Enhanced Expression of the Mouse L-Histidine Decarboxylase Gene with a Combination of Dexamethasone and 12-O-Tetradecanoylphorbol-13-Acetate

Ohgoh, Makoto; Yamamoto, Jun; Kawata, M.; Yamamura, Isao; Fukui, Tetsuya; Ichikawa, Atsushi

doi:10.1006/bbrc.1993.2366

Cited by 18 publications

(8 citation statements)

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“…tion and maturation of mast cells, as demonstrated by several works performed with HDC knock out mice [Ohtsu et al, 2001;Wiener et al, 2002]. Expression of the HDC gene has been studied in different cell types and tissues such as gastric carcinoma cells, mastocytoma cells, oxyntic mucosa and fetal liver, and it has been shown that it responds to a number of signals, including gastrin, phorbol esters, glucocorticoids or demethylation of its promoter sequences [Kawai et al, 1992;Ohgoh et al, 1993;Hocker et al, 1997a,b;Suzuki-Ishigaki et al, 2000]. However, little is known about the regulation of histamine synthesis in mast cells and other hematopoietic derived cells like basophils and macrophages.…”

Section: Discussionmentioning

confidence: 98%

Polyamines affect histamine synthesis during early stages of IL‐3‐induced bone marrow cell differentiation

Garcia-Faroldi

Correa‐Fiz

Abrighach

et al. 2009

J of Cellular Biochemistry

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Mast cells synthesize and store histamine, a key immunomodulatory mediator. Polyamines are essential for every living cell. Previously, we detected an antagonistic relationship between the metabolisms of these amines in established mast cell and basophilic cell lines. Here, we used the IL-3-driven mouse bone marrow-derived mast cell (BMMC) culture system to further investigate this antagonism in a mast cell model of deeper physiological significance. Polyamines and histamine levels followed opposite profiles along the bone marrow cell cultures leading to BMMCs. alpha-Difluoromethylornithine (DFMO)-induced polyamine depletion resulted in an upregulation of histidine decarboxylase (HDC, the histamine-synthesizing enzyme) expression and activity, accompanied by increased histamine levels, specifically during early stages of these cell cultures, where an active histamine synthesis process occurs. In contrast, DFMO did not induce any effect in either HDC activity or histamine levels of differentiated BMMCs or C57.1 mast cells, that exhibit a nearly inactive histamine synthesis rate. Sequence-specific DNA methylation analysis revealed that the DFMO-induced HDC mRNA upregulation observed in early bone marrow cell cultures is not attributable to a demethylation of the gene promoter caused by the pharmacological polyamine depletion. Taken together, the results support an inverse relationship between histamine and polyamine metabolisms during the bone marrow cell cultures leading to BMMCs and, moreover, suggest that the regulation of the histamine synthesis occurring during the early stages of these cultures depends on the concentrations of polyamines.

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Section: Discussionmentioning

confidence: 98%

Polyamines affect histamine synthesis during early stages of IL‐3‐induced bone marrow cell differentiation

Garcia-Faroldi

Correa‐Fiz

Abrighach

et al. 2009

J of Cellular Biochemistry

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“…However, in adult mammals, HDC is highly expressed in enterochromaffin-like (ECL) cells of the stomach, where HDC activity is tightly regulated by a gut peptide hormone, gastrin (22). HDC regulation occurs at both transcriptional and posttranslational levels, with the latter by proteolytic processing through the ubiquitin-proteasome pathway (11,12,18).HDC promoter activity is upregulated by several different stimuli, including gastrin (45), PMA (21,22,32,45), oxidative stress (20), thrombopointin (34), Helicobacter pylori infection (43,44), and by neural peptide pituitary adenylate cyclaseactivating polypeptide (PACAP) in PC12 cells through a cis element located at the Ϫ177-to Ϫ170-bp (relative to the transcriptional start site) region of the HDC promoter (30). Recently, Kruppel-like factor 4 (KLF4), formerly known as gut-enriched Kruppel-like factor, was shown to inhibit HDC promoter activity through three elements: an upstream GC box and two downstream gastrin-responsive elements (1), both of which are GC-rich sequences.…”

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confidence: 99%

Yin yang 1 (YY1) represseshistidine decarboxylasegene expression with SREBP-1a in part through an upstream Sp1 site

