Advertisement

Research Article Free access | 10.1172/JCI117506

Proteoglycan form of macrophage colony-stimulating factor binds low density lipoprotein.

S Suzu, T Inaba, N Yanai, T Kawashima, N Yamada, T Oka, R Machinami, T Ohtsuki, F Kimura, and S Kondo

Biochemical Research Laboratory, Morinaga Milk Industry Co., Ltd., Kanagawa, Japan.

Find articles by Suzu, S. in: JCI | PubMed | Google Scholar

Biochemical Research Laboratory, Morinaga Milk Industry Co., Ltd., Kanagawa, Japan.

Find articles by Inaba, T. in: JCI | PubMed | Google Scholar

Biochemical Research Laboratory, Morinaga Milk Industry Co., Ltd., Kanagawa, Japan.

Find articles by Yanai, N. in: JCI | PubMed | Google Scholar

Biochemical Research Laboratory, Morinaga Milk Industry Co., Ltd., Kanagawa, Japan.

Find articles by Kawashima, T. in: JCI | PubMed | Google Scholar

Biochemical Research Laboratory, Morinaga Milk Industry Co., Ltd., Kanagawa, Japan.

Find articles by Yamada, N. in: JCI | PubMed | Google Scholar

Biochemical Research Laboratory, Morinaga Milk Industry Co., Ltd., Kanagawa, Japan.

Find articles by Oka, T. in: JCI | PubMed | Google Scholar

Biochemical Research Laboratory, Morinaga Milk Industry Co., Ltd., Kanagawa, Japan.

Find articles by Machinami, R. in: JCI | PubMed | Google Scholar

Biochemical Research Laboratory, Morinaga Milk Industry Co., Ltd., Kanagawa, Japan.

Find articles by Ohtsuki, T. in: JCI | PubMed | Google Scholar

Biochemical Research Laboratory, Morinaga Milk Industry Co., Ltd., Kanagawa, Japan.

Find articles by Kimura, F. in: JCI | PubMed | Google Scholar

Biochemical Research Laboratory, Morinaga Milk Industry Co., Ltd., Kanagawa, Japan.

Find articles by Kondo, S. in: JCI | PubMed | Google Scholar

Published October 1, 1994 - More info

Published in Volume 94, Issue 4 on October 1, 1994
J Clin Invest. 1994;94(4):1637–1641. https://doi.org/10.1172/JCI117506.
© 1994 The American Society for Clinical Investigation
Published October 1, 1994 - Version history
View PDF
Abstract

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.

Images.

Browse pages

Click on an image below to see the page. View PDF of the complete article

Version history
  • Version 1 (October 1, 1994): No description
Advertisement
Advertisement