This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Mori, N. Articles by Prager, D. Search for Related Content PubMed PubMed Citation Articles by Mori, N. Articles by Prager, D.

High Levels of AP-2-binding Activity in Cell Lines Infected with Human T-Cell Leukemia Virus Type I: Possible Enhancement of AP-2 Binding by Human T-Cell Leukemia Virus Type 1 tax¹

Department of Medicine, Division of Endocrinology and Metabolism, Cedars-Sinai Medical Center, University of California-Los Angeles School of Medicine, Los Angeles, California 90048

Human T-cell leukemia virus type I (HTLV-I) is the etiological agent for adult T-cell leukemia and tropical spastic paraparesis/HTLV-I-associated myelopathy. Recently, the transcription factor AP-2 has been demonstrated to be capable of activating gene expression from HTLV-I long terminal repeat. To determine whether changes occur in the levels of AP-2-binding activity in HTLV-I-infected cell lines, we compared the levels of AP-2 binding of nuclear extracts obtained from HTLV-I-infected T-cell lines with those of nuclear extracts obtained from uninfected T-cell lines. High levels of AP-2-binding activity were observed in HTLV-I-infected cell lines (MT-2, HUT-102, and SLB-1) using the mobility shift assay. In contrast, in the uninfected cell lines (Jurkat, HUT-78, and MLA 144), AP-2-binding activity was obviously low compared with that in the HTLV-I-infected cell lines. HTLV-I transactivator protein tax activates expression of both viral and cellular genes. We have demonstrated further that introduction of the tax gene into Jurkat cells stimulated AP-2-binding activity. These results indicate that HTLV-I-infected T cells exhibit constitutive AP-2-binding activity, and that tax may increase the DNA binding activity of AP-2.

¹ This work was supported by NIH Grant R01 DK46484. N. M. was supported by a Cedars-Sinai Research Institute Fellowship.

² To whom requests for reprints should be addressed, at Department of Medicine, Division of Endocrinology and Metabolism, Cedars-Sinai Medical Center, UCLA School of Medicine, Davis Building 3008, 8700 Beverly Boulevard, Los Angeles, CA 90048. Phone: (310) 855-7665; Fax: (310) 652-7987.

Received 10/17/95. Accepted 12/11/95.

This article has been cited by other articles:

				M. L. Yeung, J.-i. Yasunaga, Y. Bennasser, N. Dusetti, D. Harris, N. Ahmad, M. Matsuoka, and K.-T. Jeang Roles for MicroRNAs, miR-93 and miR-130b, and Tumor Protein 53-Induced Nuclear Protein 1 Tumor Suppressor in Cell Growth Dysregulation by Human T-Cell Lymphotrophic Virus 1 Cancer Res., November 1, 2008; 68(21): 8976 - 8985. [Abstract] [Full Text] [PDF]

				Q. Li and R. H. Dashwood Activator Protein 2{alpha} Associates with Adenomatous Polyposis Coli/{beta}-Catenin and Inhibits {beta}-Catenin/T-cell Factor Transcriptional Activity in Colorectal Cancer Cells J. Biol. Chem., October 29, 2004; 279(44): 45669 - 45675. [Abstract] [Full Text] [PDF]

				O. Nyormoi, Z. Wang, D. Doan, M. Ruiz, D. McConkey, and M. Bar-Eli Transcription Factor AP-2{alpha} Is Preferentially Cleaved by Caspase 6 and Degraded by Proteasome during Tumor Necrosis Factor Alpha-Induced Apoptosis in Breast Cancer Cells Mol. Cell. Biol., August 1, 2001; 21(15): 4856 - 4867. [Abstract] [Full Text] [PDF]