Stimulation of tissue-type plasminogen activator gene expression by sodium butyrate and trichostatin A in human endothelial cells involves histone acetylation

Arts, Janine; Lansink, Mirian; Grimbergen, Jos; Toet, Karin; Kooistra, Teake

doi:10.1042/bj3100171

Cited by 96 publications

(67 citation statements)

References 31 publications

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“…Histone acetylation influences the higher order structure of chromatin, resulting in a chromatin conformation that is more accessible to transcription factors and leading to enhanced transcription of some genes (17). As part of our effort to optimize conditions for evaluating VR1 pharmacology, we have found that butyrate can influence the function of VR1.…”

Section: Resultsmentioning

confidence: 98%

Interaction between Protein Kinase Cμ and the Vanilloid Receptor Type 1

Wang

Kedei

Wei

et al. 2004

Journal of Biological Chemistry

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The capsaicin receptor VR1 is a polymodal nociceptor activated by multiple stimuli. It has been reported that protein kinase C plays a role in the sensitization of VR1. Protein kinase D/PKC is a member of the protein kinase D serine/threonine kinase family that exhibits structural, enzymological, and regulatory features distinct from those of the PKCs, with which they are related. As part of our effort to optimize conditions for evaluating VR1 pharmacology, we found that treatment of Chinese hamster ovary (CHO) cells heterologously expressing rat VR1 (CHO/rVR1) with butyrate enhanced rVR1 expression and activity. The expression of PKC and PKC␤1, but not of other PKC isoforms, was also enhanced by butyrate treatment, suggesting the possibility that these two isoforms might contribute to the enhanced activity of rVR1. In support of this hypothesis, we found the following. 1) Overexpression of PKC enhanced the response of rVR1 to capsaicin and low pH, and expression of a dominant negative variant of PKC reduced the response of rVR1. 2) Reduction of endogenous PKC using antisense oligonucleotides decreased the response of exogenous rVR1 expressed in CHO cells as well as of endogenous rVR1 in dorsal root ganglion neurons. 3) PKC localized to the plasma membrane when overexpressed in CHO/rVR1 cells. 4) PKC directly bound to rVR1 expressed in CHO cells as well as to endogenous rVR1 in dorsal root ganglia or to an N-terminal fragment of rVR1, indicating a direct interaction between PKC and rVR1. 5) PKC directly phosphorylated rVR1 or a longer N-terminal fragment (amino acids 1-118) of rVR1 but not a shorter one (amino acids 1-99). 6) Mutation of S116A in rVR1 blocked both the phosphorylation of rVR1 by PKC and the enhancement by PKC of the rVR1 response to capsaicin. We conclude that PKC functions as a direct modulator of rVR1.The vanilloid receptor type 1 (VR1 or TRPV1)1 is a vanilloidgated, nonselective cation channel that belongs to the transient receptor potential (TRP) channel superfamily. VR1 is expressed on small diameter neurons within sensory ganglia and accounts for the highly selective action of vanilloids as excitatory agents for nociceptors. In addition to vanilloids, heat and protons also influence vanilloid receptors and nociceptive pathways, and VR1 thus can be viewed as a molecular integrator of chemical and physical stimuli that elicit pain (1). Following tissue injury, the magnitude of VR1 responses is modulated by the combined effects of protons, temperature, endogenous ligands, and signaling pathways, and this modulation of VR1 activity contributes to the sensitization of nociceptors associated with the development of allodynia and hyperalgesia (2).Current evidence implicates multiple signaling pathways in the modulation of VR1. PKA reduces vanilloid receptor type 1 (VR1) desensitization and directly phosphorylates VR1 (3). PKC␣ contributes to VR1 activation by pH (4), and PKC⑀ both directly phosphorylates VR1 and is implicated in the development of hyperalgesia (19). Finally, p38 mitogen-activated ...

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Section: Resultsmentioning

confidence: 98%

Interaction between Protein Kinase Cμ and the Vanilloid Receptor Type 1

Wang

Kedei

Wei

et al. 2004

Journal of Biological Chemistry

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“…In contrast, a variety of proteins can be up-regulated by TSA. The prominent examples include p21 WAF1/CIP1 (32,33), gelsolin (35), cytokeratin A (endoA) (39), Stra13 (40), and plasminogen activator (41). p21 WAF1/CIP1 is an inhibitor of cyclin-dependent kinase, and Stra13 is a transcriptional repressor of the c-myc gene.…”

