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Titolo:
Requirement of tyrosine-phosphorylated Vav for morphological differentiation of all-trans-retinoic acid-treated HL-60 cells
Autore:
Bertagnolo, V; Marchisio, M; Brugnoli, F; Bavelloni, A; Boccafogli, L; Colamussi, ML; Capitani, S;
Indirizzi:
Univ Ferrara, Dept Morphol & Embryol, Signal Transduct Unit, Lab Cell Biol,Sect Human Anat, I-44100 Ferrara, Italy Univ Ferrara Ferrara Italy I-44100 ct Human Anat, I-44100 Ferrara, Italy Ist Ortoped Rizzoli, Lab Cell Biol & Electron Microscopy, I-40100 Bologna,Italy Ist Ortoped Rizzoli Bologna Italy I-40100 roscopy, I-40100 Bologna,Italy
Titolo Testata:
CELL GROWTH & DIFFERENTIATION
fascicolo: 4, volume: 12, anno: 2001,
pagine: 193 - 200
SICI:
1044-9523(200104)12:4<193:ROTVFM>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
GRANULOCYTIC DIFFERENTIATION; PHOSPHOINOSITIDE 3-KINASE; T-CELLS; PHOSPHATIDYLINOSITOL 3-KINASE; PROTOONCOGENE PRODUCT; SIGNAL-TRANSDUCTION; ANTIGEN RECEPTORS; LEUKEMIA-CELLS; UP-REGULATION; B-CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Capitani, S Univ Ferrara, Dept Morphol & Embryol, Signal Transduct Unit, Lab Cell Biol,Sect Human Anat, Via Fossato Mortara 66, I-44100 Ferrara, Italy Univ Ferrara Via Fossato Mortara 66 Ferrara Italy I-44100 aly
Citazione:
V. Bertagnolo et al., "Requirement of tyrosine-phosphorylated Vav for morphological differentiation of all-trans-retinoic acid-treated HL-60 cells", CELL GROWTH, 12(4), 2001, pp. 193-200

Abstract

Our previous data demonstrated that cellular and nuclear tyrosine-phosphorylated Vav associate with phosphoinositide 3-kinase during all-trans-retinoic acid-dependent granulocytic differentiation of HL-60 cells. In this study, aimed to analyze the mechanism by which Vav is recruited and activated, we report that the Src homology 2 domain of Vav interacts with tyrosine-phosphorylated proteins in a differentiation-dependent manner. Two adaptor proteins, Cbl and SLP-76, were identified, showing a discrete distribution inside the cells, with Cbl absent from the nuclei and SLP-76 particularly abundant in the nuclear compartment, Of note, Vav interacts with the tyrosine kinase Syk, which is also present in the nuclear compartment and may phosphorylate Vav in vitro when cells differentiate. Inhibition of Syk activity bypiceatannol prevents both in vitro and in vivo Vav tyrosine phosphorylation, its association with the regulatory subunit of phosphoinositide 9-kinase, and the nuclear modifications typically observed during granulocytic differentiation of this cell line. These findings suggest that tyrosine-phosphorylated Vav and its association with phosphoinositide 3-kinase play a crucial role in all-trans-retinoic acid-induced reorganization of the nucleoskeleton, which is responsible for the changes in nuclear morphology observed during granulocytic differentiation of HL-60 cells.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 07:08:57