@article{oai:tsukuba.repo.nii.ac.jp:00017621,
 author = {Suzu, S and Inaba, T and Yanai, N and Kawashima, T and 山田, 信博 and YAMADA, Nobuhiro and Oka, T and Machinami, R and Ohtsuki, T and Kimura, F and Kondo, S and Torikata, C and Nagata, N and Motoyoshi, K},
 issue = {4},
 journal = {The journal of clinical investigation},
 month = {Oct},
 note = {We recently isolated a proteoglycan form of macrophage colony-stimulating factor (PG-M-CSF) that carries a chondroitin sulfate glycosaminoglycan chain. Here, we examined the interaction of PG-M-CSF with low density lipoprotein (LDL). When LDL preincubated with PG-M-CSF was fractionated by molecular size sieving chromatography, it was eluted earlier than untreated LDL. When LDL was preincubated with chondroitin sulfate-free 85-kD M-CSF instead of PG-M-CSF, the elution profile of LDL remained unchanged, indicating specific interaction between PG-M-CSF and LDL. The level of PG-M-CSF binding in the wells of a plastic microtitration plate precoated with LDL was significant, this binding being completely abolished by pretreatment of PG-M-CSF with chondroitinase AC, which degrades chondroitin sulfate. The addition of exogenous chondroitin sulfate or apolipoprotein B inhibited the binding of PG-M-CSF to LDL in a dose-dependent manner, indicating that the interaction between PG-M-CSF and LDL was mediated by the binding of the chondroitin sulfate chain of PG-M-CSF to LDL apolipoprotein B. PG-M-CSF was also demonstrated in the arterial wall, and there were increased amounts of PG-M-CSF in atherosclerotic lesions. The in vitro interaction between PG-M-CSF and LDL thus appears to have physiological significance.},
 pages = {1637--1641},
 title = {Proteoglycan form of macrophage colony-stimulating factor binds low density lipoprotein},
 volume = {94},
 year = {1994},
 yomi = {ヤマダ, ノブヒロ}
}