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Journal articles on the topic 'Hepatocyte nuclear factor'

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Published: 4 June 2021

Last updated: 1 February 2022

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1

Eeckhoute, J. "Hepatocyte Nuclear Factor 4 enhances the Hepatocyte Nuclear Factor 1 -mediated activation of transcription." Nucleic Acids Research 32, no. 8 (April 28, 2004): 2586–93. http://dx.doi.org/10.1093/nar/gkh581.

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2

Sund, Newman J., Siew-Lan Ang, Sara Dutton Sackett, Wei Shen, Nathalie Daigle, Mark A. Magnuson, and Klaus H. Kaestner. "Hepatocyte Nuclear Factor 3β (Foxa2) Is Dispensable for Maintaining the Differentiated State of the Adult Hepatocyte." Molecular and Cellular Biology 20, no. 14 (July 15, 2000): 5175–83. http://dx.doi.org/10.1128/mcb.20.14.5175-5183.2000.

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ABSTRACT Liver-specific gene expression is controlled by a heterogeneous group of hepatocyte-enriched transcription factors. One of these, the winged helix transcription factor hepatocyte nuclear factor 3β (HNF3β or Foxa2) is essential for multiple stages of embryonic development. Recently, HNF3β has been shown to be an important regulator of other hepatocyte-enriched transcription factors as well as the expression of liver-specific structural genes. We have addressed the role of HNF3β in maintenance of the hepatocyte phenotype by inactivation ofHNF3β in the liver. Remarkably, adult mice lackingHNF3β expression specifically in hepatocytes are viable, with histologically normal livers and normal liver function. Moreover, analysis of >8,000 mRNAs by array hybridization revealed that lack ofHNF3β affects the expression of only very few genes. Based on earlier work it appears that HNF3β plays a critical role in early liver development; however, our studies demonstrate that HNF3β is not required for maintenance of the adult hepatocyte or for normal liver function. This is the first example of such functional dichotomy for a tissue specification transcription factor.

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3

ULVILA, Johanna, Satu ARPIAINEN, Olavi PELKONEN, Kaoru AIDA, Tatsuya SUEYOSHI, Masahiko NEGISHI, and Jukka HAKKOLA. "Regulation of Cyp2a5 transcription in mouse primary hepatocytes: roles of hepatocyte nuclear factor 4 and nuclear factor I." Biochemical Journal 381, no. 3 (July 27, 2004): 887–94. http://dx.doi.org/10.1042/bj20040387.

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The cytochrome P4502a5 (Cyp2a5) gene is expressed principally in liver and olfactory mucosa. In the present study, the transcriptional mechanisms of hepatocyte-specific expression of Cyp2a5 were studied in mouse primary hepatocytes. The Cyp2a5 5′-flanking region −3033 to +10 was cloned in front of a luciferase reporter gene and transfected into hepatocytes. Deletion analysis revealed two major activating promoter regions localized at proximal 271 bp and at a more distal area from −3033 to −2014 bp. The proximal activation region was characterized further by DNase I footprinting, and a single clear footprint was detected in the studied area centred over a sequence similar to the NF-I (nuclear factor I)-binding site. The binding of NF-I was confirmed using an EMSA (electrophoretic mobility-shift assay). A putative HNF-4 (hepatocyte nuclear factor 4)-binding site was localized at the proximal promoter by computer analysis of the sequence, and HNF-4α was shown to interact with the site using an EMSA. The functional significance of HNF-4 and NF-I binding to the Cyp2a5 promoter was evaluated by site-directed mutagenesis of the binding motifs in reporter constructs. Both mutations strongly decreased transcriptional activation by the Cyp2a5 promoter in primary hepatocytes, and double mutation almost completely abolished transcriptional activity. Also, the functionality of the distal activation region was found to be dependent on the intact HNF-4 and NF-I sites at the proximal promoter. In conclusion, these results indicate that HNF-4 and NF-I play major roles in the constitutive regulation of hepatic expression of Cyp2a5.

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4

Wang, Zhongyan, and Peter A. Burke. "Hepatocyte nuclear factor-4α interacts with other hepatocyte nuclear factors in regulating transthyretin gene expression." FEBS Journal 277, no. 19 (August 23, 2010): 4066–75. http://dx.doi.org/10.1111/j.1742-4658.2010.07802.x.

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5

Gardner-Stephen, Dione A., and Peter I. Mackenzie. "Hepatocyte nuclear factor1 transcription factors are essential for the UDP-glucuronosyltransferase 1A9 promoter response to hepatocyte nuclear factor 4α." Pharmacogenetics and Genomics 17, no. 1 (January 2007): 25–36. http://dx.doi.org/10.1097/fpc.0b013e32801112b5.

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6

Khurana, Satish, Amit K. Jaiswal, and Asok Mukhopadhyay. "Hepatocyte Nuclear Factor-4α Induces Transdifferentiation of Hematopoietic Cells into Hepatocytes." Journal of Biological Chemistry 285, no. 7 (December 16, 2009): 4725–31. http://dx.doi.org/10.1074/jbc.m109.058198.

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7

Tian, J. M., and U. Schibler. "Tissue-specific expression of the gene encoding hepatocyte nuclear factor 1 may involve hepatocyte nuclear factor 4." Genes & Development 5, no. 12a (December 1, 1991): 2225–34. http://dx.doi.org/10.1101/gad.5.12a.2225.

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8

Aboudehen, Karam, Min Soo Kim, Matthew Mitsche, Kristina Garland, Norma Anderson, Lama Noureddine, Marco Pontoglio, et al. "Transcription Factor Hepatocyte Nuclear Factor–1βRegulates Renal Cholesterol Metabolism." Journal of the American Society of Nephrology 27, no. 8 (December 28, 2015): 2408–21. http://dx.doi.org/10.1681/asn.2015060607.

