Proteoglycan form of macrophage colony-stimulating factor binds low density lipoprotein
| Autor: | N. Yamada, Shinya Suzu, S Kondo, T Kawashima, Tetsuya Ohtsuki, T Inaba, Fumihiko Kimura, T Oka, R Machinami, N Yanai |
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| Rok vydání: | 1994 |
| Předmět: |
Macrophage colony-stimulating factor
biology Apolipoprotein B Arteriosclerosis Macrophage Colony-Stimulating Factor Chondroitin Sulfates General Medicine Plasma protein binding Lipoproteins LDL Glycosaminoglycan chemistry.chemical_compound Proteoglycan chemistry Biochemistry Low-density lipoprotein biology.protein Humans Chondroitin lipids (amino acids peptides and proteins) Chondroitin sulfate Aorta Research Article Apolipoproteins B Protein Binding |
| Zdroj: | Journal of Clinical Investigation. 94:1637-1641 |
| ISSN: | 0021-9738 |
| DOI: | 10.1172/jci117506 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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