Loss of Thioredoxin-Binding Protein-2/Vitamin D3 Up-Regulated Protein 1 in Human T-Cell Leukemia Virus Type I-Dependent T-Cell Transformation

Nishinaka, Yumiko; Nishiyama, Akira; Masutani, Hiroshi; Oka, Shinichi; Ahsan, Kaimul; Nakayama, Yasushi; Ishii, Yasuyuki; Nakamura, Hajime; Maeda, Masako; Yodoi, Junji

doi:10.1158/0008-5472.can-03-0908

Cited by 118 publications

(113 citation statements)

References 35 publications

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“…These antibodies recognized rat TBP-2. 26 Anti-mouse Trx rabbit polyclonal antibody that also recognizes rat Trx was used as described. 28 Mouse monoclonal antibody against cytochrome c (clone A-8) was obtained from Santa Cruz Biotechnology (Santa Cruz, CA, USA).…”

Section: Antibodiesmentioning

confidence: 99%

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Two distinct mechanisms for loss of thioredoxin-binding protein-2 in oxidative stress-induced renal carcinogenesis

Dutta

Nishinaka

Masutani

et al. 2005

Laboratory Investigation

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Thioredoxin is a major component of thiol-reducing system. Recently, we identified thioredoxin-binding protein-2 (TBP-2) as a negative regulator of thioredoxin. Here, we report the role of TBP-2 in oxidative renal tubular injury and the subsequent carcinogenesis by ferric nitrilotriacetate. TBP-2 was abundantly expressed in the rat kidney. Immunohistochemical analysis revealed that TBP-2 was present in association with nuclei and mitochondrial intermembrane space in the proximal tubular cells and coimmunoprecipitated with cytochrome c. After acute oxidative tubular damage, TBP-2 protein, but not messenger RNA, markedly decreased, demonstrating shortened half-life of this protein. Most cases of the induced renal cell carcinoma showed undetectable levels of TBP-2 protein, which was associated with the methylation of CpG island in the promoter region. Genome sequence analyses identified the poly-A tract in the 3 0 untranslated region as a mutation hot spot in this rather nonselective environment. Collectively, the amounts of TBP-2 protein were inversely associated with proliferation of tubular cells, as evaluated by proliferating cell nuclear antigen. These results suggest that loss of TBP-2 is essential for proliferation of not only neoplastic but also non-neoplastic renal tubular cells, and that TBP-2 is a target gene in oxidative stress-induced renal carcinogenesis by ferric nitrilotriacetate.

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Section: Antibodiesmentioning

confidence: 99%

“…25 In a more recent work, we found that loss of TBP-2 plays an important role in human T-cell leukemia virus type I-induced T-cell transformation. 26 In the present study, we examined the significance of TBP-2 in the Fe-NTA-induced renal cancer model of rats. TBP-2 was abundantly present in the rat renal proximal tubular cells.…”

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confidence: 98%

Two distinct mechanisms for loss of thioredoxin-binding protein-2 in oxidative stress-induced renal carcinogenesis

Dutta

Nishinaka

Masutani

et al. 2005

Laboratory Investigation

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“…However, the effect of Txnip overexpression on apoptosis is cell type-specific. For instance, the overexpression of Txnip is not sufficient to induce apoptosis in various human carcinoma cell lines [17,22], whereas the Txnip overexpression in a murine T-cell lymphoma cell line results in apoptosis [21]. We did not detect any relevant indication of apoptosis in the HEp-2 cells overexpressing Txnip (data not shown).…”

Section: Discussionmentioning

confidence: 84%

hnRNP G elicits tumor-suppressive activity in part by upregulating the expression of Txnip

Shin

Kim

et al. 2008

Biochemical and Biophysical Research Communications

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Heterogeneous nuclear ribonuclearproteins (hnRNPs) are nucleic acid-binding proteins and have critical roles in DNA repair, telomere regulation, and transcriptional gene regulation. Previously, we showed that hnRNP G has tumor-suppressive activity in human oral squamous cell carcinoma cells. Therefore, the identification of hnRNP G target genes is important for understanding the function of hnRNP G and its tumor suppressive activity. In this study, we identify a known tumor suppressor gene, thioredoxin-interacting protein (Txnip) gene as a novel target of hnRNP G. Expression of Txnip is upregulated by wild-type (wt) hnRNP G but not by a suppression-defective mutant hnRNP G (K22R) in human squamous cell carcinoma. Wt hnRNP G binds and transactivates the Txnip promoter in vivo, whereas the K22R mutant does not. Furthermore, overexpression of Txnip alone in cancer cells leads to the inhibition of anchorage-independent growth and in vivo tumorigenicity in immunocompromised mice, suggesting a reversion of the transformation phenotype. These studies indicate that hnRNP G promotes the expression of Txnip and mediates its tumor suppressive effect.

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“…The expression of TBP2 is lost in HTLV-I-positive, interleukin-2-independent T cell lines but maintained in HTLV-I-positive, interleukin-2-dependent T cell lines, as well as HTLVI-negative T cell lines (25,26). Ectopic overexpression of TBP2 in HTLV-I-positive T cells resulted in growth suppression.…”

Section: Trx Binding Proteinmentioning

confidence: 99%

Thioredoxin and thioredoxin binding protein 2 in the liver

et al. 2008

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SummaryThioredoxin (TRX) is a 12-kDa protein with redox-active dithiol in the active site -Cys-Gly-Pro-Cys-and constitutes a major thiol reducing system. TRX protects cells from stressinduced damage through antioxidative, antiapoptotic, and antiinflammatory effect. In animal models, thioacetamide (TAA)-induced acute hepatitis and TAA-induced liver fibrosis was attenuated in TRX transgenic (TRXTG) mice. Plasma level of TRX is a good marker for hepatitis and nonalcoholic steatohepatitis (NASH) in human patients. Recently, we identified TRX binding protein 2 (TBP2) in a yeast two-hybrid screening. TBP2 regulates both the expression and reducing activity of TRX as well as cell growth. TBP2 knockout (TBP2KO) mice showed disorder in lipid metabolism. TBP2 plays a multiple role on cell growth and lipid and glucose metabolism. Thus, TRX and TBP2 play important roles in the pathophysiology of liver diseases, including NASH, indicating that ratio of TRX and TBP2 expression could be a novel marker of liver diseases like NASH.2008 IUBMB IUBMB Life, 60(10): 656-660, 2008

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Loss of Thioredoxin-Binding Protein-2/Vitamin D3 Up-Regulated Protein 1 in Human T-Cell Leukemia Virus Type I-Dependent T-Cell Transformation

Abstract: ABSTRACT

Cited by 118 publications

References 35 publications

Two distinct mechanisms for loss of thioredoxin-binding protein-2 in oxidative stress-induced renal carcinogenesis

Two distinct mechanisms for loss of thioredoxin-binding protein-2 in oxidative stress-induced renal carcinogenesis

hnRNP G elicits tumor-suppressive activity in part by upregulating the expression of Txnip

Thioredoxin and thioredoxin binding protein 2 in the liver

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