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9

Freedman, A. R., R. J. Sharma, G. J. Nabel, S. G. Emerson, and G. E. Griffin. "Cellular distribution of nuclear factor κB binding activity in rat liver." Biochemical Journal 287, no. 2 (October 15, 1992): 645–49. http://dx.doi.org/10.1042/bj2870645.

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The cellular localization of nuclear factor kappa B (NF-kappa B) binding activity in rat liver has been investigated using electrophoretic mobility shift assay on extracts of highly purified hepatocytes and Kupffer cells obtained from liver perfused in vivo with collagenase. Constitutive NF-kappa B binding activity was demonstrated in nuclear extracts of control Kupffer cells, and this was not apparently influenced by injection of lipopolysaccharide (LPS) into rats 24 h before perfusion. In contrast, little nuclear NF-kappa B binding activity was present in hepatocytes from control animals, although there was detectable inactive, inhibitor-bound, NF-kappa B in the cytoplasm. However, nuclear NF-kappa B binding activity was increased in hepatocytes from LPS-treated animals and after in vitro culture of control rat hepatocytes. Thus NF-kappa B binding activity has been demonstrated in highly purified hepatocytes and appears to be inducible both in vivo and in vitro. These findings support a role for NF-kappa B in hepatocyte gene regulation which may be important in the modulation of the hepatic acute phase response.

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10

Tang, Hong, and Alan McLachlan. "Avian and Mammalian Hepadnaviruses Have Distinct Transcription Factor Requirements for Viral Replication." Journal of Virology 76, no. 15 (August 1, 2002): 7468–72. http://dx.doi.org/10.1128/jvi.76.15.7468-7472.2002.

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ABSTRACT Hepadnavirus replication occurs in hepatocytes in vivo and in hepatoma cell lines in cell culture. Hepatitis B virus (HBV) replication can occur in nonhepatoma cells when pregenomic RNA synthesis from viral DNA is activated by the expression of the nuclear hormone receptors hepatocyte nuclear factor 4 (HNF4) and the retinoid X receptor α (RXRα) plus peroxisome proliferator-activated receptor α (PPARα) heterodimer. Nuclear hormone receptor-dependent HBV replication is inhibited by hepatocyte nuclear factor 3 (HNF3). In contrast, HNF3 and HNF4 support duck hepatitis B virus (DHBV) replication in nonhepatoma cells, whereas the RXRα-PPARα heterodimer inhibits HNF4-dependent DHBV replication. HNF3 and HNF4 synergistically activate DHBV pregenomic RNA synthesis and viral replication. The conditions that support HBV or DHBV replication in nonhepatoma cells are not able to support woodchuck hepatitis virus replication. These observations indicate that avian and mammalian hepadnaviruses have distinct transcription factor requirements for viral replication.

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11

Pierreux, C. E., J. Stafford, D. Demonte, D. K. Scott, J. Vandenhaute, R. M. O'Brien, D. K. Granner, G. G. Rousseau, and F. P. Lemaigre. "Antiglucocorticoid activity of hepatocyte nuclear factor-6." Proceedings of the National Academy of Sciences 96, no. 16 (August 3, 1999): 8961–66. http://dx.doi.org/10.1073/pnas.96.16.8961.

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12

Dmitrieva, Renata I., Cruz A. Hinojos, Eric Boerwinkle, Michael C. Braun, Myriam Fornage, and Peter A. Doris. "Hepatocyte Nuclear Factor 1 and Hypertensive Nephropathy." Hypertension 51, no. 6 (June 2008): 1583–89. http://dx.doi.org/10.1161/hypertensionaha.108.110163.

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13

Lannoy, Vincent J., Annie Rodolosse, Christophe E. Pierreux, Guy G. Rousseau, and Frédéric P. Lemaigre. "Transcriptional Stimulation by Hepatocyte Nuclear Factor-6." Journal of Biological Chemistry 275, no. 29 (May 12, 2000): 22098–103. http://dx.doi.org/10.1074/jbc.m000855200.

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14

Wang, Kewei, and Ai-Xuan Holterman. "Pathophysiologic role of hepatocyte nuclear factor 6." Cellular Signalling 24, no. 1 (January 2012): 9–16. http://dx.doi.org/10.1016/j.cellsig.2011.08.009.

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15

Yue, H.-Y., C. Yin, J.-L. Hou, X. Zeng, Y.-X. Chen, W. Zhong, P.-F. Hu, et al. "Hepatocyte nuclear factor 4α attenuates hepatic fibrosis in rats." Gut 59, no. 2 (August 10, 2009): 236–46. http://dx.doi.org/10.1136/gut.2008.174904.

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Background and aimsHepatocyte nuclear factor 4α (HNF4α) is a central transcriptional regulator of hepatocyte differentiation and function. The aim of this study was to evaluate the effect of HNF4α on attenuation of hepatic fibrosis.MethodsThe adenoviruses carrying HNF4α gene or containing siRNA targeting HNF4α were injected through tail vein on two distinct hepatic fibrosis models either induced by dimethylnitrosamine or by bile duct ligation in rats. Moreover, HNF4α, epithelial–mesenchymal transition (EMT)-related and fibrotic markers in hepatocytes, hepatic stellate cells (HSCs) and liver tissues were detected by real time PCR, immunofluorescence or immunohistochemistry.ResultsWe demonstrated that decreased expression of HNF4α and epithelial markers accompanied by enhanced expression of mesenchymal markers occurred in fibrotic liver. More importantly, forced expression of HNF4α remarkably alleviated hepatic fibrosis and improved liver function with suppression of EMT in both fibrosis models. In contrast, downregulation of HNF4α by siRNA aggravated hepatic fibrosis and decreased the expression of E-cadherin in association with the enhanced expression of vimentin and fibroblast-specific protein-1. In vitro study revealed that HNF4α could suppress the EMT process of hepatocytes induced by transforming growth factor-β1 and increase the expression of liver-specific genes. A similar phenomenon of the EMT process was observed during the activation of HSCs, which was abrogated by HNF4α. Additionally, HNF4α deactivated the myofibroblasts through inducing the mesenchymal-to-epithelial transition and inhibited their proliferation.ConclusionsOur study suggests that HNF4α is critical for hepatic fibrogenesis and upregulation of HNF4α might present as an ideal option for the treatment of hepatic fibrosis.

