pubmed-article:2895421 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2895421 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:2895421 | lifeskim:mentions | umls-concept:C0040100 | lld:lifeskim |
pubmed-article:2895421 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
pubmed-article:2895421 | lifeskim:mentions | umls-concept:C0017950 | lld:lifeskim |
pubmed-article:2895421 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
pubmed-article:2895421 | lifeskim:mentions | umls-concept:C1524062 | lld:lifeskim |
pubmed-article:2895421 | lifeskim:mentions | umls-concept:C0456387 | lld:lifeskim |
pubmed-article:2895421 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:2895421 | pubmed:dateCreated | 1988-5-4 | lld:pubmed |
pubmed-article:2895421 | pubmed:abstractText | Recent evidence shows that the mature Thy-1 surface glycoprotein lacks the C-terminal amino acids 113 to 143 predicted from the cDNA sequence and is anchored in the plasma membrane by a complex, phosphatidylinositol-containing glycolipid attached to the alpha-carboxyl group of amino acid 112. Here we studied the biosynthesis of Thy-1 in two previously described and two newly isolated Thy-1-deficient mutant cell lines. Somatic cell hybridization indicated that their mutations affected some processing step rather than the Thy-1 structural gene. The Thy-1 made by mutants of classes C, F, and H bound detergent but, in contrast to wild-type Thy-1, their detergent-binding moieties could not be removed by phospholipase C. In addition, tryptophan, which only occurs in position 124, was incorporated into Thy-1 of these mutants but not of wild-type cells. Last, the Thy-1 of wild-type but not mutant cells could be radiolabeled with [3H]palmitic acid. Together, these findings strongly suggest that mutants of classes C, F, and H accumulate a biosynthetic intermediate of Thy-1 which retains at least part of the hydrophobic C-terminal peptide. The Thy-1 of these mutants remained endoglycosidase H sensitive, suggesting that it accumulated in the rough endoplasmic reticulum or the Cis-Golgi. A different Thy-1 intermediate was found in a class B mutant cell line: the Thy-1 of this mutant was 2 kilodaltons smaller than the Thy-1 of other cell lines, did not bind detergent, and was rapidly secreted via a normal secretory pathway. | lld:pubmed |
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pubmed-article:2895421 | pubmed:language | eng | lld:pubmed |
pubmed-article:2895421 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2895421 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:2895421 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2895421 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2895421 | pubmed:month | Feb | lld:pubmed |
pubmed-article:2895421 | pubmed:issn | 0270-7306 | lld:pubmed |
pubmed-article:2895421 | pubmed:author | pubmed-author:BrosXX | lld:pubmed |
pubmed-article:2895421 | pubmed:author | pubmed-author:HymanRR | lld:pubmed |
pubmed-article:2895421 | pubmed:author | pubmed-author:ConzelmannAA | lld:pubmed |
pubmed-article:2895421 | pubmed:author | pubmed-author:SpiazziAA | lld:pubmed |
pubmed-article:2895421 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2895421 | pubmed:volume | 8 | lld:pubmed |
pubmed-article:2895421 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2895421 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2895421 | pubmed:pagination | 674-8 | lld:pubmed |
pubmed-article:2895421 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:2895421 | pubmed:year | 1988 | lld:pubmed |
pubmed-article:2895421 | pubmed:articleTitle | No glycolipid anchors are added to Thy-1 glycoprotein in Thy-1-negative mutant thymoma cells of four different complementation classes. | lld:pubmed |
pubmed-article:2895421 | pubmed:affiliation | Institut de Biochimie, Université de Lausanne, Epalinges, Switzerland. | lld:pubmed |
pubmed-article:2895421 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2895421 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2895421 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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