Linked Life Data

11337488

Source:http://linkedlifedata.com/resource/pubmed/id/11337488

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
2001-7-23
pubmed:abstractText
We introduced various mutations and modifications in the GPI anchoring signal of rat acetylcholinesterase (AChE). 1) The resulting mutants, expressed in transiently transfected COS cells, were initially produced at the same rate, in an active form, but the fraction of GPI-anchored AChE and the steady state level of AChE activity varied over a wide range. 2) Productive interaction with the GPI addition machinery led to GPI anchoring, secretion of uncleaved protein, and secretion of a cleaved protein, in variable proportions. Unproductive interaction led to degradation; poorly processed molecules were degraded rather than retained intracellularly or secreted. 3) An efficient glypiation appeared necessary but not sufficient for a high level of secretion; the cleaved, secreted protein was possibly generated as a by-product of transamidation. 4) Glypiation was influenced by a wider context than the triplet omega/omega + 1/omega + 2, particularly omega - 1. 5) Glypiation was not affected by the closeness of the omega site to the alpha(10) helix of the catalytic domain. 6) A cysteine could simultaneously form a disulfide bond and serve as an omega site; however, there was a mutual interference between glypiation and the formation of an intercatenary disulfide bond, at a short distance upstream of omega. 7) Glypiation was not affected by the presence of an N-glycosylation site at omega or in its vicinity or by the addition of a short hydrophilic, highly charged peptide (FLAG; DYKDDDDK) at the C terminus of the hydrophobic region.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27881-92
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:11337488-Acetylcholinesterase, pubmed-meshheading:11337488-Amino Acid Sequence, pubmed-meshheading:11337488-Animals, pubmed-meshheading:11337488-COS Cells, pubmed-meshheading:11337488-Catalytic Domain, pubmed-meshheading:11337488-Cells, Cultured, pubmed-meshheading:11337488-DNA, Complementary, pubmed-meshheading:11337488-Disulfides, pubmed-meshheading:11337488-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:11337488-Epitopes, pubmed-meshheading:11337488-Molecular Sequence Data, pubmed-meshheading:11337488-Mutagenesis, Site-Directed, pubmed-meshheading:11337488-Mutation, pubmed-meshheading:11337488-Peptides, pubmed-meshheading:11337488-Phosphatidylinositol Diacylglycerol-Lyase, pubmed-meshheading:11337488-Phosphatidylinositols, pubmed-meshheading:11337488-Precipitin Tests, pubmed-meshheading:11337488-Rats, pubmed-meshheading:11337488-Recombinant Fusion Proteins, pubmed-meshheading:11337488-Sucrose, pubmed-meshheading:11337488-Transfection, pubmed-meshheading:11337488-Type C Phospholipases
pubmed:year
2001
pubmed:articleTitle
Addition of a glycophosphatidylinositol to acetylcholinesterase. Processing, degradation, and secretion.
pubmed:affiliation
Laboratoire de Neurobiologie Moléculaire et Cellulaire, CNRS UMR 8544, Ecole Normale Supérieure, 46 rue d'Ulm, 75005 Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't