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16

Bulla, G. A. "Hepatocyte nuclear factor-4 prevents silencing of hepatocyte nuclear factor-1 expression in hepatoma x fibroblast cell hybrids." Nucleic Acids Research 25, no. 12 (June 1, 1997): 2501–8. http://dx.doi.org/10.1093/nar/25.12.2501.

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17

ERICKSON, Roger H., James R. GUM, Craig D. LOTTERMAN, James W. HICKS, Roy S. LAI, and Young S. KIM. "Regulation of the gene for human dipeptidyl peptidase IV by hepatocyte nuclear factor 1α." Biochemical Journal 338, no. 1 (February 8, 1999): 91–97. http://dx.doi.org/10.1042/bj3380091.

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Hepatocyte nuclear factor 1 was identified as the transcription factor binding to a 20 bp (-150 to -131) region of the gene for human dipeptidyl peptidase IV, which has been shown to be important for the expression of dipeptidyl peptidase IV in the human intestinal and hepatic epithelial cell lines Caco-2 and HepG2. Functional analysis of the hepatocyte nuclear factor 1 site was performed with two minimal dipeptidyl peptidase IV promoter constructs (-250 to -41, and -150 to -41) with and without a 3 bp mutation in the hepatocyte nuclear factor 1 sequence, and used in transient transfection experiments with Caco-2 cells. The results show that the mutated constructs were able to drive transcription at only 5–10% of the activity of the non-mutated controls. Co-transfection of 3T3 cells with hepatocyte nuclear factor 1 (α or β) and dipeptidyl peptidase IV promoter constructs (-250 to -41 or -150 to -41) resulted in a 2.5–6-fold increase in transcription over controls with hepatocyte nuclear factor 1α but not with hepatocyte nuclear factor 1β. The results of this study show that hepatocyte nuclear factor 1 binds to the -150 to -131 region of the human dipeptidyl peptidase IV promoter and is necessary for transcriptional activation of the gene for dipeptidyl peptidase IV.

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18

Wu, Zhi-Tao, Dan Yao, Shu-Yi Ji, Xuan Ni, Yi-Meng Gao, Li-Jian Hui, and Guo-Yu Pan. "Optimized Hepatocyte-Like Cells with Functional Drug Transporters Directly-Reprogrammed from Mouse Fibroblasts and their Potential in Drug Disposition and Toxicology." Cellular Physiology and Biochemistry 38, no. 5 (2016): 1815–30. http://dx.doi.org/10.1159/000443120.

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Background/Aims: To develop a suitable hepatocyte-like cell model that could be a substitute for primary hepatocytes with essential transporter expression and functions. Induced hepatocyte-like (iHep) cells directly reprogrammed from mice fibroblast cells were fully characterized. Methods: Naïve iHep cells were transfected with nuclear hepatocyte factor 4 alpha (Hnf4α) and treated with selected small molecules. Sandwich cultured configuration was applied. The mRNA and protein expression of transporters were determined by Real Time PCR and confocal. The functional transporters were estimated by drug biliary excretion measurement. The inhibition of bile acid efflux transporters by cholestatic drugs were assessed. Results: The expression and function of p-glycoprotein (P-gp), bile salt efflux pump (Bsep), multidrug resistance-associated protein 2 (Mrp2), Na+-dependent taurocholate cotransporting polypeptide (Ntcp), and organic anion transporter polypedtides (Oatps) in iHep cells were significantly improved after transfection of hepatocyte nuclear factor 4 alpha (Hnf4α) and treatment with selected inducers. In vitro intrinsic biliary clearances (CLb,int) of optimized iHep cells for rosuvastatin, methotrexate, d8-TCA (deuterium-labeled sodium taurocholate acid) and DPDPE ([D-Pen2,5] enkephalin hydrate) correlated well with that of sandwich-cultured primary mouse hepatocytes (SCMHs) (r2 = 0.984). Cholestatic drugs were evaluated and the results were compared well with primary mice hepatocytes. Conclusion: The optimized iHep cells expressed functional drug transporters and were comparable to primary mice hepatocytes. This study suggested direct reprogramming could provide a potential alternative to primary hepatocytes for drug candidate hepatobiliary disposition and hepatotoxicity screening.

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19

Liu, Hua, Hui Ren, and Brett T. Spear. "The Mouse Alpha-Albumin (Afamin) Promoter Is Differentially Regulated by Hepatocyte Nuclear Factor 1α and Hepatocyte Nuclear Factor 1β." DNA and Cell Biology 30, no. 3 (March 2011): 137–47. http://dx.doi.org/10.1089/dna.2010.1097.

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20

Hadzopoulou-Cladaras, Margarita, Elena Kistanova, Catherine Evagelopoulou, Shengyou Zeng, Christos Cladaras, and John A. A. Ladias. "Functional Domains of the Nuclear Receptor Hepatocyte Nuclear Factor 4." Journal of Biological Chemistry 272, no. 1 (January 3, 1997): 539–50. http://dx.doi.org/10.1074/jbc.272.1.539.