Ai¹,

Liu²,

Wang³

2006

American Journal of Physiology-Gastrointestinal and Liver Physi

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Histidine decarboxylase (HDC) is the enzyme that converts histidine to histamine, a bioamine that plays an important role in many physiological aspects including allergic responses, inflammation, neurotransmission, and gastric acid secretion. In previous studies, we demonstrated that Kruppel-like factor 4 represses HDC promoter activity in a gastric cell line through both an upstream Sp1-binding GC box (GGGCGG sequence) and downstream gastrin-responsive elements. In the current study, Yin Yang 1 (YY1), a pleiotropic transcriptional factor, was also shown in cotransfection assays to repress HDC promoter activity through the upstream GC box. DNA affinity purification assay demonstrated that YY1 was pulled down specifically by the upstream GC box. In addition, sterol-responsive element-binding protein 1a (SREBP-1a), a transcriptional factor that binds YY1, represses the HDC promoter. Interestingly, deletion analysis and cotransfection assays indicated that mutation of the upstream GC box or truncation of downstream gastrin-responsive elements in the HDC promoter disrupted the inhibitory effect of YY1 and SREBP-1a in an identical fashion. Furthermore, quantitative real-time PCR analysis indicated that gastrin treatment downregulated SREBP-1a gene expression and reduced the DNA binding activity of SREBP in EMSAs. Taken together, these results suggest that YY1 and SREBP-1a form a complex to inhibit HDC gene expression through both the upstream GC box and downstream gastrin-responsive elements and gastrin-induced activation of HDC gene expression is mediated at least partly through downregulation of transcriptional repressors such as SREBPs.

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“…The downstream primer was designed from the nucleotide sequence ϩ65 to ϩ91 and had an SphI site in its 5Ј end. HDC phage clone was amplified and digested with XbaI and SphI for subcloning into the XbaI-SphI site of pUC00CAT (36). This plasmid was digested again with BamHI and HindIII, and was subcloned into the BglII-HindIII site of pGL2-basic (Promega).…”

Section: Cotransfection Of Qt6 Cells With Hdc-luciferase and P45 And/mentioning

confidence: 99%

Histidine Decarboxylase Expression in Mouse Mast Cell Line P815 Is Induced by Mouse Peritoneal Cavity Incubation

Ohtsu

Kuramasu

Suzuki

et al. 1996

Journal of Biological Chemistry

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Phenotype of P815 mouse mast cells changes markedly during culture in the peritoneal cavity of syngenic BDF1 mice. The cells, cultured for 1 week in the peritoneal cavity of syngenic BDF1 mice, proliferate and express high levels of L-histidine decarboxylase (HDC) and mouse mast cell protease (MMCP)-6 mRNAs, indicating the ability of P815 cells to differentiate toward mature connective tissue mast cells. Peritoneal fluid aspirated from P815-inoculated BDF1 mouse and added to cultured P815 cells in vitro was also found to induce HDC mRNA expression, suggesting that at least some of the humoral factors in the peritoneal fluid induce HDC mRNA transcription. Among the erythroid transcription factors, P815 cells expressed GATA-2 but not GATA-1 mRNA before and after the intraperitoneal incubation. In contrast, the expression of NF-E2 subunit p45 disappeared, while expression of subunit mafK was markedly reduced after incubation. Cotransfection assays using HDC-luciferase reporter and p45 and/or mafK expression constructs showed that NF-E2 affects the transactivation of HDC gene. These results suggest that NF-E2 is also an important transcription factor in mast cell differentiation.Precursor cells derived from multipotential stem cells differentiate along defined cell lineages in vivo to become mature cells. Mast cells are derived from progenitor cells in the bone marrow and show a characteristic differentiation profile. Differentiation is completed after these cells reach peripheral tissues such as skin, peritoneal cavity, and bronchial submucosa (1). Mouse mast cells are classified into at least two subtypes, i.e. mucosal and connective tissue mast cells (MMC 1 and CTMC), both of which are derived from common precursor cells (2). Mature mast cells retain more intracellular granules containing mast cell-specific proteases than undifferentiated mast cells (3-5). Whereas the proteases in MMC are primarily MMCP-1 (6) and MMCP-2 (7), in CTMC the main granular proteases are MC-CPA (8), MMCP-4 (9), MMCP-5 (10), and MMCP-6 (5, 11). The expression of each mast cell protease changes during differentiation. Therefore, examination of the expression of granular proteases is one way to assess the stage of differentiation and the subtypes of mast cells.Expression of genes conferring certain specific phenotypes during development and differentiation processes is often controlled by lineage-specific transcription factors. For instance, GATA factors and NF-E2 are known to play important roles in the expression of erythroid genes (12). Targeted disruption of mouse GATA-1 and GATA-2 genes results in impaired maturation of erythroid cells and loss of hematopoietic stem cells, respectively (13-17). Furthermore, mast cell-specific genes MC-CPA and IL-4 were also activated by GATA factors (18,19). Therefore, it is suggested that GATA factors are not only expressed but important for the function of mast cells. NF-E2 consists of a hematopoietic lineage-specific p45 subunit and a broadly expressed p18 subunit (20,21). Recently, the p18 subunit...

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Enhanced Expression of the Mouse L-Histidine Decarboxylase Gene with a Combination of Dexamethasone and 12-O-Tetradecanoylphorbol-13-Acetate

Cited by 18 publications

References 0 publications

Polyamines affect histamine synthesis during early stages of IL‐3‐induced bone marrow cell differentiation

Polyamines affect histamine synthesis during early stages of IL‐3‐induced bone marrow cell differentiation

Yin yang 1 (YY1) represseshistidine decarboxylasegene expression with SREBP-1a in part through an upstream Sp1 site

Histidine Decarboxylase Expression in Mouse Mast Cell Line P815 Is Induced by Mouse Peritoneal Cavity Incubation

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