Section: Discussionmentioning

confidence: 99%

Participation of p97Eps8 in Src-mediated Transformation

Leu

Yeh

Huang

et al. 2004

Journal of Biological Chemistry

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Histone acetylase and histone deacetylase are two crucial enzymes that determine the structure of chromatin, regulating gene expression. In this study, we observed that trichostatin A (TSA), a specific histone deacetylase inhibitor, could effectively inhibit the growth of v-Src-transformed (IV5) cells and abrogate their ability to form colonies in soft agar. Further analysis demonstrated that, although TSA reduced the expression of Eps8 in a dose-and time-dependent manner, both the protein expression and kinase activity of v-Src remained constant, and the abundance and phosphotyrosine levels of Src substrates, including cortactin, focal adhesion kinase, p130 Cas , paxillin, and Shc, were not altered. Notably, removal of TSA from the medium restored not only the expression of Eps8, but also cellular growth. Northern and reverse transcription-PCR analyses revealed the significant reduction of eps8 transcripts in TSA-treated IV5 cells relative to control cells. When active Src-expressing chicken embryonic cells were forced to overexpress p97 Eps8 , they became resistant to TSA-mediated anti-proliferation. Furthermore, using small interference RNA of eps8, we demonstrated the requirement for Eps8 in IV5 cell proliferation. Thus, our results highlight a critical role for p97 Eps8 in TSA-exerted growth inhibition of v-Src-transformed cells.

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“…In particular, histone H4 in heterochromatin regions was less acetylated at lysines 5 and 8 but hyperacetylated at lysine 12 (67). In contrast to all other chromosomes, the inactive mammalian X chromosome is largely unlabelled by specific antibodies directed against the acetylated form of lysines 5,8,12, and 16 at histone H4 (27). Immunoprecipitation of chromatin fragments from human HL-60 cells with similar antibodies confirmed that the heterochromatin contains underacetylated forms of H4, although the acetylation of histone H4 was not correlated with transcriptional activity (47).…”

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confidence: 98%

“…Another important step toward the understanding of the role of histone acetylation was the identification of specific inhibitors of histone deacetylases (12; for a review, see reference 77). Trichostatin A, a fungistatic antibiotic, has been shown to induce differentiation in erythroleukemia cells (78), to block the development of Xenopus and starfish embryos (2), to induce the expression of different genes (5,20,25,43), and to arrest normal fibroblasts in the G 1 or G 2 phase of the cell cycle (76). Furthermore, trichostatin A and trapoxin, another specific inhibitor of histone deacetylases, also have the potential to revert the phenotype of oncogene-transformed fibroblasts (17,62,75).…”

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confidence: 99%

Identification of Mouse Histone Deacetylase 1 as a Growth Factor-Inducible Gene

Bartl

Taplick

Lagger

et al. 1997

Molecular and Cellular Biology

114

100

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Reversible acetylation of core histones plays an important role in transcriptional regulation, cell cycle progression, and developmental events. The acetylation state of histones is controlled by the activities of acetylating and deacetylating enzymes. By using differential mRNA display, we have identified a mouse histone deacetylase gene, HD1, as an interleukin-2-inducible gene in murine T cells. Sequence alignments revealed that murine HD1 is highly homologous to the yeast RPD3 pleiotropic transcriptional regulator. Indirect immunofluorescence microscopy proved that mouse HD1 is a nuclear protein. When expressed in yeast, murine HD1 was also detected in the nucleus, although it failed to complement the rpd3⌬ deletion phenotype. HD1 mRNA expression was low in G 0 mouse cells but increased when the cells crossed the G 1 /S boundary after growth stimulation. Immunoprecipitation experiments and functional in vitro assays showed that HD1 protein is associated with histone deacetylase activity. Both HD1 protein levels and total histone deacetylase activity increased upon interleukin-2 stimulation of resting B6.1 cells. When coexpressed with a luciferase reporter construct, HD1 acted as a negative regulator of the Rous sarcoma virus enhancer/promoter. HD1 overexpression in stably transfected Swiss 3T3 cells caused a severe delay during the G 2 /M phases of the cell cycle. Our results indicate that balanced histone acetylation/deacetylation is crucial for normal cell cycle progression of mammalian cells.

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Stimulation of tissue-type plasminogen activator gene expression by sodium butyrate and trichostatin A in human endothelial cells involves histone acetylation

Cited by 96 publications

References 31 publications

Interaction between Protein Kinase Cμ and the Vanilloid Receptor Type 1

Interaction between Protein Kinase Cμ and the Vanilloid Receptor Type 1

Participation of p97Eps8 in Src-mediated Transformation

Identification of Mouse Histone Deacetylase 1 as a Growth Factor-Inducible Gene

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