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21

Nikolaidou-Neokosmidou, Varvara, Vassilis I. Zannis, and Dimitris Kardassis. "Inhibition of hepatocyte nuclear factor 4 transcriptional activity by the nuclear factor κB pathway." Biochemical Journal 398, no. 3 (August 29, 2006): 439–50. http://dx.doi.org/10.1042/bj20060169.

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HNF-4 (hepatocyte nuclear factor 4) is a key regulator of liver-specific gene expression in mammals. We have shown previously that the activity of the human APOC3 (apolipoprotein C-III) promoter is positively regulated by the anti-inflammatory cytokine TGFβ (transforming growth factor β) and its effectors Smad3 (similar to mothers against decapentaplegic 3) and Smad4 proteins via physical and functional interactions between Smads and HNF-4. We now show that the pro-inflammatory cytokine TNFα (tumour necrosis factor α) antagonizes TGFβ for the regulation of APOC3 gene expression in hepatocytes. TNFα was a strong inhibitor of the activity of apolipoprotein promoters that harbour HNF-4 binding sites and this inhibition required HNF-4. Using specific inhibitors of TNFα-induced signalling pathways, it was shown that inhibition of the APOC3 promoter by TNFα involved NF-κB (nuclear factor κB). Latent membrane protein 1 of the Epstein–Barr virus, which is an established potent activator of NF-κB as well as wild-type forms of various NF-κB signalling mediators, also inhibited strongly the APOC3 promoter and the transactivation function of HNF-4. TNFα had no effect on the stability or the nuclear localization of HNF-4 in HepG2 cells, but inhibited the binding of HNF-4 to the proximal APOC3 HRE (hormone response element). Using the yeast-transactivator-GAL4 system, we showed that both AF-1 and AF-2 (activation functions 1 and 2) of HNF-4 are inhibited by TNFα and that this inhibition was abolished by overexpression of different HNF-4 co-activators, including PGC-1 (peroxisome-proliferator-activated-receptor-γ co-activator 1), CBP [CREB (cAMP-response-element-binding protein) binding protein] and SRC3 (steroid receptor co-activator 3). In summary, our findings indicate that TNFα, or other factors that trigger an NF-κB response in hepatic cells, inhibit the transcriptional activity of the APOC3 and other HNF-4-dependent promoters and that this inhibition could be accounted for by a decrease in DNA binding and the down-regulation of the transactivation potential of the AF-1 and AF-2 domains of HNF-4.

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22

Ning, Bei-Fang, Jin Ding, Jiao Liu, Chuan Yin, Wen-Ping Xu, Wen-Ming Cong, Qing Zhang, et al. "Hepatocyte nuclear factor 4α-nuclear factor-κB feedback circuit modulates liver cancer progression." Hepatology 60, no. 5 (June 27, 2014): 1607–19. http://dx.doi.org/10.1002/hep.27177.

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23

Bonzo, Jessica A., Christina H. Ferry, Tsutomu Matsubara, Jung-Hwan Kim, and Frank J. Gonzalez. "Suppression of Hepatocyte Proliferation by Hepatocyte Nuclear Factor 4α in Adult Mice." Journal of Biological Chemistry 287, no. 10 (January 12, 2012): 7345–56. http://dx.doi.org/10.1074/jbc.m111.334599.

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24

Gonzalez, Frank J. "Regulation of Hepatocyte Nuclear Factor 4α-mediated Transcription." Drug Metabolism and Pharmacokinetics 23, no. 1 (2008): 2–7. http://dx.doi.org/10.2133/dmpk.23.2.

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25

Massa, F., S. Garbay, R. Bouvier, Y. Sugitani, T. Noda, M. C. Gubler, L. Heidet, M. Pontoglio, and E. Fischer. "Hepatocyte nuclear factor 1 controls nephron tubular development." Development 140, no. 4 (January 29, 2013): 886–96. http://dx.doi.org/10.1242/dev.086546.

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26

de Boussac, Hugues, Marcin Ratajewski, Iwona Sachrajda, Gabriella Köblös, Attila Tordai, Lukasz Pulaski, László Buday, András Váradi, and Tamás Arányi. "The ERK1/2-Hepatocyte Nuclear Factor 4α Axis Regulates HumanABCC6Gene Expression in Hepatocytes." Journal of Biological Chemistry 285, no. 30 (May 12, 2010): 22800–22808. http://dx.doi.org/10.1074/jbc.m110.105593.

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27

Rausa, Francisco M., Yongjun Tan, Heping Zhou, Kyung W. Yoo, Donna Beer Stolz, Simon C. Watkins, Roberta R. Franks, Terry G. Unterman, and Robert H. Costa. "Elevated Levels of Hepatocyte Nuclear Factor 3β in Mouse Hepatocytes Influence Expression of Genes Involved in Bile Acid and Glucose Homeostasis." Molecular and Cellular Biology 20, no. 21 (November 1, 2000): 8264–82. http://dx.doi.org/10.1128/mcb.20.21.8264-8282.2000.

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ABSTRACT The winged helix transcription factor, hepatocyte nuclear factor-3β (HNF-3β), mediates the hepatocyte-specific transcription of numerous genes important for liver function. However, the in vivo role of HNF-3β in regulating these genes remains unknown because homozygous null HNF3β mouse embryos die in utero prior to liver formation. In order to examine the regulatory function of HNF-3β, we created transgenic mice in which the −3-kb transthyretin promoter functions to increase hepatocyte expression of the rat HNF-3β protein. Postnatal transgenic mice exhibit growth retardation, depletion of hepatocyte glycogen storage, and elevated levels of bile acids in serum. The retarded growth phenotype is likely due to a 20-fold increase in hepatic expression of insulin-like growth factor binding protein 1 (IGFBP-1), which results in elevated levels in serum of IGFBP-1 and limits the biological availability of IGFs required for postnatal growth. The defects in glycogen storage and serum bile acids coincide with diminished postnatal expression of hepatocyte genes involved in gluconeogenesis (phosphoenolpyruvate carboxykinase and glycogen synthase) and sinusoidal bile acid uptake (Ntcp), respectively. These changes in gene transcription may result from the disruptive effect of HNF-3β on the hepatic expression of the endogenous mouse HNF-3α,-3β, -3γ, and -6 transcription factors. Furthermore, adult transgenic livers lack expression of the canalicular phospholipid transporter, mdr2, which is consistent with ultrastructure evidence of damage to transgenic hepatocytes and bile canaliculi. These transgenic studies represent the first in vivo demonstration that the HNF-3β transcriptional network regulates expression of hepatocyte-specific genes required for bile acid and glucose homeostasis, as well as postnatal growth.

