TY - JOUR
T1 - Interferon α induces rapid tyrosine phosphorylation of the vav proto-oncogene product in hematopoietic cells
AU - Platanias, Leonidas C.
AU - Sweet, Michelle E.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1994/2/4
Y1 - 1994/2/4
N2 - The vav proto-oncogene product (p95vav) is specifically expressed in cells of the hematopoietic system, contains one Src homology 2 and two Src homology 3 domains, and is a substrate for receptor and non-receptor tyrosine kinases. Immunoblotting experiments using an anti-phosphotyrosine monoclonal antibody showed that interferon α (IFNα) induces rapid tyrosine phosphorylation of p95vav after binding to its cell surface receptor in the U-266 human myeloma cell line. The IFNα-induced tyrosine phosphorylation of p95vav was time- and dose-dependent, confirming the specificity of the process. IFNα-dependent tyrosine phosphorylation of p95vav was also observed in other hematopoietic cell lines of B-cell origin (Daudi), T-cell origin (MOLT-4), and promyelocytic origin (HL-60). Immunoprecipitation experiments performed with 32P-labeled U-266 cells and phosphoaminoacid analysis of the bands corresponding to p95vav showed that p95vav is phosphorylated on serine residues prior to IFNα stimulation of the cells. After IFNα stimulation significant amounts of phosphorylation of p95vav on tyrosine residues were detectable. Tyrosine phosphorylation of p95vav in U-266 and HL-60 cells was also induced by two other Type I IFNs, IFNβ and IFNω. Altogether these data suggest that the vav proto-oncogene product is a substrate for a Type I IFN-regulated tyrosine kinase(s) and may be involved in the signal transduction pathway of Type I IFNs in hematopoietic cells.
AB - The vav proto-oncogene product (p95vav) is specifically expressed in cells of the hematopoietic system, contains one Src homology 2 and two Src homology 3 domains, and is a substrate for receptor and non-receptor tyrosine kinases. Immunoblotting experiments using an anti-phosphotyrosine monoclonal antibody showed that interferon α (IFNα) induces rapid tyrosine phosphorylation of p95vav after binding to its cell surface receptor in the U-266 human myeloma cell line. The IFNα-induced tyrosine phosphorylation of p95vav was time- and dose-dependent, confirming the specificity of the process. IFNα-dependent tyrosine phosphorylation of p95vav was also observed in other hematopoietic cell lines of B-cell origin (Daudi), T-cell origin (MOLT-4), and promyelocytic origin (HL-60). Immunoprecipitation experiments performed with 32P-labeled U-266 cells and phosphoaminoacid analysis of the bands corresponding to p95vav showed that p95vav is phosphorylated on serine residues prior to IFNα stimulation of the cells. After IFNα stimulation significant amounts of phosphorylation of p95vav on tyrosine residues were detectable. Tyrosine phosphorylation of p95vav in U-266 and HL-60 cells was also induced by two other Type I IFNs, IFNβ and IFNω. Altogether these data suggest that the vav proto-oncogene product is a substrate for a Type I IFN-regulated tyrosine kinase(s) and may be involved in the signal transduction pathway of Type I IFNs in hematopoietic cells.
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M3 - Article
C2 - 7508909
AN - SCOPUS:0028169696
SN - 0021-9258
VL - 269
SP - 3143
EP - 3146
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 5
ER -