In vitro attachment of glycosyl-inositolphospholipid anchor structures to mouse Thy-1 antigen and human decay-accelerating factor.

Détails

ID Serval
serval:BIB_3A8094F6471B
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
In vitro attachment of glycosyl-inositolphospholipid anchor structures to mouse Thy-1 antigen and human decay-accelerating factor.
Périodique
Proceedings of the National Academy of Sciences of the United States of America
Auteur(s)
Fasel N., Rousseaux M., Schaerer E., Medof M.E., Tykocinski M.L., Bron C.
ISSN
0027-8424 (Print)
ISSN-L
0027-8424
Statut éditorial
Publié
Date de publication
1989
Volume
86
Numéro
18
Pages
6858-6862
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
Publication Status: ppublish
Résumé
Glycosyl-inositolphospholipid (GPL) anchoring structures are incorporated into GPL-anchored proteins immediately posttranslationally in the rough endoplasmic reticulum, but the biochemical and cellular constituents involved in this "glypiation" process are unknown. To establish whether glypiation could be achieved in vitro, mRNAs generated by transcription of cDNAs encoding two GPL-anchored proteins, murine Thy-1 antigen and human decay-accelerating factor (DAF), and a conventionally anchored control protein, polymeric-immunoglobulin receptor (IgR), were translated in a rabbit reticulocyte lysate. Upon addition of dog pancreatic rough microsomes, nascent polypeptides generated from the three mRNAs translocated into vesicles. Dispersal of the vesicles with Triton X-114 detergent and incubation of the hydrophobic phase with phosphatidylinositol-specific phospholipases C and D, enzymes specific for GPL-anchor structures, released Thy-1 and DAF but not IgR protein into the aqueous phase. The selective incorporation of phospholipase-sensitive anchoring moieties into Thy-1 and DAF but not IgR translation products during in vitro translocation indicates that rough microsomes are able to support and regulate glypiation.
Mots-clé
Animals, Antigens, CD55, Antigens, Surface/genetics, Antigens, Surface/isolation & purification, Antigens, Thy-1, Blood Proteins/genetics, Complement Inactivator Proteins/genetics, Endoplasmic Reticulum/metabolism, Glycolipids/metabolism, Glycosylphosphatidylinositols, Humans, Membrane Proteins/genetics, Membrane Proteins/isolation & purification, Mice, Molecular Weight, Phosphatidylinositols/metabolism, Plasmids, Protein Biosynthesis, Protein Processing, Post-Translational, RNA, Messenger/genetics, RNA, Messenger/isolation & purification, Rabbits, Reticulocytes/metabolism, Transcription, Genetic
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 16:02
Dernière modification de la notice
20/08/2019 14:30
Données d'usage