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28

Ninomiya, Toshiaki, Hayashi Yoshitake, Saijoh Kiyofumi, Ohta Kyosuke, Yoon Seitetsu, Nakabayashi Hidekazu, Tamaoki Taiki, Kasuga Masato, and Itoh Hiroshi. "Expression ratio of hepatocyte nuclear factor-1 to variant hepatocyte nuclear factor-1 in differentiation of hepatocellular carcinoma and hepatoblastoma." Journal of Hepatology 25, no. 4 (October 1996): 445–53. http://dx.doi.org/10.1016/s0168-8278(96)80203-0.

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29

Guo, Hongtao, Chengjiang Gao, Zhiyong Mi, Philip Y. Wai, and Paul C. Kuo. "Phosphorylation of Ser158 regulates inflammatory redox-dependent hepatocyte nuclear factor-4α transcriptional activity." Biochemical Journal 394, no. 2 (February 10, 2006): 379–87. http://dx.doi.org/10.1042/bj20051730.

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In IL-1β (interleukin 1β)-stimulated rat hepatocytes exposed to superoxide, we have previously identified an IRX (inflammatory redox)-sensitive DR1 [direct repeat of RG(G/T)TCA with one base spacing] cis-acting activator element (nt –1327 to –1315) in the iNOS (inducible nitric oxide synthase) promoter: AGGTCAGGGGACA. The corresponding transcription factor was identified to be HNF4α (hepatocyte nuclear factor-4α). HNF4α DNA binding activity and transactivation potential are tightly regulated by its state of phosphorylation. However, the functional consequences of IRX-mediated post-translational phosphorylation of HNF4α have not been well characterized. In the setting of IL-1β+H2O2, HNF4α functional activity is associated with a unique serine/threonine phosphorylation pattern. This indicates that an IRX-sensitive serine/threonine kinase pathway targets HNF4α to augment hepatocyte iNOS transcription. In the present study, following identification of phosphorylated residues in HNF4α, serial mutations were performed to render the target residues phosphorylation-resistant. Electrophoretic mobility-shift assays and transient transfection studies utilizing the iNOS promoter showed that the S158A mutation ablates IRX-mediated HNF4α DNA binding and transactivation. Gain-of-function mutation with the S158D phosphomimetic HNF4α vector supports a critical role for Ser158 phosphorylation. In vitro phosphorylation and kinase inhibitor studies implicate p38 kinase activity. Our results indicate that p38 kinase-mediated Ser158 phosphorylation is essential for augmentation of the DNA binding and transactivation potential of HNF4α in the presence of IL-1β+H2O2. This pathway results in enhanced iNOS expression in hepatocytes exposed to pro-inflammatory cytokines and oxidative stress.

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30

Walesky, Chad, Sumedha Gunewardena, Ernest F. Terwilliger, Genea Edwards, Prachi Borude, and Udayan Apte. "Hepatocyte-specific deletion of hepatocyte nuclear factor-4α in adult mice results in increased hepatocyte proliferation." American Journal of Physiology-Gastrointestinal and Liver Physiology 304, no. 1 (January 1, 2013): G26—G37. http://dx.doi.org/10.1152/ajpgi.00064.2012.

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Hepatocyte nuclear factor-4α (HNF4α) is known as the master regulator of hepatocyte differentiation. Recent studies indicate that HNF4α may inhibit hepatocyte proliferation via mechanisms that have yet to be identified. Using a HNF4α knockdown mouse model based on delivery of inducible Cre recombinase via an adeno-associated virus 8 viral vector, we investigated the role of HNF4α in the regulation of hepatocyte proliferation. Hepatocyte-specific deletion of HNF4α resulted in increased hepatocyte proliferation. Global gene expression analysis showed that a majority of the downregulated genes were previously known HNF4α target genes involved in hepatic differentiation. Interestingly, ≥500 upregulated genes were associated with cell proliferation and cancer. Furthermore, we identified potential negative target genes of HNF4α, many of which are involved in the stimulation of proliferation. Using chromatin immunoprecipitation analysis, we confirmed binding of HNF4α at three of these genes. Furthermore, overexpression of HNF4α in mouse hepatocellular carcinoma cells resulted in a decrease in promitogenic gene expression and cell cycle arrest. Taken together, these data indicate that, apart from its role in hepatocyte differentiation, HNF4α actively inhibits hepatocyte proliferation by repression of specific promitogenic genes.

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31

Courtois, G., S. Baumhueter, and G. R. Crabtree. "Purified hepatocyte nuclear factor 1 interacts with a family of hepatocyte-specific promoters." Proceedings of the National Academy of Sciences 85, no. 21 (November 1, 1988): 7937–41. http://dx.doi.org/10.1073/pnas.85.21.7937.

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32

Hayhurst, Graham P., Ying-Hue Lee, Gilles Lambert, Jerrold M. Ward, and Frank J. Gonzalez. "Hepatocyte Nuclear Factor 4α (Nuclear Receptor 2A1) Is Essential for Maintenance of Hepatic Gene Expression and Lipid Homeostasis." Molecular and Cellular Biology 21, no. 4 (February 15, 2001): 1393–403. http://dx.doi.org/10.1128/mcb.21.4.1393-1403.2001.

