| pubmed-article:8730102 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8730102 | lifeskim:mentions | umls-concept:C0008109 | lld:lifeskim |
| pubmed-article:8730102 | lifeskim:mentions | umls-concept:C2752508 | lld:lifeskim |
| pubmed-article:8730102 | lifeskim:mentions | umls-concept:C0031676 | lld:lifeskim |
| pubmed-article:8730102 | lifeskim:mentions | umls-concept:C1327616 | lld:lifeskim |
| pubmed-article:8730102 | lifeskim:mentions | umls-concept:C1167322 | lld:lifeskim |
| pubmed-article:8730102 | lifeskim:mentions | umls-concept:C0001044 | lld:lifeskim |
| pubmed-article:8730102 | lifeskim:mentions | umls-concept:C1706395 | lld:lifeskim |
| pubmed-article:8730102 | lifeskim:mentions | umls-concept:C0013138 | lld:lifeskim |
| pubmed-article:8730102 | lifeskim:mentions | umls-concept:C0037081 | lld:lifeskim |
| pubmed-article:8730102 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:8730102 | lifeskim:mentions | umls-concept:C1624581 | lld:lifeskim |
| pubmed-article:8730102 | lifeskim:mentions | umls-concept:C1527177 | lld:lifeskim |
| pubmed-article:8730102 | lifeskim:mentions | umls-concept:C0441513 | lld:lifeskim |
| pubmed-article:8730102 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:8730102 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:8730102 | lifeskim:mentions | umls-concept:C1293132 | lld:lifeskim |
| pubmed-article:8730102 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:8730102 | pubmed:dateCreated | 1996-10-17 | lld:pubmed |
| pubmed-article:8730102 | pubmed:abstractText | Despite advances in understanding the cell biology of glycoinositol phospholipid (GPI)-anchored proteins in cultured cells, the in vivo functions of GPI anchors have remained elusive. We have focused on Drosophila acetylcholinesterase (AChE) as a model GPI-anchored protein that can be manipulated in vivo with sophisticated genetic techniques. In Drosophila, AChE is found only as a GPI-anchored G2 form encoded by the Ace locus on the third chromosome. To pursue our goal of replacing wild-type GPI-anchored AChE with forms that have alternative anchor structures in transgenic files, we report the construction of two secreted forms of Drosophila AChE (SEC1 and SEC2) and a chimeric form (TM-AChE) anchored by the transmembrane and cytoplasmic domains of herpes simplex virus type 1 glycoprotein C. To confirm that the biochemical properties of these AChEs were unchanged from GPI-AChE except as predicted, we made stably transfected Drosophila Schneider Line 2(S2) cells expressing each of the four forms. TM-AChE, SEC1, and SEC2 had the same catalytic activity and quaternary structure as wild type. TM-AChE was expressed as an amphiphilic membrane-bound protein resistant to an enzyme that cleaves GPI-AChE (phosphatidylinositol-specific phospholipase C), and the same percentage of TM-AChE and GPI-AChE was on the cell surface according to immunofluorescence and pharmacological data. SEC1 and SEC2 were constructed by truncating the C-terminal signal peptide initially present in GPI-AChE: in SEC1 the last 25 residues of this 34-residue peptide were deleted while in SEC2 the last 29 were deleted. Both SEC1 and SEC2 were efficiently secreted and are very stable in culture medium; with one cloned SEC1-expressing line, AChE accumulated to as high as 100 mg/liter. Surprisingly, 5-10% of SEC1 was attached to a GPI anchor, but SEC2 showed no GPI anchoring. Since no differences in catalytic activity were observed among the four AChEs, and since the same percentage of GPI-AChE and TM-AChE were on the cell surface, we contend that in vivo experiments in which GPI-AChE is replaced can be interpreted solely on the basis of the altered anchoring domain. | lld:pubmed |
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| pubmed-article:8730102 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8730102 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8730102 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8730102 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8730102 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8730102 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8730102 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:8730102 | pubmed:author | pubmed-author:RosenberryT... | lld:pubmed |
| pubmed-article:8730102 | pubmed:author | pubmed-author:IncardonaJ... | lld:pubmed |
| pubmed-article:8730102 | pubmed:issnType | Print | lld:pubmed |
