| pubmed-article:2666417 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2666417 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:2666417 | lifeskim:mentions | umls-concept:C0007589 | lld:lifeskim |
| pubmed-article:2666417 | lifeskim:mentions | umls-concept:C0026473 | lld:lifeskim |
| pubmed-article:2666417 | lifeskim:mentions | umls-concept:C1157216 | lld:lifeskim |
| pubmed-article:2666417 | lifeskim:mentions | umls-concept:C1511938 | lld:lifeskim |
| pubmed-article:2666417 | lifeskim:mentions | umls-concept:C0591833 | lld:lifeskim |
| pubmed-article:2666417 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:2666417 | pubmed:dateCreated | 1989-9-7 | lld:pubmed |
| pubmed-article:2666417 | pubmed:abstractText | Murine monocytic leukemic (M1) cells were cultured in the presence of [3H]glucosamine and [35S]sulfate. Labeled proteoglycans were purified by anion exchange chromatography and characterized by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis in combination with chemical and enzymatic degradation. M1 cells synthesize a single predominant species of proteoglycan which distributes almost equally between the cell and medium after 17 h labeling. The cell-associated proteoglycan has an overall size of about 135 kDa and contains three to five chondroitin sulfate chains (28-31 kDa each) attached to a chondroitinase-generated core protein of 28 kDa. The synthesis and subsequent secretion of this proteoglycan was enhanced 4-5-fold in cells induced to differentiate into macrophages. This was not a phenomenon of arrest in the G0/G1 stage of the cell cycle, since density inhibited undifferentiated cells arrested at this stage did not increase proteoglycan synthesis. The chondroitin sulfate chains contained exclusively chondroitin 4- and 6-sulfate; however, the ratio of these two disaccharides differed between the medium- and cell-associated proteoglycans, and changed during progression of the cells into a fully differentiated phenotype. Pulse-chase kinetics indicate the presence of two distinct pools of proteoglycan; one that is secreted very rapidly from the cell after a approximately 1-h lag, and a second pool that is turned over in the cell with a half-time of approximately 3.5 h. Subtle differences in the glycosylation patterns of the medium- and cell-associated species are consistent with synthesis of two pools. Papain digestion suggests that the chondroitin sulfate chains are clustered on a small protease resistant peptide. The data suggest that this proteoglycan is similar to the serglycin proteoglycan family. | lld:pubmed |
| pubmed-article:2666417 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2666417 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2666417 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2666417 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2666417 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2666417 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2666417 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2666417 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2666417 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2666417 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:2666417 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:2666417 | pubmed:author | pubmed-author:BickelMM | lld:pubmed |
| pubmed-article:2666417 | pubmed:author | pubmed-author:HascallV CVC | lld:pubmed |
| pubmed-article:2666417 | pubmed:author | pubmed-author:YanagishitaMM | lld:pubmed |
| pubmed-article:2666417 | pubmed:author | pubmed-author:McQuillanD... | lld:pubmed |
| pubmed-article:2666417 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2666417 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:2666417 | pubmed:volume | 264 | lld:pubmed |
| pubmed-article:2666417 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2666417 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2666417 | pubmed:pagination | 13245-51 | lld:pubmed |
| pubmed-article:2666417 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:2666417 | pubmed:meshHeading | pubmed-meshheading:2666417-... | lld:pubmed |
| pubmed-article:2666417 | pubmed:meshHeading | pubmed-meshheading:2666417-... | lld:pubmed |
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| pubmed-article:2666417 | pubmed:meshHeading | pubmed-meshheading:2666417-... | lld:pubmed |
| pubmed-article:2666417 | pubmed:meshHeading | pubmed-meshheading:2666417-... | lld:pubmed |
| pubmed-article:2666417 | pubmed:meshHeading | pubmed-meshheading:2666417-... | lld:pubmed |
| pubmed-article:2666417 | pubmed:meshHeading | pubmed-meshheading:2666417-... | lld:pubmed |
| pubmed-article:2666417 | pubmed:meshHeading | pubmed-meshheading:2666417-... | lld:pubmed |
| pubmed-article:2666417 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2666417 | pubmed:articleTitle | Proteoglycan biosynthesis in murine monocytic leukemic (M1) cells before and after differentiation. | lld:pubmed |
| pubmed-article:2666417 | pubmed:affiliation | Bone Research Branch, National Institute of Dental Research, Bethesda, Maryland 20892. | lld:pubmed |
| pubmed-article:2666417 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2666417 | lld:pubmed |