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ABSTRACT The numerous functions of the liver are controlled primarily at the transcriptional level by the concerted actions of a limited number of hepatocyte-enriched transcription factors (hepatocyte nuclear factor 1α [HNF1α], -1β, -3α, -3β, -3γ, -4α, and -6 and members of the c/ebp family). Of these, only HNF4α (nuclear receptor 2A1) and HNF1α appear to be correlated with the differentiated phenotype of cultured hepatoma cells. HNF1α-null mice are viable, indicating that this factor is not an absolute requirement for the formation of an active hepatic parenchyma. In contrast, HNF4α-null mice die during embryogenesis. Moreover, recent in vitro experiments using tetraploid aggregation suggest that HNF4α is indispensable for hepatocyte differentiation. However, the function of HNF4α in the maintenance of hepatocyte differentiation and function is less well understood. To address the function of HNF4α in the mature hepatocyte, a conditional gene knockout was produced using the Cre-loxP system. Mice lacking hepatic HNF4α expression accumulated lipid in the liver and exhibited greatly reduced serum cholesterol and triglyceride levels and increased serum bile acid concentrations. The observed phenotypes may be explained by (i) a selective disruption of very-low-density lipoprotein secretion due to decreased expression of genes encoding apolipoprotein B and microsomal triglyceride transfer protein, (ii) an increase in hepatic cholesterol uptake due to increased expression of the major high-density lipoprotein receptor, scavenger receptor BI, and (iii) a decrease in bile acid uptake to the liver due to down-regulation of the major basolateral bile acid transporters sodium taurocholate cotransporter protein and organic anion transporter protein 1. These data indicate that HNF4α is central to the maintenance of hepatocyte differentiation and is a major in vivo regulator of genes involved in the control of lipid homeostasis.

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Rawat, Siddhartha, and Michael J. Bouchard. "The Hepatitis B Virus (HBV) HBx Protein Activates AKT To Simultaneously Regulate HBV Replication and Hepatocyte Survival." Journal of Virology 89, no. 2 (October 29, 2014): 999–1012. http://dx.doi.org/10.1128/jvi.02440-14.

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ABSTRACTChronic infection with hepatitis B virus (HBV) is a risk factor for developing liver diseases such as hepatocellular carcinoma (HCC). HBx is a multifunctional protein encoded by the HBV genome; HBx stimulates HBV replication and is thought to play an important role in the development of HBV-associated HCC. HBx can activate the phosphatidylinositol 3-kinase (PI3K)/AKT signaling pathway in some cell lines; however, whether HBx regulates PI3K/AKT signaling in normal hepatocytes has not been evaluated. In studies described here, we assessed HBx activation of PI3K/AKT signaling in anex vivomodel of cultured primary hepatocytes and determined how this HBx activity affects HBV replication. We report that HBx activates AKT in primary hepatocytes and that the activation of AKT decreases HBV replication and HBV mRNA and core protein levels. We show that the transcription factor hepatocyte nuclear factor 4α (HNF4α) is a target of HBx-regulated AKT, and we link HNF4α to HBx-regulated AKT modulation of HBV transcription and replication. Although we and others have shown that HBx stimulates and is likely required for HBV replication, we now report that HBx also activates signals that can diminish the overall level of HBV replication. While this may seem counterintuitive, we show that an important effect of HBx activation of AKT is inhibition of apoptosis. Consequently, our studies suggest that HBx balances HBV replication and cell survival by stimulating signaling pathways that enhance hepatocyte survival at the expense of higher levels of HBV replication.IMPORTANCEChronic hepatitis B virus (HBV) infection is a common cause of the development of liver cancer. Regulation of cell signaling pathways by the HBV HBx protein is thought to influence the development of HBV-associated liver cancer. HBx stimulates, and may be essential for, HBV replication. We show that HBx activates AKT in hepatocytes to reduce HBV replication. While this seems contradictory to an essential role of HBx during HBV replication, HBx activation of AKT inhibits hepatocyte apoptosis, and this may facilitate persistent, noncytopathic HBV replication. AKT regulates HBV replication by reducing the activity of the transcription factor hepatocyte nuclear factor 4α (HNF4α). HBx activation of AKT may contribute to the development of liver cancer by facilitating persistent HBV replication, augmenting the dedifferentiation of hepatocytes by inhibiting HNF4α functions, and activating AKT-regulated oncogenic pathways. AKT-regulated factors may provide therapeutic targets for inhibiting HBV replication and the development of HBV-associated liver cancer.

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Drewes, Thorsten, Annette Clairmont, Ludger Klein-Hitpass, and Gerhart U. Ryffel. "Estrogen-Inducible Derivatives of Hepatocyte Nuclear Factor-4, Hepatocyte Nuclear Factor-3 and Liver Factor B1 are Differently Affected by Pure and Partial Antiestrogens." European Journal of Biochemistry 225, no. 1 (October 1994): 441–48. http://dx.doi.org/10.1111/j.1432-1033.1994.00441.x.

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Chou, Ho, Lai, Chen, Wu, Shun, Wen, and Lai. "B-Cell Activating Factor Enhances Hepatocyte-Driven Angiogenesis via B-Cell CLL/Lymphoma 10/Nuclear Factor-KappaB Signaling during Liver Regeneration." International Journal of Molecular Sciences 20, no. 20 (October 10, 2019): 5022. http://dx.doi.org/10.3390/ijms20205022.

