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Titolo:
Mass spectrometric characterization of proteins extracted from Jurkat T cell detergent-resistant membrane domains
Autore:
von Haller, PD; Donohoe, S; Aebersold, R; Watts, JD; Goodlett, DR;
Indirizzi:
Univ Washington, Dept Mol Biotechnol, Seattle, WA 98195 USA Univ Washington Seattle WA USA 98195 ol Biotechnol, Seattle, WA 98195 USA Inst Syst Biol, Seattle, WA 98105 USA Inst Syst Biol Seattle WA USA 98105Inst Syst Biol, Seattle, WA 98105 USA
Titolo Testata:
EUROPEAN JOURNAL OF MASS SPECTROMETRY
fascicolo: 2, volume: 7, anno: 2001,
pagine: 181 - 193
SICI:
1469-0667(2001)7:2<181:MSCOPE>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
GPI-ANCHORED PROTEINS; LIPID RAFTS; ANTIGEN RECEPTOR; ACTIN CYTOSKELETON; TYROSINE KINASE; PLASMA-MEMBRANE; IMMUNOLOGICAL SYNAPSE; QUANTITATIVE-ANALYSIS; IN-VIVO; ACTIVATION;
Keywords:
lipid rafts; Jurkat T cells; protein identification; tandem mass spectrometry;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
65
Recensione:
Indirizzi per estratti:
Indirizzo: Watts, JD Univ Washington, Dept Mol Biotechnol, Seattle, WA 98195 USA UnivWashington Seattle WA USA 98195 nol, Seattle, WA 98195 USA
Citazione:
P.D. von Haller et al., "Mass spectrometric characterization of proteins extracted from Jurkat T cell detergent-resistant membrane domains", EUR J MASS, 7(2), 2001, pp. 181-193

Abstract

Plasma membranes of most cell types are thought to contain microdomains commonly referred to as lipid rafts, biochemically distinct from bulk plasma membrane and apparently enriched for proteins involved in signal transduction. In T cells, it is believed that lipid rafts aggregate at the site of T cell receptor engagement and act as foci for initiation of the signaling process. In order to gain insight into the possible functioning of lipid rafts, we applied microcapillary liquid chromatography-electrospray ionization-tandem mass spectrometry (mu LC-ESI-MS/MS) methodologies to the identification of proteins which co-purified with lipid rafts. Following isolation of lipid rafts as Triton-insoluble, low-density membrane fractions from JurkatT cells, tryptic digests were generated of electrophoretically-resolved, individual protein bands. Alternatively, avidin-affinity purification was used to isolate cysteine-containing peptides from total tryptic digests of unseparated lipid raft proteins following protein labeling with a cysteine-specific biotinylation reagent. In both cases, protein identifications were made by comparison of tandem mass spectra, generated by mu LC-ESI-MS/MS, with both protein and DNA sequence databases using Sequest software. Proteins identified essentially fell into two groups: cytoskeletal proteins and proteins involved in signal transduction. These findings are discussed in lightof the current understanding of both lipid-raft biology and signal transduction.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/04/20 alle ore 20:21:14