The protein tyrosine kinase Fyn activates transcription from the HIV promoter via activation of NFkB-like DNA-binding proteins

Naohiro Hohashi, Takuma Hayashi, Noemi Fusaki, Masakazu Takeuchi, Makoto Higurashi, Takashi Okamoto, Kentaro Senba, Tadashi Yamamoto

研究成果: Article

14 引用 (Scopus)

抄録

Protein tyrosine kinase p59fyn (Fyn) associates with the TCR-CD3 complex, which suggests that Fyn plays a significant role in the signal transduction involving TCR complex. In addition to cellular genes, viral promoters such as the HIV long terminal repeat (LTR) are also activated upon T cell activation. To elucidate the functional significance of Fyn in the expression of viral promoters, we transfected a Fyn-expression vector together with a reporter plasmid containing the chloramphenicol acetyltransferase gene driven by HIV LTR into a human T cell line, Jurkat. In this assay, Fyn stimulated the promoter in HIV LTR when the transfected cells were treated with both concanavalin A and PMA as an antigen-mimic stimulation. This activation required the intact SH2 domain of Fyn. Mutational analysis of HIV LTR showed that the NFKB binding sites were responsible for this effect. Electrophoretic mobility shift assays and UV cross-linking experiments showed that activation of T cells by anti-CD3 antibody induced four KB-binding proteins (50, 60, 65 and 100 kDa) in Fyn-overexpressing cells more efficiently than in the parental cells. Our results suggested that Fyn was able to regulate expression of a subset of genes via KB-binding proteins upon T cell activation.

元の言語English
ページ(範囲)1851-1859
ページ数9
ジャーナルInternational Immunology
7
発行部数11
DOI
出版物ステータスPublished - 1995 11
外部発表Yes

Fingerprint

HIV Long Terminal Repeat
DNA-binding Protein
Protein Kinase
T-cells
DNA-Binding Proteins
Transcription
Promoter
T Cell Activation
Protein-Tyrosine Kinases
Activation
DNA
Chemical activation
HIV
Gene
Proteins
T-Lymphocytes
Genes
Cell
Protein
Assays

ASJC Scopus subject areas

  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Public Health, Environmental and Occupational Health
  • Neuropsychology and Physiological Psychology
  • Transplantation
  • Immunology

これを引用

Hohashi, N., Hayashi, T., Fusaki, N., Takeuchi, M., Higurashi, M., Okamoto, T., ... Yamamoto, T. (1995). The protein tyrosine kinase Fyn activates transcription from the HIV promoter via activation of NFkB-like DNA-binding proteins. International Immunology, 7(11), 1851-1859. https://doi.org/10.1093/intimm/7.11.1851

The protein tyrosine kinase Fyn activates transcription from the HIV promoter via activation of NFkB-like DNA-binding proteins. / Hohashi, Naohiro; Hayashi, Takuma; Fusaki, Noemi; Takeuchi, Masakazu; Higurashi, Makoto; Okamoto, Takashi; Senba, Kentaro; Yamamoto, Tadashi.

:: International Immunology, 巻 7, 番号 11, 11.1995, p. 1851-1859.

研究成果: Article

Hohashi, Naohiro ; Hayashi, Takuma ; Fusaki, Noemi ; Takeuchi, Masakazu ; Higurashi, Makoto ; Okamoto, Takashi ; Senba, Kentaro ; Yamamoto, Tadashi. / The protein tyrosine kinase Fyn activates transcription from the HIV promoter via activation of NFkB-like DNA-binding proteins. :: International Immunology. 1995 ; 巻 7, 番号 11. pp. 1851-1859.
@article{2cbc0762accf496d932b4f93fec1724a,
title = "The protein tyrosine kinase Fyn activates transcription from the HIV promoter via activation of NFkB-like DNA-binding proteins",
abstract = "Protein tyrosine kinase p59fyn (Fyn) associates with the TCR-CD3 complex, which suggests that Fyn plays a significant role in the signal transduction involving TCR complex. In addition to cellular genes, viral promoters such as the HIV long terminal repeat (LTR) are also activated upon T cell activation. To elucidate the functional significance of Fyn in the expression of viral promoters, we transfected a Fyn-expression vector together with a reporter plasmid containing the chloramphenicol acetyltransferase gene driven by HIV LTR into a human T cell line, Jurkat. In this assay, Fyn stimulated the promoter in HIV LTR when the transfected cells were treated with both concanavalin A and PMA as an antigen-mimic stimulation. This activation required the intact SH2 domain of Fyn. Mutational analysis of HIV LTR showed that the NFKB binding sites were responsible for this effect. Electrophoretic mobility shift assays and UV cross-linking experiments showed that activation of T cells by anti-CD3 antibody induced four KB-binding proteins (50, 60, 65 and 100 kDa) in Fyn-overexpressing cells more efficiently than in the parental cells. Our results suggested that Fyn was able to regulate expression of a subset of genes via KB-binding proteins upon T cell activation.",
keywords = "Signal transduction, Src family, Transcription factor",
author = "Naohiro Hohashi and Takuma Hayashi and Noemi Fusaki and Masakazu Takeuchi and Makoto Higurashi and Takashi Okamoto and Kentaro Senba and Tadashi Yamamoto",
year = "1995",
month = "11",
doi = "10.1093/intimm/7.11.1851",
language = "English",
volume = "7",
pages = "1851--1859",
journal = "International Immunology",
issn = "0953-8178",
publisher = "Oxford University Press",
number = "11",