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B-cell activating factor (BAFF) is found to be associated with the histological severity of nonalcoholic steatohepatitis (NASH). BAFF was also found to have a protective role in hepatic steatosis via down regulating the expression of steatogenesis genes and enhancing steatosis in hepatocytes through BAFF-R. However, the roles of BAFF during liver regeneration are not well defined. In this study, C57/B6 mice with 70% partial hepatectomy were used as a liver regeneration model. BAFF expression was determined by enzyme immunoassay, and anti-BAFF-neutralizing antibodies were administered to confirm the effects of BAFF on liver regeneration. Western blotting, immunohistochemistry, and florescence staining determined the expression of B-cell CCL/lymphoma 10 (BCL10). The angiogenesis promoting capability was evaluated after the transfection of cells with siRNA targeting BCL10 expression, and the role of NF-κB was assessed. The results revealed that the BAFF and BCL10 levels were upregulated after partial hepatectomy. Treatment with anti-BAFF-neutralizing antibodies caused death in mice that were subjected to 70% partial hepatectomy within 72 h. In vitro, recombinant BAFF protein did not enhance hepatocyte proliferation; however, transfection with BCL10 siRNA arrested hepatocytes at the G2/M phase. Interestingly, conditioned medium from BAFF-treated hepatocytes enhanced angiogenesis and endothelial cell proliferation. Moreover, Matrix metalloproteinase-9 (MMP-9), Fibroblast growth factor 4 (FGF4), and Interleukin-8 (IL-8) proteins were upregulated by BAFF through BCL10/NF-κB signaling. In mice that were treated with anti-BAFF-neutralizing antibodies, the microvessel density (MVD) of the remaining liver tissues and liver regeneration were both reduced. Taken together, our study demonstrated that an increased expression of BAFF and activation of BCL10/NF-κB signaling were involved in hepatocyte-driven angiogenesis and survival during liver regeneration.

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Cheng, Chun-Chia, Wan-Yu Yang, Ming-Chen Hsiao, Kuan-Hao Lin, Hao-Wei Lee, and Chiou-Hwa Yuh. "Transcriptomically Revealed Oligo-Fucoidan Enhances the Immune System and Protects Hepatocytes via the ASGPR/STAT3/HNF4A Axis." Biomolecules 10, no. 6 (June 12, 2020): 898. http://dx.doi.org/10.3390/biom10060898.

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Oligo-fucoidan, a sulfated polysaccharide extracted from brown seaweed, exhibits anti-inflammatory and anti-tumor effects. However, the knowledge concerning the detailed mechanism of oligo-fucoidan on liver cells is obscure. In this study, we investigate the effect of oligo-fucoidan in normal hepatocytes by transcriptomic analysis. Using an oligo-fucoidan oral gavage in wild-type adult zebrafish, we find that oligo-fucoidan pretreatment enhances the immune system and anti-viral genes in hepatocytes. Oligo-fucoidan pretreatment also decreases the expression of lipogenic enzymes and liver fibrosis genes. Using pathway analysis, we identify hepatocyte nuclear factor 4 alpha (HNF4A) to be the potential driver gene. We further investigate whether hepatocyte nuclear factor 4 alpha (HNF4A) could be induced by oligo-fucoidan and the underlying mechanism. Therefore, a normal hepatocyte clone 9 cell as an in vitro model was used. We demonstrate that oligo-fucoidan increases cell viability, Cyp3a4 activity, and Hnf4a expression in clone 9 cells. We further demonstrate that oligo-fucoidan might bind to asialoglycoprotein receptors (ASGPR) in normal hepatocytes through both in vitro and in vivo competition assays. This binding, consequently activating the signal transducer and activator of transcription 3 (STAT3), increases the expression of the P1 isoform of HNF4A. According to our data, we suggest that oligo-fucoidan not only enhances the gene expression associated with anti-viral ability and immunity, but also increases P1-HNF4A levels through ASGPR/STAT3 axis, resulting in protecting hepatocytes.

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37

Naiki, Takafumi, Masahito Nagaki, Takahiko Asano, Takayuki Kimata, and Hisataka Moriwaki. "Adenovirus-mediated hepatocyte nuclear factor-4α overexpression maintains liver phenotype in cultured rat hepatocytes." Biochemical and Biophysical Research Communications 335, no. 2 (September 2005): 496–500. http://dx.doi.org/10.1016/j.bbrc.2005.07.102.

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MACHIDA, Tomohisa, Masanori YASUDA, Michio SIMIZU, Norihide MOCHIZUKI, Kenji KAWAI, Hitoshi ITOH, Hiroshi KAJIWARA, Naoya NAKAMURA, and Yoshiyuki OSAMURA. "Immunocytochemical hepatocyte nuclear factor-1.BETA. expression in effusions." Journal of the Japanese Society of Clinical Cytology 49, no. 4 (2010): 242–47. http://dx.doi.org/10.5795/jjscc.49.242.

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39

Bellanné-Chantelot, Christine, Dominique Chauveau, Jean-François Gautier, Danièle Dubois-Laforgue, Séverine Clauin, Sandrine Beaufils, Jean-Marie Wilhelm, et al. "Clinical Spectrum Associated with Hepatocyte Nuclear Factor-1β Mutations." Annals of Internal Medicine 140, no. 7 (April 6, 2004): 510. http://dx.doi.org/10.7326/0003-4819-140-7-200404060-00009.

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40

Singh, Puja, Shu-Ping Tung, Eun Hee Han, In-Kyu Lee, and Young-In Chi. "Dimerization defective MODY mutations of hepatocyte nuclear factor 4α." Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis 814 (March 2019): 1–6. http://dx.doi.org/10.1016/j.mrfmmm.2019.01.002.

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41

Taraviras, Stavros, Gunther SchuTz, and Gavin Kelsey. "Generation of Inhibitory Mutants of Hepatocyte Nuclear Factor 4." European Journal of Biochemistry 244, no. 3 (March 15, 1997): 883–89. http://dx.doi.org/10.1111/j.1432-1033.1997.00883.x.

