| pubmed-article:2318860 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2318860 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:2318860 | lifeskim:mentions | umls-concept:C0699040 | lld:lifeskim |
| pubmed-article:2318860 | lifeskim:mentions | umls-concept:C0040688 | lld:lifeskim |
| pubmed-article:2318860 | lifeskim:mentions | umls-concept:C1527195 | lld:lifeskim |
| pubmed-article:2318860 | lifeskim:mentions | umls-concept:C1522240 | lld:lifeskim |
| pubmed-article:2318860 | lifeskim:mentions | umls-concept:C0079411 | lld:lifeskim |
| pubmed-article:2318860 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:2318860 | pubmed:dateCreated | 1990-5-10 | lld:pubmed |
| pubmed-article:2318860 | pubmed:abstractText | The precursor for transforming growth factor-alpha (TGF-alpha) is a membrane glycoprotein that can establish contact with epidermal growth factor/TGF-alpha receptors on adjacent cells or can be cleaved to release TGF-alpha that diffuses into the medium. Cleavage of pro-TGF-alpha occurs at Ala/Leu-Ala/Leu-Ala-Val-Val sites located at each end of the mature TGF-alpha sequence. To characterize the cleavage process of pro-TGF-alpha and the role of glycosylation in this process, we have introduced a pro-TGF-alpha expression vector in wild type Chinese hamster ovary (CHO) cells and in the mutant CHO cell clone ldlD that has a reversible defect in protein glycosylation. Analysis of metabolically labeled and cell surface-labeled products immunoprecipitated with antibodies directed against the extracellular TGF-alpha sequence and the cytoplasmic pro-TGF-alpha C-terminal domain shows that cleavage of pro-TGF-alpha in wild type CHO cells occurs in two steps. Both processing steps occur after pro-TGF-alpha reaches the cell surface. In the first step, pro-TGF-alpha rapidly (t1/2 = 30 min) loses the amino-terminal segment that precedes the TGF-alpha sequence. In the second step, pro-TGF-alpha is cleaved at the carboxyl terminus of the TGF-alpha sequence releasing this factor into the medium. This second step is slow (t1/2 = 2 h). The action of pancreatic elastase added to CHO-TGF-alpha cells mimics the first step but not the second one. Synthesis, cell surface exposure, rate of cleavage, and generation of bioactive TGF-alpha in ldlD-TGF-alpha cells are not markedly affected by the lack of N-acetylgalactosamine-dependent protein O-glycosylation or galactose-dependent glycan chain modification. The results indicate that, despite their similarity in amino acid sequence, the two cleavage sites that flank TGF-alpha may be processed with different kinetics which can lead to retention of pro-TGF-alpha on the cell surface. | lld:pubmed |
| pubmed-article:2318860 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2318860 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2318860 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2318860 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2318860 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2318860 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2318860 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2318860 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:2318860 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:2318860 | pubmed:author | pubmed-author:LeeD CDC | lld:pubmed |
| pubmed-article:2318860 | pubmed:author | pubmed-author:WongS TST | lld:pubmed |
| pubmed-article:2318860 | pubmed:author | pubmed-author:MassaguéJJ | lld:pubmed |
| pubmed-article:2318860 | pubmed:author | pubmed-author:TeixidoJJ | lld:pubmed |
| pubmed-article:2318860 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2318860 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2318860 | pubmed:volume | 265 | lld:pubmed |
| pubmed-article:2318860 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2318860 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2318860 | pubmed:pagination | 6410-5 | lld:pubmed |
| pubmed-article:2318860 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:2318860 | pubmed:meshHeading | pubmed-meshheading:2318860-... | lld:pubmed |
| pubmed-article:2318860 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2318860 | pubmed:articleTitle | Generation of transforming growth factor-alpha from the cell surface by an O-glycosylation-independent multistep process. | lld:pubmed |
| pubmed-article:2318860 | pubmed:affiliation | Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, New York 10021. | lld:pubmed |
| pubmed-article:2318860 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2318860 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2318860 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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