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Relevant bibliographies by topics / Proteine i-mfa

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Academic literature on the topic 'Proteine i-mfa'

Author: Grafiati

Published: 4 June 2021

Last updated: 12 February 2022

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Journal articles on the topic "Proteine i-mfa"

1

Kusano, Shuichi, and Nancy Raab-Traub. "I-mfa Domain Proteins Interact with Axin and Affect Its Regulation of the Wnt and c-Jun N-Terminal Kinase Signaling Pathways." Molecular and Cellular Biology 22, no. 18 (2002): 6393–405. http://dx.doi.org/10.1128/mcb.22.18.6393-6405.2002.

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ABSTRACT I-mfa has been identified as an inhibitor of myogenic basic helix-loop-helix transcription factors, and a related human I-mfa domain-containing protein (HIC) also has been identified as a protein that regulates Tat- and Tax-mediated expression of viral promoters. HIC and I-mfa represent a family of proteins that share a highly conserved cysteine-rich domain, termed the I-mfa domain. We show here that both I-mfa domain proteins, HIC and I-mfa, interacted in vivo with the Axin complex through their C-terminal I-mfa domains. This interaction inhibited Axin-mediated downregulation of free levels of cytosolic β-catenin. I-mfa and HIC also both directly interacted with lymphocyte enhancer factor (LEF); however, I-mfa but not HIC significantly inhibited reporter constructs regulated by β-catenin. The overexpression of HIC but not I-mfa decreased the inhibitory effects of Axin on β-catenin-regulated reporter constructs, while both HIC and I-mfa decreased Axin-mediated c-Jun N-terminal kinase (JNK) activation. These data reveal for the first time that I-mfa domain proteins interact with the Axin complex and affect Axin regulation of both the Wnt and the JNK activation pathways. Interestingly, HIC differs from I-mfa in that I-mfa affects both Axin function and T-cell factor- or LEF-regulated transcription in the Wnt signaling pathway while HIC affects primarily Axin function.

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2

Shotorbani, Parisa Yazdizadeh, Sarika Chaudhari, Yu Tao, Leonidas Tsiokas, and Rong Ma. "Inhibitor of myogenic differentiation family isoform a, a new positive regulator of fibronectin production by glomerular mesangial cells." American Journal of Physiology-Renal Physiology 318, no. 3 (2020): F673—F682. http://dx.doi.org/10.1152/ajprenal.00508.2019.

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Overproduction of extracellular matrix proteins, including fibronectin by mesangial cells (MCs), contributes to diabetic nephropathy. Inhibitor of myogenic differentiation family isoform a (I-mfa) is a multifunctional cytosolic protein functioning as a transcriptional modulator or plasma channel protein regulator. However, its renal effects are unknown. The present study was conducted to determine whether I-mfa regulated fibronectin production by glomerular MCs. In human MCs, overexpression of I-mfa significantly increased fibronectin abundance. Silencing I-mfa significantly reduced the level of fibronectin mRNA and blunted transforming growth factor-β1-stimulated production of fibronectin. We further found that high glucose increased I-mfa protein content in a time course (≥48 h) and concentration (≥25 mM)-dependent manner. Although high glucose exposure increased I-mfa at the protein level, it did not significantly alter transcripts of I-mfa in MCs. Furthermore, the abundance of I-mfa protein was significantly increased in the renal cortex of rats with diabetic nephropathy. The I-mfa protein level was also elevated in the glomerulus of mice with diabetic kidney disease. However, there was no significant difference in glomerular I-mfa mRNA levels between mice with and without diabetic nephropathy. Moreover, H2O2 significantly increased I-mfa protein abundance in a dose-dependent manner in cultured human MCs. The antioxidants polyethylene glycol-catalase, ammonium pyrrolidithiocarbamate, and N-acetylcysteine significantly blocked the high glucose-induced increase of I-mfa protein. Taken together, our results suggest that I-mfa, increased by high glucose/diabetes through the production of reactive oxygen species, stimulates fibronectin production by MCs.

