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Titolo:
Comparison of the glycosyl-phosphatidylinositol cleavage/attachment site between mammalian cells and parasitic protozoa
Autore:
White, IJ; Souabni, A; Hooper, NM;
Indirizzi:
Univ Leeds, Sch Biochem & Mol Biol, Leeds LS2 9JT, W Yorkshire, England Univ Leeds Leeds W Yorkshire England LS2 9JT S2 9JT, W Yorkshire, England
Titolo Testata:
JOURNAL OF CELL SCIENCE
fascicolo: 4, volume: 113, anno: 2000,
pagine: 721 - 727
SICI:
0021-9533(200002)113:4<721:COTGCS>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANCHORED MEMBRANE-PROTEINS; KIDNEY MICROVILLAR MEMBRANE; ACID-REQUIREMENTS ADJACENT; TERMINAL SIGNAL PEPTIDE; RENAL DIPEPTIDASE; PHOSPHOLIPASE-C; DIRECTED MUTAGENESIS; ECTO-ENZYMES; GPI ANCHOR; ATTACHMENT;
Keywords:
GPI; variant surface glycoprotein; membrane dipeptidase; transamidase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Hooper, NM Univ Leeds, Sch Biochem & Mol Biol, Leeds LS2 9JT, W Yorkshire,England Univ Leeds Leeds W Yorkshire England LS2 9JT orkshire, England
Citazione:
I.J. White et al., "Comparison of the glycosyl-phosphatidylinositol cleavage/attachment site between mammalian cells and parasitic protozoa", J CELL SCI, 113(4), 2000, pp. 721-727

Abstract

It was previously hypothesised that the requirements for glycosyl-phosphatidylinositol (GPI) anchoring in mammalian cells and parasitic protozoa are similar but not identical. We have investigated this by converting the GPI cleavage/attachment site in porcine membrane dipeptidase to that found in the trypanosomal variant surface glycoprotein 117 and expressing the resulting mutants in COS-1 cells. Changing the entire omega, omega+1 and omega+2 triplet in membrane dipeptidase from Ser-Ala-Ala to Asp-Ser-Ser resulted in efficient GPI anchoring of the mutant proteins, as assessed by cell-surfaceactivity assays and susceptibility to release by phosphatidylinositol-specific phospholipase C. Immunoelectrophoretic blot analysis with antibodies recognising epitopes either side of the native omega residue in porcine membrane dipeptidase, and expression of a mutant in which potential alternativecleavage/attachment sites were disrupted, indicated that alternative GPI cleavage/attachment sites had not been used. These results indicate that therequirements for GPI anchoring between mammalian and protozoal cells are not as different as previously suggested, and that rules for predicting the probability of a sequence acting as a GPI cleavage/attachment site need to be applied with caution.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 10:31:35