| pubmed-article:7499838 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7499838 | lifeskim:mentions | umls-concept:C0033692 | lld:lifeskim |
| pubmed-article:7499838 | lifeskim:mentions | umls-concept:C0017973 | lld:lifeskim |
| pubmed-article:7499838 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:7499838 | lifeskim:mentions | umls-concept:C0728940 | lld:lifeskim |
| pubmed-article:7499838 | lifeskim:mentions | umls-concept:C1514570 | lld:lifeskim |
| pubmed-article:7499838 | lifeskim:mentions | umls-concept:C0015252 | lld:lifeskim |
| pubmed-article:7499838 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:7499838 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:7499838 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:7499838 | pubmed:dateCreated | 1996-1-18 | lld:pubmed |
| pubmed-article:7499838 | pubmed:abstractText | A proteoglycan had been isolated from the conditioned media of a human osteosarcoma cell line and had tentatively been named proteoglycan-100 (PG-100) because of the size of its core glycoprotein. Amino acid sequencing of the purified proteoglycan and cDNA analysis were consistent with the assumption that PG-100 is identical with the proteoglycan form of CSF-1 (or macrophage colony-stimulating factor). PG-100 induced mouse macrophage differentiation. Proliferation of macrophages was stimulated in a dose-dependent manner. On a molar basis, however, about 100- to 300-fold higher doses of PG-100 than of recombinant human (rh)CSF-1 were required for the half-maximal growth-stimulating effect. Upon enzymatic removal of the glycosaminoglycan chain, the purified core protein exhibited higher activity, but was still about 20-fold less active than rhCSF-1. Incubation of the purified proteoglycan for 48 h at 37 degrees C led to the formation of a glycosaminoglycan-free 50-kDa fragment either by autoproteolysis or by the action of a protease not yet identified. The purified fragment exhibited almost the same biologic activity as rhCSF-1. The glycosaminoglycan chain of the growth factor was not only shown to inhibit CSF-1 activity but also to increase the stability of the core protein when the CSF-1-producing osteosarcoma cells were maintained in a collagen lattice. These findings provide a link between a soluble, highly active cytokine and its extracellular matrix storage form of comparatively low activity. | lld:pubmed |
| pubmed-article:7499838 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7499838 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499838 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:7499838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7499838 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7499838 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:7499838 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:7499838 | pubmed:author | pubmed-author:KresseHH | lld:pubmed |
| pubmed-article:7499838 | pubmed:author | pubmed-author:KölschEE | lld:pubmed |
| pubmed-article:7499838 | pubmed:author | pubmed-author:SchwarzKK | lld:pubmed |
| pubmed-article:7499838 | pubmed:author | pubmed-author:PartenheimerA... | lld:pubmed |
| pubmed-article:7499838 | pubmed:author | pubmed-author:WrocklageCC | lld:pubmed |
| pubmed-article:7499838 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7499838 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:7499838 | pubmed:volume | 155 | lld:pubmed |
| pubmed-article:7499838 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7499838 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7499838 | pubmed:pagination | 5557-65 | lld:pubmed |
| pubmed-article:7499838 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:7499838 | pubmed:meshHeading | pubmed-meshheading:7499838-... | lld:pubmed |
| pubmed-article:7499838 | pubmed:meshHeading | pubmed-meshheading:7499838-... | lld:pubmed |
| pubmed-article:7499838 | pubmed:meshHeading | pubmed-meshheading:7499838-... | lld:pubmed |
| pubmed-article:7499838 | pubmed:meshHeading | pubmed-meshheading:7499838-... | lld:pubmed |
| pubmed-article:7499838 | pubmed:meshHeading | pubmed-meshheading:7499838-... | lld:pubmed |
| pubmed-article:7499838 | pubmed:meshHeading | pubmed-meshheading:7499838-... | lld:pubmed |
| pubmed-article:7499838 | pubmed:meshHeading | pubmed-meshheading:7499838-... | lld:pubmed |
| pubmed-article:7499838 | pubmed:meshHeading | pubmed-meshheading:7499838-... | lld:pubmed |
| pubmed-article:7499838 | pubmed:meshHeading | pubmed-meshheading:7499838-... | lld:pubmed |
| pubmed-article:7499838 | pubmed:meshHeading | pubmed-meshheading:7499838-... | lld:pubmed |
| pubmed-article:7499838 | pubmed:meshHeading | pubmed-meshheading:7499838-... | lld:pubmed |
| pubmed-article:7499838 | pubmed:meshHeading | pubmed-meshheading:7499838-... | lld:pubmed |
| pubmed-article:7499838 | pubmed:meshHeading | pubmed-meshheading:7499838-... | lld:pubmed |
| pubmed-article:7499838 | pubmed:meshHeading | pubmed-meshheading:7499838-... | lld:pubmed |
| pubmed-article:7499838 | pubmed:meshHeading | pubmed-meshheading:7499838-... | lld:pubmed |
| pubmed-article:7499838 | pubmed:meshHeading | pubmed-meshheading:7499838-... | lld:pubmed |
| pubmed-article:7499838 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7499838 | pubmed:articleTitle | Proteoglycan form of colony-stimulating factor-1 (proteoglycan-100). Stimulation of activity by glycosaminoglycan removal and proteolytic processing. | lld:pubmed |
| pubmed-article:7499838 | pubmed:affiliation | Institute of Immunology, University of Münster, Germany. | lld:pubmed |
| pubmed-article:7499838 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7499838 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7499838 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7499838 | lld:pubmed |
