Apg‐2 has a chaperone‐like activity similar to Hsp110 and is overexpressed in hepatocellular carcinomas

Gotoh, K.; Nonoguchi, Kohsuke; Higashitsuji, Hiroaki; Kaneko, Yoshiyuki; Sakurai, Toshiharu; Sumitomo, Yasuhiko; Itoh, Katsuhiko; Subjeck, John R.; Fujita, Jun

doi:10.1016/s0014-5793(04)00034-1

Cited by 45 publications

(35 citation statements)

References 34 publications

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“…Moreover, overexpression of Apg-2 conferred a proliferative advantage to BaF3-BCR/ABL cells in vitro. In accord with our findings, a previous study has demonstrated that Apg-2 is overexpressed in hepatocellular carcinoma (16). Together, these findings suggested that Apg-2 is overexpressed when exposed to H 2 O 2 in BaF3-BCR/ABL cells, which promotes cell proliferation.…”

Section: Baf3-bcr/abl Cells With Apg-2 Overexpression Had Higher Propsupporting

confidence: 92%

“…Interestingly, Apg-2 protein shows a chaperone-like activity similar to Hsp110 and is overexpressed in hepatocellular carcinomas (16) as well as in pancreatic cancer (17), indicating that Apg-2 may be critical to tumor progression. In our previous comparative proteomics study, we found that Apg-2 was overexpressed in BaF3-BCR/ABL cells that were treated with hydrogen peroxide (H 2 O 2 ) comparing to BaF3-MIGR1 cells (unpublished data).…”

Section: Introductionmentioning

confidence: 99%

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Overexpression of Apg-2 increases cell proliferation and protects from oxidative damage in BaF3-BCR/ABL cells

Liu²,

Yuan³

et al. 2010

Int J Oncol

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Abstract. Apg-2, a mammalian heat-shock protein belonging to the heat-shock protein 110 (Hsp110) family, was previously found to be overexpressed in BaF3-BCR/ABL cells that were treated with hydrogen peroxide (H 2 O 2 ) through our comparative proteomics study. The expression of Apg-2 in chronic myelogenous leukemia (CML) cells and its role have not been investigated, forming the basis for this study. BaF3-MIGR1 and BaF3-BCR/ABL cell lines stably overexpressing Apg-2 were established and exposed to 50 μM H 2 O 2 for 10 min. Western blot analysis of Apg-2 expression confirmed that H 2 O 2 treatment significantly up-regulated Apg-2 expression. Apg-2 overexpression elevated BaF3-BCR/ABL cell proportions in S and G 2 /M phase, increased cell proliferation and colony formation in vitro. Moreover, BaF3-MIGR1 and BaF3-BCR/ABL cells were exposed to 50 μM H 2 O 2 in the absence or presence of Apg-2 overexpression and induction of H 2 AX phosphorylation, the reporters of DNA damage were assessed by Western blot and immunofluorescence. Results showed that exposure to H 2 O 2 induced H 2 AX phosphorylation in BaF3-MIGR1 cells, but no increase was observed in BaF3-BCR/ABL cells. Together, the data indicate that Apg-2 is overexpressed and overexpression of Apg-2 in BaF3-BCR/ABL cells increases cell proliferation and protects cells from oxidative damage, which may play an important role in CML carcinogenesis and progression.

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Section: Baf3-bcr/abl Cells With Apg-2 Overexpression Had Higher Propsupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Overexpression of Apg-2 increases cell proliferation and protects from oxidative damage in BaF3-BCR/ABL cells

Liu²,

Yuan³

et al. 2010

Int J Oncol

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“…By constructing subtracted cDNA libraries, we have previously identified 19 genes overexpressed in HCCs, including two novel genes (18,19). One of these genes was named HSCO (hepatoma subtracted-cDNA library clone one) (20).…”

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confidence: 99%

Enhanced Deacetylation of p53 by the Anti-apoptotic Protein HSCO in Association with Histone Deacetylase 1

Higashitsuji

Masuda

Liu

et al. 2007

Journal of Biological Chemistry

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HSCO (hepatoma subtracted-cDNA library clone one, also called ETHE1) was originally identified by its frequent overexpression in hepatocellular carcinomas. HSCO inhibits function of NF-B by binding to RelA and accelerating its export from the nucleus. We show here that HSCO exhibits anti-apoptotic activity in cells exposed to DNA-damaging agents by suppressing transcriptional activity of p53. Induction of pro-apoptotic genes, Noxa, Perp, PIG3, and Bax were suppressed in cells overexpressing HSCO. By increasing ubiquitylation and degradation of p53, HSCO reduces p53 protein levels. HSCO specifically associates with histone deacetylase 1 (HDAC1) independently of Mdm2 and facilitates deacetylation of p53 at Lys-373/382 by HDAC1. The metallo-␤-lactamase family consensus sequence in HSCO is important for its effect on p53 deacetylation. Coimmunoprecipitation and immunofluorescence studies suggested that HSCO, HDAC1, and p53 form a complex in the nucleus. Thus, HSCO is a cofactor that increases the deacetylase activity of HDAC1 toward p53, leading to suppression of apoptosis. Treatment of hepatocellular carcinomas that retain wildtype p53 and overexpress HSCO with anti-HSCO agents might re-establish the p53 response and revert chemoresistance.

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“…Similarly, several junctional scaffolding proteins are bound and inactivated by viral oncogenes (Glaunsinger et al, 2001;Latorre et al, 2005). By contrast, ZONAB and its activating protein Apg2 are both upregulated in hepatocellular carcinomas, which suggests that this proliferationpromoting pathway is stimulated (Arakawa et al, 2004;Gotoh et al, 2004;Hayashi et al, 2002).…”

Section: Tjs In Diseasementioning

confidence: 99%

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Apg‐2 has a chaperone‐like activity similar to Hsp110 and is overexpressed in hepatocellular carcinomas

Cited by 45 publications

References 34 publications

Overexpression of Apg-2 increases cell proliferation and protects from oxidative damage in BaF3-BCR/ABL cells

Overexpression of Apg-2 increases cell proliferation and protects from oxidative damage in BaF3-BCR/ABL cells

Enhanced Deacetylation of p53 by the Anti-apoptotic Protein HSCO in Association with Histone Deacetylase 1

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