces of the cells. p43 bound to the isolated lipid rafts, and its interaction with the lipid rafts, was prevented by high salt content, but not by detergent. This suggests that ionic bonds are involved in the molecular association of p43 with the lipid rafts. Taken together, we conclude that p43 binds to the endothelial cell surface via lipid rafts. J. Cell. Biochem. © 2005 Wiley‐Liss, Inc.