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3

Snider, Lauren, Hilary Thirlwell, Jeffrey R. Miller, Randall T. Moon, Mark Groudine, and Stephen J. Tapscott. "Inhibition of Tcf3 Binding by I-mfa Domain Proteins." Molecular and Cellular Biology 21, no. 5 (2001): 1866–73. http://dx.doi.org/10.1128/mcb.21.5.1866-1873.2001.

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ABSTRACT We have determined that I-mfa, an inhibitor of several basic helix-loop-helix (bHLH) proteins, and XIC, a Xenopusortholog of human I-mf domain-containing protein that shares a highly conserved cysteine-rich C-terminal domain with I-mfa, inhibit the activity and DNA binding of the HMG box transcription factor XTcf3. Ectopic expression of I-mfa or XIC in early Xenopus embryos inhibited dorsal axis specification, the expression of the Tcf3/β-catenin-regulated genessiamois and Xnr3, and the ability of β-catenin to activate reporter constructs driven by Lef/Tcf binding sites. I-mfa domain proteins can regulate both the Wnt signaling pathway and a subset of bHLH proteins, possibly coordinating the activities of these two critical developmental pathways.

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4

Young, Tara M., Qi Wang, Tsafi Pe'ery, and Michael B. Mathews. "The Human I-mfa Domain-Containing Protein, HIC, Interacts with Cyclin T1 and Modulates P-TEFb-Dependent Transcription." Molecular and Cellular Biology 23, no. 18 (2003): 6373–84. http://dx.doi.org/10.1128/mcb.23.18.6373-6384.2003.

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ABSTRACT Positive transcription elongation factor b (P-TEFb) hyperphosphorylates the carboxy-terminal domain of RNA polymerase II, permitting productive transcriptional elongation. The cyclin T1 subunit of P-TEFb engages cellular transcription factors as well as the human immunodeficiency virus type 1 (HIV-1) transactivator Tat. To identify potential P-TEFb regulators, we conducted a yeast two-hybrid screen with cyclin T1 as bait. Among the proteins isolated was the human I-mfa domain-containing protein (HIC). HIC has been reported to modulate expression from both cellular and viral promoters via its C-terminal cysteine-rich domain, which is similar to the inhibitor of MyoD family a (I-mfa) protein. We show that HIC binds cyclin T1 in yeast and mammalian cells and that it interacts with intact P-TEFb in mammalian cell extracts. The interaction involves the I-mfa domain of HIC and the regulatory histidine-rich region of cyclin T1. HIC also binds Tat via its I-mfa domain, although the sequence requirements are different. HIC colocalizes with cyclin T1 in nuclear speckle regions and with Tat in the nucleolus. Expression of the HIC cDNA modulates Tat transactivation of the HIV-1 long terminal repeat (LTR) in a cell type-specific fashion. It is mildly inhibitory in CEM cells but stimulates gene expression in HeLa, COS, and NIH 3T3 cells. The isolated I-mfa domain acts as a dominant negative inhibitor. Activation of the HIV-1 LTR by HIC in NIH 3T3 cells occurs at the RNA level and is mediated by direct interactions with P-TEFb.

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5

Xu, Bing, Huijuan Dong, Feili Chen, Yong Zhou, Jiabao Liang, and Shuyun Zhou. "The Expression of I-Mfa in Adult Patients with De Novo Acute Myeloid Leukemia and Its Clinical Significance." Blood 124, no. 21 (2014): 5316. http://dx.doi.org/10.1182/blood.v124.21.5316.5316.