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Antkowiak, Mark, and Richard M. Green. "Telomeres, p53, Hepatocyte Nuclear Factor 4α, and Liver Disease." Hepatology 72, no. 4 (October 2020): 1166–68. http://dx.doi.org/10.1002/hep.31454.

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43

Kanazawa, T., A. Konno, Y. Hashimoto, and Y. Kon. "Expression of Hepatocyte Nuclear Factor 4α in Developing Mice." Anatomia, Histologia, Embryologia 38, no. 1 (February 2009): 34–41. http://dx.doi.org/10.1111/j.1439-0264.2008.00889.x.

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44

Lazarevich, N. L., and D. V. Alpern. "Hepatocyte nuclear factor 4 in epithelial development and carcinogenesis." Molecular Biology 42, no. 5 (October 2008): 699–709. http://dx.doi.org/10.1134/s0026893308050075.

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45

Green, Janelle, Dorit Naot, and Garth Cooper. "Hepatocyte nuclear factor 1 negatively regulates amylin gene expression." Biochemical and Biophysical Research Communications 310, no. 2 (October 2003): 464–69. http://dx.doi.org/10.1016/j.bbrc.2003.09.046.

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46

Yokoyama, Atsushi, Shogo Katsura, Ryo Ito, Waka Hashiba, Hiroki Sekine, Ryoji Fujiki, and Shigeaki Kato. "Multiple post-translational modifications in hepatocyte nuclear factor 4α." Biochemical and Biophysical Research Communications 410, no. 4 (July 2011): 749–53. http://dx.doi.org/10.1016/j.bbrc.2011.06.033.

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47

Cao, Henian, and Robert A. Hegele. "Human hepatocyte nuclear factor-1β (HNF1B) 1968A/G polymorphism." Journal of Human Genetics 45, no. 2 (March 2000): 98–99. http://dx.doi.org/10.1007/s100380050021.

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48

Chandra, Shubhra, Srilakshmi Srinivasan, and Jyotsna Batra. "Hepatocyte nuclear factor 1 beta: A perspective in cancer." Cancer Medicine 10, no. 5 (February 13, 2021): 1791–804. http://dx.doi.org/10.1002/cam4.3676.

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49

Liu, Hailing, Brett E. Jones, Cynthia Bradham, and Mark J. Czaja. "Increased cytochrome P-450 2E1 expression sensitizes hepatocytes to c-Jun-mediated cell death from TNF-α." American Journal of Physiology-Gastrointestinal and Liver Physiology 282, no. 2 (February 1, 2002): G257—G266. http://dx.doi.org/10.1152/ajpgi.00304.2001.

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The mechanisms underlying hepatocyte sensitization to tumor necrosis factor-α (TNF-α)-mediated cell death remain unclear. Increases in hepatocellular oxidant stress such as those that occur with hepatic overexpression of cytochrome P-450 2E1 (CYP2E1) may promote TNF-α death. TNF-α treatment of hepatocyte cell lines with differential CYP2E1 expression demonstrated that overexpression of CYP2E1 converted the hepatocyte TNF-α response from proliferation to apoptotic and necrotic cell death. Death occurred despite the presence of increased levels of nuclear factor-κB transcriptional activity and was associated with increased lipid peroxidation and GSH depletion. CYP2E1-overexpressing hepatocytes had increased basal and TNF-α-induced levels of c-Jun NH2-terminal kinase (JNK) activity, as well as prolonged JNK activation after TNF-α stimulation. Sensitization to TNF-α-induced cell death by CYP2E1 overexpression was inhibited by antioxidants or adenoviral expression of a dominant-negative c-Jun. Increased CYP2E1 expression sensitized hepatocytes to TNF-α toxicity mediated by c-Jun and overwhelming oxidative stress. The chronic increase in intracellular oxidant stress created by CYP2E1 overexpression may serve as a mechanism by which hepatocytes are sensitized to TNF-α toxicity in liver disease.

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50

Bingle, C. D., B. P. Hackett, M. Moxley, W. Longmore, and J. D. Gitlin. "Role of hepatocyte nuclear factor-3α and hepatocyte nuclear factor-3β in Clara cell secretory protein gene expression in the bronchiolar epithelium." Biochemical Journal 308, no. 1 (May 15, 1995): 197–202. http://dx.doi.org/10.1042/bj3080197.

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The 5′ flanking region of the Clara cell secretory protein (CCSP) gene contains two cis-acting elements which bind hepatocyte nuclear factor (HNF)-3 alpha and HNF-3 beta in vitro. To determine the role of these proteins in mediating CCSP gene expression in the bronchiolar epithelium, chimeric CCSP-reporter gene constructs containing various regions of the CCSP 5′ flanking region were co-transfected into H-441 cells with HNF-3 alpha or HNF-3 beta expression plasmids. These studies indicate that each of these transcription factors positively regulates CCSP gene expression and revealed that CCSP region I (-132 to -76) is sufficient to mediate this effect. Gel-mobility-shift assays with oligonucleotides corresponding to CCSP region I, nuclear extract from bronchiolar epithelial cells and HNF-3-specific antibodies indicate that HNF-3 alpha and HNF-3 beta are the only proteins in bronchiolar epithelial cells which directly interact with this region. Consistent with these observations, HNF-3 alpha and HNF-3 beta transcripts were found to be enriched in this cell population and in situ hybridization of adult lung revealed HNF-3 gene expression in non-ciliated bronchiolar epithelial cells expressing the CCSP gene. Finally, experiments with CCSP region I and a heterologous promoter indicate that this region acts in a promoter-specific context, suggesting that additional factors interacting via the minimal CCSP promoter region are essential in determining the effects of HNF-3 on cell-specific CCSP gene expression in the bronchiolar epithelium.

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