TY - JOUR
T1 - Aminoacyl-tRNA synthetase-interacting multi-functional protein, p43, is imported to endothelial cells via lipid rafts
AU - Yi, Jae Sung
AU - Lee, Ji Yeon
AU - Chi, Sung Gil
AU - Kim, Ji Hyun
AU - Park, Sang Gyu
AU - Kim, Sunghoon
AU - Ko, Young Gyu
PY - 2005/12/15
Y1 - 2005/12/15
N2 - 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.
AB - 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.
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U2 - 10.1002/jcb.20632
DO - 10.1002/jcb.20632
M3 - Article
C2 - 16167337
AN - SCOPUS:27944501019
VL - 96
SP - 1286
EP - 1295
JO - Journal of supramolecular structure and cellular biochemistry
JF - Journal of supramolecular structure and cellular biochemistry
SN - 0730-2312
IS - 6
ER -