| pubmed-article:2787329 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2787329 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:2787329 | lifeskim:mentions | umls-concept:C0079784 | lld:lifeskim |
| pubmed-article:2787329 | lifeskim:mentions | umls-concept:C0086934 | lld:lifeskim |
| pubmed-article:2787329 | lifeskim:mentions | umls-concept:C1274040 | lld:lifeskim |
| pubmed-article:2787329 | lifeskim:mentions | umls-concept:C0017982 | lld:lifeskim |
| pubmed-article:2787329 | lifeskim:mentions | umls-concept:C1514570 | lld:lifeskim |
| pubmed-article:2787329 | lifeskim:mentions | umls-concept:C0019409 | lld:lifeskim |
| pubmed-article:2787329 | lifeskim:mentions | umls-concept:C0443199 | lld:lifeskim |
| pubmed-article:2787329 | lifeskim:mentions | umls-concept:C1523987 | lld:lifeskim |
| pubmed-article:2787329 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2787329 | pubmed:dateCreated | 1989-8-25 | lld:pubmed |
| pubmed-article:2787329 | pubmed:abstractText | The single gene for human macrophage colony-stimulating factor (M-CSF, or CSF-1) generates multiple mRNA species that diverge within the coding region. We have characterized translation products of these mRNA species from native and recombinant sources. Immunoblots of reduced native M-CSF indicate that multiple glycosylated species ranging from 25 kd to 200 kd are secreted by human monocytes and cell lines. In contrast, CV-1 cells expressing a short M-CSF clone secrete only 24 kd recombinant M-CSF. Synthetic peptide antibodies were developed to distinguish between secreted recombinant M-CSF from long and short mRNA splicing variants. Immunoblot analysis indicates that alternative mRNA splicing generates some M-CSF protein heterogeneity. Most secreted MIA PaCa-2 M-CSF reacts with long-clone-specific antibody. Lectin affinity chromatography shows that variable glycosylation contributes significantly to MIA PaCa-2 M-CSF size heterogeneity. In addition, cell lysates also contain larger M-CSF species that apparently undergo proteolytic processing before secretion. The data indicate that M-CSF protein heterogeneity results from both pre- and post-translational processing. | lld:pubmed |
| pubmed-article:2787329 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2787329 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2787329 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2787329 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2787329 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2787329 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2787329 | pubmed:month | May | lld:pubmed |
| pubmed-article:2787329 | pubmed:issn | 0730-2312 | lld:pubmed |
| pubmed-article:2787329 | pubmed:author | pubmed-author:NiteckiD EDE | lld:pubmed |
| pubmed-article:2787329 | pubmed:author | pubmed-author:KothsKK | lld:pubmed |
| pubmed-article:2787329 | pubmed:author | pubmed-author:AldwinLL | lld:pubmed |
| pubmed-article:2787329 | pubmed:author | pubmed-author:ShadleP JPJ | lld:pubmed |
| pubmed-article:2787329 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2787329 | pubmed:volume | 40 | lld:pubmed |
| pubmed-article:2787329 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2787329 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2787329 | pubmed:pagination | 91-107 | lld:pubmed |
| pubmed-article:2787329 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
| pubmed-article:2787329 | pubmed:meshHeading | pubmed-meshheading:2787329-... | lld:pubmed |
| pubmed-article:2787329 | pubmed:meshHeading | pubmed-meshheading:2787329-... | lld:pubmed |
| pubmed-article:2787329 | pubmed:meshHeading | pubmed-meshheading:2787329-... | lld:pubmed |
| pubmed-article:2787329 | pubmed:meshHeading | pubmed-meshheading:2787329-... | lld:pubmed |
| pubmed-article:2787329 | pubmed:meshHeading | pubmed-meshheading:2787329-... | lld:pubmed |
| pubmed-article:2787329 | pubmed:meshHeading | pubmed-meshheading:2787329-... | lld:pubmed |
| pubmed-article:2787329 | pubmed:meshHeading | pubmed-meshheading:2787329-... | lld:pubmed |
| pubmed-article:2787329 | pubmed:meshHeading | pubmed-meshheading:2787329-... | lld:pubmed |
| pubmed-article:2787329 | pubmed:meshHeading | pubmed-meshheading:2787329-... | lld:pubmed |
| pubmed-article:2787329 | pubmed:meshHeading | pubmed-meshheading:2787329-... | lld:pubmed |
| pubmed-article:2787329 | pubmed:meshHeading | pubmed-meshheading:2787329-... | lld:pubmed |
| pubmed-article:2787329 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2787329 | pubmed:articleTitle | Human macrophage colony-stimulating factor heterogeneity results from alternative mRNA splicing, differential glycosylation, and proteolytic processing. | lld:pubmed |
| pubmed-article:2787329 | pubmed:affiliation | Department of Protein Chemistry, Cetus Corporation, Emeryville, California 94608. | lld:pubmed |
| pubmed-article:2787329 | pubmed:publicationType | Journal Article | lld:pubmed |
