Simultaneous activation of heat shock protein (hsp 70) and nucleolin genes during in vivo and in vitro prereplicative stages of rat hepatocytes

Ohmori, Hisamitsu; Murakami, Tadamasa; Furutani, Aki; Higashi, Ken; Hirano, Hideyasu; Gotoh, Sadao; Kuroiwa, Akio; Masui, Asako; Nakamura, Toshikazu; Amalríc, François

doi:10.1016/0014-4827(90)90240-b

Cited by 24 publications

(11 citation statements)

References 48 publications

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“…The increased expression of nucleolin mRNA has been reported in the early stage of embryogenesis of Xenopus laevis (23). The increase of nucleolin protein was also demonstrated in the regenerative liver after partial hepatectomy (32). Moreover, nucleolin was definitely implicated in ribosome biogenesis (9,10).…”

Section: Discussionmentioning

confidence: 86%

Functional Implication of Nucleolin in the Mouse First Molar Development

Xie

Kobayashi

Kiyoshima

et al. 2007

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 86%

Functional Implication of Nucleolin in the Mouse First Molar Development

Xie

Kobayashi

Kiyoshima

et al. 2007

Journal of Biological Chemistry

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“…Thus, APP production was compromised largely by accelerated decay of its coding mRNA. It was previously demonstrated that nucleolin mRNA levels increased in response to PHA in lymphocytes (30), serum stimulation in HeLa cells (31), vitamin A in monkey tracheobronchial epithelial cells (32), interleukin-2 in the C30.1 T cell line (33), and during liver regeneration in rat hepatocytes (34), whereas nucleolin mRNA levels were down-regulated during differentiation of human neuroblastoma cells with dibutyryl cAMP and/or retinoic acid (35) and by glucocorticoids in murine lymphosarcoma cells (36). In this study, we report that phorbol ester activation of ERK in PBMC increased nucleolin mRNA levels, and this increase was predominantly due to posttranscriptional stabilization of nucleolin mRNA.…”

Section: Resultsmentioning

confidence: 99%

Up-regulation of Nucleolin mRNA and Protein in Peripheral Blood Mononuclear Cells by Extracellular-regulated Kinase

Westmark

Malter

2001

Journal of Biological Chemistry

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The signal transduction pathways regulating nucleolin mRNA and protein production have yet to be elucidated. Peripheral blood mononuclear cells treated with phorbol 12-myristate 13-acetate showed steady state levels of nucleolin mRNA that were 2-2.5-fold greater than untreated control cells. The up-regulation of nucleolin mRNA was substantially repressed by U0126, a specific inhibitor that blocks phosphorylation of extracellularregulated kinase (ERK). Calcium ionophores A23187 and ionomycin also activated ERK and substantially elevated nucleolin mRNA levels, demonstrating phorbol 12-myristate 13-acetate and calcium signaling converge on ERK. Drugs that affected protein kinase C, protein kinase A, and phospholipase C signal transduction pathways did not alter nucleolin mRNA levels significantly. The half-life of nucleolin mRNA increased from 1.8 h in resting cells to 3.2 h with phorbol ester activation, suggesting ERK-mediated posttranscriptional regulation. Concomitantly, full-length nucleolin protein was increased. The higher levels of nucleolin protein were accompanied by increased binding of a 70-kDa nucleolin fragment to the 29-base instability element in the 3-untranslated region of amyloid precursor protein (APP) mRNA in gel mobility shift assays. Supplementation of rabbit reticulocyte lysate with nucleolin decreased APP mRNA stability and protein production. These data suggest ERK up-regulates nucleolin posttranscriptionally thereby controlling APP production.

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“…The expression of HSPs 25, 60 70, and 90 has been reported in the liver (Ohmori et al 1990;Delhaye et al 1992;Jorge et al 1993;Koskinas et al 1993;Ciocca et al 1991;Broome et al 1993;Benjamin 1993). HSP70 is induced in hepatectomized liver and in proliferating hepatocytes (Ohmori et al 1990). HSP25 is overexpressed in adenocarcinoma in the liver (Delhaye et al 1992).…”

Section: Discussionmentioning

confidence: 98%

Expression of heat-shock protein 47 in mouse liver

Kawada

Kuroki

Kobayashi

et al. 1996

Cell and Tissue Research

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Expression of heat-shock protein 47 in intact and fibrotic liver and in hepatic constituent cells was investigated in mice. Immunohistochemical study of intact liver and Western blot analysis of the protein from isolated liver cells revealed that stellate cells and smooth muscle cells of interlobular vessels, but not hepatocytes, Kupffer cells, or endothelial cells, expressed heat-shock protein 47. The protein was found in both vitamin-A-storing stellate cells and myofibroblast-like cells. The amount of the protein in cultured stellate cells was reduced by dexamethasone but was not regulated by quercetin, transforming growth factor beta, interferon gamma, or retinoic acid. In CCl4-treated or bile-duct-ligated mouse liver, the number of cells positive for heat-shock protein 47 markedly increased in the centrilobular area or around the periportal area, respectively, and the level of heat-shock protein 47 also increased.

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Simultaneous activation of heat shock protein (hsp 70) and nucleolin genes during in vivo and in vitro prereplicative stages of rat hepatocytes

Cited by 24 publications

References 48 publications

Functional Implication of Nucleolin in the Mouse First Molar Development

Functional Implication of Nucleolin in the Mouse First Molar Development

Up-regulation of Nucleolin mRNA and Protein in Peripheral Blood Mononuclear Cells by Extracellular-regulated Kinase

Expression of heat-shock protein 47 in mouse liver

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