}

TY - JOUR

T1 - The protein tyrosine kinase Fyn activates transcription from the HIV promoter via activation of NFkB-like DNA-binding proteins

AU - Hohashi, Naohiro

AU - Hayashi, Takuma

AU - Fusaki, Noemi

AU - Takeuchi, Masakazu

AU - Higurashi, Makoto

AU - Okamoto, Takashi

AU - Senba, Kentaro

AU - Yamamoto, Tadashi

PY - 1995/11

Y1 - 1995/11

N2 - Protein tyrosine kinase p59fyn (Fyn) associates with the TCR-CD3 complex, which suggests that Fyn plays a significant role in the signal transduction involving TCR complex. In addition to cellular genes, viral promoters such as the HIV long terminal repeat (LTR) are also activated upon T cell activation. To elucidate the functional significance of Fyn in the expression of viral promoters, we transfected a Fyn-expression vector together with a reporter plasmid containing the chloramphenicol acetyltransferase gene driven by HIV LTR into a human T cell line, Jurkat. In this assay, Fyn stimulated the promoter in HIV LTR when the transfected cells were treated with both concanavalin A and PMA as an antigen-mimic stimulation. This activation required the intact SH2 domain of Fyn. Mutational analysis of HIV LTR showed that the NFKB binding sites were responsible for this effect. Electrophoretic mobility shift assays and UV cross-linking experiments showed that activation of T cells by anti-CD3 antibody induced four KB-binding proteins (50, 60, 65 and 100 kDa) in Fyn-overexpressing cells more efficiently than in the parental cells. Our results suggested that Fyn was able to regulate expression of a subset of genes via KB-binding proteins upon T cell activation.

AB - Protein tyrosine kinase p59fyn (Fyn) associates with the TCR-CD3 complex, which suggests that Fyn plays a significant role in the signal transduction involving TCR complex. In addition to cellular genes, viral promoters such as the HIV long terminal repeat (LTR) are also activated upon T cell activation. To elucidate the functional significance of Fyn in the expression of viral promoters, we transfected a Fyn-expression vector together with a reporter plasmid containing the chloramphenicol acetyltransferase gene driven by HIV LTR into a human T cell line, Jurkat. In this assay, Fyn stimulated the promoter in HIV LTR when the transfected cells were treated with both concanavalin A and PMA as an antigen-mimic stimulation. This activation required the intact SH2 domain of Fyn. Mutational analysis of HIV LTR showed that the NFKB binding sites were responsible for this effect. Electrophoretic mobility shift assays and UV cross-linking experiments showed that activation of T cells by anti-CD3 antibody induced four KB-binding proteins (50, 60, 65 and 100 kDa) in Fyn-overexpressing cells more efficiently than in the parental cells. Our results suggested that Fyn was able to regulate expression of a subset of genes via KB-binding proteins upon T cell activation.

KW - Signal transduction

KW - Src family

KW - Transcription factor

UR - http://www.scopus.com/inward/record.url?scp=0028804092&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028804092&partnerID=8YFLogxK

U2 - 10.1093/intimm/7.11.1851

DO - 10.1093/intimm/7.11.1851

M3 - Article

C2 - 8580083

AN - SCOPUS:0028804092

VL - 7

SP - 1851

EP - 1859

JO - International Immunology

JF - International Immunology

SN - 0953-8178

IS - 11

ER -