Upregulation of Annexin A1 Expression by Butyrate in Human Colon Adenocarcinoma Cells: Role of p53, NF-Y, and p38 Mitogen-Activated Protein Kinase

Lecona, Emilio; Barrasa, Juan I.; Olmo, Nieves; Llorente, B.; Turnay, Javier; Lizarbe, M.A.

doi:10.1128/mcb.00650-07

Cited by 66 publications

(51 citation statements)

References 49 publications

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“…Whole-cell extracts were prepared by lysing cells in a solution containing 50 mM Tris (pH 7.5), 8 M urea, and 1% 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate (CHAPS). Cytosolic and nuclear extracts were prepared as described previously (29), with the following modifications: nuclei were resuspended in 600 mM KCl, and a short sonication was applied to shear the chromatin. Acid-extracted proteins were obtained by resuspending the cells in phosphate-buffered saline (PBS) containing 0.5% Triton X-100, 2 mM phenylmethylsulfonyl fluoride (PMSF), and 0.02% NaN 3 .…”

Section: Methodsmentioning

confidence: 99%

USP7 Cooperates with SCML2 To Regulate the Activity of PRC1

Lecona

Narendra

Reinberg

2015

Molecular and Cellular Biology

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USP7 is a protein deubiquitinase with an essential role in development. Here, we provide evidence that USP7 regulates the activity of Polycomb repressive complex 1 (PRC1) in coordination with SCML2. There are six versions of PRC1 defined by the association of one of the PCGF homologues (PCGF1 to PCGF6) with the common catalytic subunit RING1B. First, we show that SCML2, a Polycomb group protein that associates with PRC1.2 (containing PCGF2/MEL18) and PRC1.4 (containing PCGF4/ BMI1), modulates the localization of USP7 and bridges USP7 with PRC1.4, allowing for the stabilization of BMI1. Chromatin immunoprecipitation (ChIP) experiments demonstrate that USP7 is found at SCML2 and BMI1 target genes. Second, inhibition of USP7 leads to a reduction in the level of ubiquitinated histone H2A (H2Aub), the catalytic product of PRC1 and key for its repressive activity. USP7 regulates the posttranslational status of RING1B and BMI1, a specific component of PRC1.4. Thus, not only does USP7 stabilize PRC1 components, its catalytic activity is also necessary to maintain a functional PRC1, thereby ensuring appropriate levels of repressive H2Aub.

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Section: Methodsmentioning

confidence: 99%

USP7 Cooperates with SCML2 To Regulate the Activity of PRC1

Lecona

Narendra

Reinberg

2015

Molecular and Cellular Biology

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“…Our data are supported by other studies, which have shown that the promoter of Anxa1, although up-regulated by GCs, does not contain canonical GC responsive elements in its sequence. Moreover, Anxa1 is not considered a primary responsive gene, which suggests that Anxa1 transcription may be promoted via a mediator of GCs (22,23,(46)(47)(48). In inflammatory models, Anxa1-KO leukocytes exhibit an increase in migration and partial or total resistance to the anti-inflammatory effect of GCs (49).…”

Section: Discussionmentioning

confidence: 99%

Role of the glucocorticoid‐induced leucine zipper gene in dexamethasone‐induced inhibition of mouse neutrophil migration via control of annexin A1 expression

et al. 2017

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The glucocorticoid-induced leucine zipper (GILZ) gene is a pivotal mediator of the anti-inflammatory effects of glucocorticoids (GCs) that are known to regulate the function of both adaptive and innate immunity cells. Our aim was to investigate the role of GILZ in GC-induced inhibition of neutrophil migration, as this role has not been investigated before. We found that GILZ expression was induced by dexamethasone (DEX), a synthetic GC, in neutrophils, and that it regulated migration of these cells into inflamed tissues under DEX treatment. Of note, inhibition of neutrophil migration was not observed in GILZ-knockout mice with peritonitis that were treated by DEX. This was because DEX was unable to up-regulate annexin A1 (Anxa1) expression in the absence of GILZ. Furthermore, we showed that GILZ mediates Anxa1 induction by GCs by transactivating Anxa1 expression at the promoter level via binding with the transcription factor, PU.1. The present findings shed light on the role of GILZ in the mechanism of induction of Anxa1 by GCs. As Anxa1 is an important protein for the resolution of inflammatory response, GILZ may represent a new pharmacologic target for treatment of inflammatory

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“…Exceptions to this generalization are annexin A1, a member of the annexin family of calcium-dependent phospholipid-binding proteins, and PRAF2, a novel proapoptotic Bcl-xL/Bcl2-interacting protein (40). The role of annexin A1 in cancer cell function is complex, but several reports have suggested that annexin A1 can function in an antiproliferative capacity (15,17,20). We speculate that increased PRAF2 and/or annexin A1 gene expression resulting from THAP11 knockdown may contribute to the cell proliferation defect observed in these cells.…”

Section: Discussionmentioning

confidence: 99%

A Transcriptional Regulatory Role of the THAP11–HCF-1 Complex in Colon Cancer Cell Function

et al. 2012

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The recently identified Th anatos- a ssociated p rotein (THAP) domain is an atypical zinc finger motif with sequence-specific DNA-binding activity. Emerging data suggest that THAP proteins may function in chromatin-dependent processes, including transcriptional regulation, but the roles of most THAP proteins in normal and aberrant cellular processes remain largely unknown. In this work, we identify THAP11 as a transcriptional regulator differentially expressed in human colon cancer. Immunohistochemical analysis of human colon cancers revealed increased THAP11 expression in both primary tumors and metastases. Knockdown of THAP11 in SW620 colon cancer cells resulted in a significant decrease in cell proliferation, and profiling of gene expression in these cells identified a novel gene set composed of 80 differentially expressed genes, 70% of which were derepressed by THAP11 knockdown. THAP11 was found to associate physically with the transcriptional coregulator HCF-1 (host cell factor 1) and recruit HCF-1 to target promoters. Importantly, THAP11-mediated gene regulation and its chromatin association require HCF-1, while HCF-1 recruitment at these genes requires THAP11. Collectively, these data provide the first characterization of THAP11-dependent gene expression in human colon cancer cells and suggest that the THAP11–HCF-1 complex may be an important transcriptional and cell growth regulator in human colon cancer.

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Upregulation of Annexin A1 Expression by Butyrate in Human Colon Adenocarcinoma Cells: Role of p53, NF-Y, and p38 Mitogen-Activated Protein Kinase

Cited by 66 publications

References 49 publications

USP7 Cooperates with SCML2 To Regulate the Activity of PRC1

USP7 Cooperates with SCML2 To Regulate the Activity of PRC1

Role of the glucocorticoid‐induced leucine zipper gene in dexamethasone‐induced inhibition of mouse neutrophil migration via control of annexin A1 expression

A Transcriptional Regulatory Role of the THAP11–HCF-1 Complex in Colon Cancer Cell Function

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