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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
1992-4-2
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pubmed:abstractText |
Chinese hamster ovary cells transfected with a 4.0-kilobase macrophage colony-stimulating factor (M-CSF) cDNA express two different M-CSF species; one has an apparent molecular weight of 85,000 and is identified as a homodimer of a 43-kDa subunit, and the other has an indeterminate structure greater than 200 kDa. In this study, we investigated the structure of the high molecular weight M-CSF by immunochemical procedures. The high molecular weight M-CSF was easily purified, since it bound tightly to DEAE-Sephacel and eluted at a characteristically high salt concentration. The high molecular weight M-CSF migrated as a diffuse band of over than 200,000 on nonreducing sodium dodecyl sulfate-polyacrylamide gels. Analysis of the same samples under reducing conditions revealed that the larger species consisted of a heteromer of the 43- and 150-200-kDa M-CSF subunits. Digestion of the 150-200-kDa M-CSF subunit with chondroitinase, which degrades the chondroitin sulfate glycosaminoglycan chain, yielded a 100 kDa band. This species was secreted instead of 150-200-kDa species when the cells were cultured in the presence of beta-D-xyloside, which inhibits the elongation of the chondroitin sulfate glycosaminoglycan chain in proteoglycans, providing additional evidence for the existence of a chondroitin sulfate chain in the 150-200-kDa M-CSF subunit. Removal of O- and N-linked carbohydrate from the 150-200-kDa subunit yielded a polypeptide chain with a larger molecular mass (approximately 45 kDa) than that of the 43-kDa subunit (approximately 25 kDa). Collectively, these results indicate that the 150-200-kDa M-CSF subunit is a proteoglycan with a core protein that may be an alternatively processed form of M-CSF.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
267
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4345-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1531650-Animals,
pubmed-meshheading:1531650-Blotting, Western,
pubmed-meshheading:1531650-CHO Cells,
pubmed-meshheading:1531650-Chromatography, Ion Exchange,
pubmed-meshheading:1531650-Cricetinae,
pubmed-meshheading:1531650-DNA,
pubmed-meshheading:1531650-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1531650-Fibrinolysin,
pubmed-meshheading:1531650-Glycosaminoglycans,
pubmed-meshheading:1531650-Humans,
pubmed-meshheading:1531650-Macrophage Colony-Stimulating Factor,
pubmed-meshheading:1531650-Molecular Weight
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pubmed:year |
1992
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pubmed:articleTitle |
Identification of a high molecular weight macrophage colony-stimulating factor as a glycosaminoglycan-containing species.
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pubmed:affiliation |
Biochemical Research Laboratory, Morinaga Milk Industry Co, Ltd., Kanagawa, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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