| pubmed-article:8920951 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8920951 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:8920951 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:8920951 | lifeskim:mentions | umls-concept:C0237401 | lld:lifeskim |
| pubmed-article:8920951 | lifeskim:mentions | umls-concept:C0079784 | lld:lifeskim |
| pubmed-article:8920951 | lifeskim:mentions | umls-concept:C0010654 | lld:lifeskim |
| pubmed-article:8920951 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:8920951 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:8920951 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:8920951 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8920951 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8920951 | pubmed:dateCreated | 1996-12-30 | lld:pubmed |
| pubmed-article:8920951 | pubmed:abstractText | The shortest form of human macrophage colony-stimulating factor (M-CSF alpha, CSF-1(256) is expressed on the cell surface as a homodimeric type I transmembrane glycoprotein. The seven cysteine residues in CSF-1(256) form three intrachain disulfide bonds (Cys7-Cys90, Cys48-Cys139, and Cys 102-Cys146), and one interchain disulfide bond (Cys31-Cys31). To examine the role of the seven cysteine residues in CSF-1(256), we replaced each half-cystine by a serine using site-directed mutagenesis, and stably expressed the mutated genes in mouse NIH 3T3 cells. We showed that each of the seven cysteines of CSF-1(256) is essential for its biological activity. Our data further show that substitution of Cys48 or Cys139 totally blocked dimer formation and cell surface expression of CSF-1(256), and that substitution of Cys102 and Cys146 severely impaired CSF-1 dimer formation and cell surface expression. In contrast, substitution of Cys7 or Cys90 affected CSF-1 dimer formation to a lesser degree but did not significantly affect cell surface expression of CSF-1. Furthermore, disruption of the interchain disulfide bond led to efficient cell surface expression of monomeric CSF-1. All of the cell surface expressed mutant CSF-1 proteins, either dimeric or monomeric, still underwent efficient ectodomain cleavage. The electrophoretic mobilities of the cleaved dimeric ectodomains of these mutant CSF-1 proteins on SDS-PAGE exhibited distinctly different patterns as compared with the wild type. Substitution of either Cys7 or Cys90 produced the same shift, while substitution of either Cys102 or Cys146 resulted in a shift distinct from that caused by substitution of Cys7 or Cys90. These data suggest that replacement of either of a pair of intrachain half-cystine residues results in similar conformational changes, and may provide a novel method for mapping intrachain disulfide bonds in dimeric proteins. | lld:pubmed |
| pubmed-article:8920951 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8920951 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8920951 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8920951 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8920951 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8920951 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8920951 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8920951 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8920951 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8920951 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8920951 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:8920951 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:8920951 | pubmed:author | pubmed-author:RettenmierC... | lld:pubmed |
| pubmed-article:8920951 | pubmed:author | pubmed-author:PattengaleP... | lld:pubmed |
| pubmed-article:8920951 | pubmed:author | pubmed-author:WangY LYL | lld:pubmed |
| pubmed-article:8920951 | pubmed:author | pubmed-author:DengPP | lld:pubmed |
| pubmed-article:8920951 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8920951 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:8920951 | pubmed:volume | 228 | lld:pubmed |
| pubmed-article:8920951 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8920951 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8920951 | pubmed:pagination | 557-66 | lld:pubmed |
| pubmed-article:8920951 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:8920951 | pubmed:meshHeading | pubmed-meshheading:8920951-... | lld:pubmed |
| pubmed-article:8920951 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8920951 | pubmed:articleTitle | The role of individual cysteine residues in the processing, structure, and function of human macrophage colony-stimulating factor. | lld:pubmed |
| pubmed-article:8920951 | pubmed:affiliation | Department of Pathology, Childrens Hospital of Los Angeles, USA. | lld:pubmed |
| pubmed-article:8920951 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8920951 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8920951 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
