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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; Goodlett, DR; Aebersold, R; Watts, JD;
Indirizzi:
Inst Syst Biol, Seattle, WA 98105 USA Inst Syst Biol Seattle WA USA 98105Inst Syst Biol, Seattle, WA 98105 USA Univ Washington, Dept Mol Biotechnol, Seattle, WA USA Univ Washington Seattle WA USA ton, Dept Mol Biotechnol, Seattle, WA USA
Titolo Testata:
PROTEOMICS
fascicolo: 8, volume: 1, anno: 2001,
pagine: 1010 - 1021
SICI:
1615-9853(200108)1:8<1010:MSCOPE>2.0.ZU;2-O
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:
Life Sciences
Citazioni:
65
Recensione:
Indirizzi per estratti:
Indirizzo: Watts, JD Inst Syst Biol, 4225 Roosevelt Way,Suite 200, Seattle, WA 98105 USA Inst Syst Biol 4225 Roosevelt Way,Suite 200 Seattle WA USA 98105
Citazione:
P.D. von Haller et al., "Mass spectrometric characterization of proteins extracted from Jurkat T cell detergent-resistant membrane domains", PROTEOMICS, 1(8), 2001, pp. 1010-1021

Abstract

Plasma membranes of most cell types are thought to contain microdomains commonly referred to as lipid rafts, biochemically distinct from bulk plasma membrane, 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 copurified with lipid rafts. Following isolation of lipid rafts as Triton-insoluble, low-density membrane fractions from Jurkat T cells, tryptic digests were generated of individual protein bands resolved electrophoretically. Alternatively, cysteine-containing peptides were isolated from total tryptic digests of unseparated lipid raft proteins followinglabeling with a oysteine-specific biotinylation reagent and avidin affinity purification. In both, cases, protein identifications were made by comparison of tandem MS spectra generated by mu LC-ESI-MS/MS to 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 the light of 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 31/03/20 alle ore 22:24:22