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Activation of HTLV-I gene transcription by protein tyrosine phosphatase inhibitors
- Source :
- Virology, Virology, Elsevier, 2004, 329 (2), pp.395-411. ⟨10.1016/j.virol.2004.09.003⟩
- Publication Year :
- 2004
- Publisher :
- Elsevier BV, 2004.
-
Abstract
- Human T-cell leukemia virus type I (HTLV-I) transcription generally depends on the ability of the viral Tax protein to bind the CREB transcription factor and form an active complex by recruiting CBP/p300 coactivators to the long terminal repeat (LTR). Studies have demonstrated that T-cell activating agents that stimulate CREB are potent inducers of HTLV-I transcription. Herein, we demonstrate that bpV[pic], a protein tyrosine phosphatase (PTP) inhibitor activates the HTLV-I LTR in the presence and absence of Tax expression. Optimal activation occurred at 8 h and was synergistic with forskolin or PGE(2). Infected cell lines and cells transfected with HTLV-I proviral DNA were equally responsive to the synergistic effect of bpV and forskolin on HTLV-I gene expression. Activation of the LTR by bpV[pic] was T-cell receptor-independent, but required ZAP70, calcineurin activity and functional calcium entry. Inhibition of the SHP-1 PTP was suggested to be important. Transfection experiments with a CREB dominant-negative mutant and with isolated TRE1- or CREB-responsive reporter constructs and treatment with the MDL-12,330A adenylate cyclase inhibitor all supported the involvement of a CREB/ATF family member in this bpV-dependent activation of the HTLV-I LTR, although CREB itself did not seem to be involved. Analysis of HTLV-I reporter constructs containing mutated CREB-binding sites also implied the involvement of another element in this activation. These results demonstrate for the first time a powerful effect of PTP inhibitors on HTLV-I LTR activity and suggest participation of both CREB-dependent and -independent pathways in this activation.
- Subjects :
- Transcription, Genetic
viruses
MESH: SHP1 Protein Tyrosine Phosphatase
Protein tyrosine phosphatase
MESH: Drug Synergism
MESH: Virus Activation
MESH: Gene Expression Regulation, Viral
chemistry.chemical_compound
Transcription (biology)
MESH: Gene Products, tax
Enzyme Inhibitors
Cyclic AMP Response Element-Binding Protein
Regulation of gene expression
Human T-lymphotropic virus 1
MESH: Protein-Tyrosine-Phosphatase
ZAP-70 Protein-Tyrosine Kinase
Forskolin
biology
Protein Tyrosine Phosphatase, Non-Receptor Type 6
MESH: Dinoprostone
Intracellular Signaling Peptides and Proteins
Drug Synergism
Gene Products, tax
Transfection
Protein-Tyrosine Kinases
Long terminal repeat
MESH: Terminal Repeat Sequences
MESH: Enzyme Inhibitors
[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology
MESH: Forskolin
MESH: Cyclic AMP Response Element-Binding Protein
Gene Expression Regulation, Viral
[SDV.CAN]Life Sciences [q-bio]/Cancer
CREB
MESH: Protein-Tyrosine Kinases
Dinoprostone
Cell Line
MESH: Intracellular Signaling Peptides and Proteins
Virology
Organometallic Compounds
Humans
Transcription factor
MESH: Human T-lymphotropic virus 1
MESH: Humans
MESH: Transcription, Genetic
Colforsin
Terminal Repeat Sequences
MESH: Organometallic Compounds
MESH: ZAP-70 Protein-Tyrosine Kinase
Molecular biology
MESH: Cell Line
MESH: Vanadates
chemistry
biology.protein
Virus Activation
Protein Tyrosine Phosphatases
Vanadates
Subjects
Details
- ISSN :
- 00426822 and 10960341
- Volume :
- 329
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Virology
- Accession number :
- edsair.doi.dedup.....d472996c908b8200ba6fd0a9f2da8f4e
- Full Text :
- https://doi.org/10.1016/j.virol.2004.09.003