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Titolo:
RAPID ACTIVATION OF C-RAF-1 AFTER STIMULATION OF THE T-CELL RECEPTOR OR THE MUSCARINIC RECEPTOR TYPE-1 IN RESTING T-CELLS
Autore:
SIEGEL JN; JUNE CH; YAMADA H; RAPP UR; SAMELSON LE;
Indirizzi:
USN,INST MED RES,IMMUNE CELL BIOL PROGRAM,MAIL STOP 6 BETHESDA MD 20889 NCI,FREDERICK CANC RES & DEV CTR,VIRAL CARCINOGENESIS LAB FREDERICK MD 21702 NICHHD,CELL BIOL & METAB BRANCH BETHESDA MD 20892
Titolo Testata:
The Journal of immunology
fascicolo: 8, volume: 151, anno: 1993,
pagine: 4116 - 4127
SICI:
0022-1767(1993)151:8<4116:RAOCAS>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE KINASE; ANTIGEN RECEPTOR; SIGNAL TRANSDUCTION; MAP KINASE; RAF-1 KINASE; ZETA-CHAIN; MONOCLONAL-ANTIBODY; PHOSPHATASE CD45; PHOSPHORYLATION; INTERLEUKIN-2;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
64
Recensione:
Indirizzi per estratti:
Citazione:
J.N. Siegel et al., "RAPID ACTIVATION OF C-RAF-1 AFTER STIMULATION OF THE T-CELL RECEPTOR OR THE MUSCARINIC RECEPTOR TYPE-1 IN RESTING T-CELLS", The Journal of immunology, 151(8), 1993, pp. 4116-4127

Abstract

The c-Raf-1 serine/threonine kinase is an important component of signal transduction pathways mediating the effects of a variety of growth factors. In activated T cells, IL-2 has been shown to induce activation of c-Raf-1, but c-Raf-1 has not previously been shown to be activated through the T-cell receptor (TCR) in resting G0 T cells. Using a sensitive immune complex kinase reaction, we show that cross-linking of the stimulatory and costimulatory receptors CD3, CD4, or CD28 induces c-Raf-1 activation in highly purified resting peripheral blood human T cells. In contrast, cross-linking the nonstimulatory receptor CD45 didnot induce c-Raf-1. Surprisingly, although earlier studies had shown delayed kinetics in response to Thy-1 stimulation in murine cells, c-Raf-1 activation in response to CD3 cross-linking was one of the earliest measurable events. In spite of its early kinetics, c-Raf-1 activation was found to be downstream of several other early signal transduction events, including activation of a tyrosine kinase and a tyrosine phosphatase. Several lines of evidence suggest that activation of c-Raf-1 in response to TCR stimulation may be PKC-dependent: first, phorbol esters are extremely potent activators of c-Raf-1 in human T cells; second, the kinetics of accumulation of products of phosphatidylinositolhydrolysis coincides with the kinetics of c-Raf-1 activation; and third, physiologic activation of the PLC/PKC pathway through a transfected, G-protein-coupled receptor HM1 induced similar levels of c-Raf-1 activation with a similar time course. We conclude that c-Raf-1 activation is tightly coupled to TCR stimulation and may participate in signaltransduction pathways in resting, G0 T cells. The observation that the HM1 receptor can also activate c-Raf-1 suggests that T cells have the capability to utilize both tyrosine kinase-dependent and tyrosine kinase-independent mechanisms of c-Raf-1 activation.

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Documento generato il 27/11/20 alle ore 05:58:32