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Abstract Background: I-mfa has been identified as an inhibitor of MyoD and other related myogenic basic helix-loop-helix proteins. I-mfa contains a cysteine-rich C-terminal domain, and has been reported to function as transcriptional regulator of different pathways including Wnt signaling, c-jun N-terminal kinase signaling, and the regulatory properties of I-mfa depend on the C-terminal domain. Furthermore, recent studies have found that the I-mfa domain may have a close correlation with the development of myeloid neoplasms, however the role of I-mfa in adult patients with de novo acute myeloid leukemia still remain unclear. Aims: The aim of this study was to determine I-mfa expression in adult patients with de novo acute myeloid leukemia and its clinical significance. Methods: BM samples form 110 adult patients with de novo AML were analyzed. Of the 110 AML patients, 66 were males and 44 were females, with a mean age of 32 years( range from 12 to 77 years). Among them, 1 out of 110 patients was M1, 49 were M2, 14 were M4, 28 were M5, 1was M6 and 17 were acute unclassified leukemia. All patients received 1 to 2 cycles of induction of standard-dose cytarabine continuous infusion×7 days with idarubicin or daunorubicin×3days, fellowed by consolidation therapy with HiDAC and then stem cell transplantation according to patient’s condition. Real-time reverse transcription-polymerase chain reaction(RT-PCR) was used to detect the expression of I-mfa gene in 110 de novo adult AML patients, and the patients were divided into high and low I-mfa expression groups accordint to the median expression of I-mfa mRNA. Comparisons were performed using Mann-Whitney U test, Chi-square test and Kaplan-Meier method. Results:Distribution of I-mfa gene expression in different FAB subtypes was with no significant differences (P=0.169). The median age of AML pateints in low and high I-mfa gene epxression groups were 35 and 40 years old(P=0.162), and the median expression of I-mfa in 44 female patients and 66 male patients was 0.018 and 0.013 separately(P=0.728). What’s more, there was no significant difference of WBC, Hb level, PLT, bone marrow blast counts between the two groups (P＞0.05), and the I-mfa expression level was also not correlated with chromosome risk stratification and the expression of CD34 (P＞0.05). High I-mfa expression group had a lower complete remission rate than that in the low expression group (81.8% vs 63.6%, P=0.032), However, the overall survival rate was with no significant difference in the low and hign I-mfa gene expression groups(76.4% vs 76.4%, P=0.471). Conclusions: Our results showed high I-mfa expression correlates with a poor treatment response, the OS rate was with no significant difference in the two groups. There is somewhat correlation between the expression level of I-mfa gene and prognosis and the expression of I-mfa may be a prognostic factor for adult patients with de novo acute myeloid leukemia. Disclosures No relevant conflicts of interest to declare.

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6

Mizugishi, Kiyomi, Minoru Hatayama, Takahide Tohmonda, et al. "Myogenic repressor I-mfa interferes with the function of Zic family proteins." Biochemical and Biophysical Research Communications 320, no. 1 (2004): 233–40. http://dx.doi.org/10.1016/j.bbrc.2004.05.158.

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7

Reiss-Sklan, Ella, Alexander Levitzki, and Tally Naveh-Many. "The Complex Regulation of HIC (Human I-mfa Domain Containing Protein) Expression." PLoS ONE 4, no. 7 (2009): e6152. http://dx.doi.org/10.1371/journal.pone.0006152.

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8

Kusano, Shuichi, Yuki Shiimura, and Yoshito Eizuru. "I-mfa domain proteins specifically interact with SERTA domain proteins and repress their transactivating functions." Biochimie 93, no. 9 (2011): 1555–64. http://dx.doi.org/10.1016/j.biochi.2011.05.016.

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9

Kusano, Shuichi, Makoto Yoshimitsu, Miho Hachiman, and Masanori Ikeda. "I-mfa domain proteins specifically interact with HTLV-1 Tax and repress its transactivating functions." Virology 486 (December 2015): 219–27. http://dx.doi.org/10.1016/j.virol.2015.09.020.

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10

Thébault, Sabine, Jihane Basbous, Bernard Gay, Christian Devaux, and Jean-Michel Mesnard. "Sequence requirement for the nucleolar localization of human I-mfa domain-containing protein (HIC p40)." European Journal of Cell Biology 79, no. 11 (2000): 834–38. http://dx.doi.org/10.1078/0171-9335-00111.

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Dissertations / Theses on the topic "Proteine i-mfa"

1

Thebault, Sabine. "Caractérisation d'une nouvelle protéine humaine contenant un domaine homologue à l'I-mfa : implication dans la régulation de l'expression de deux rétrovirus humains, HTLV-I et HIV-1." Montpellier 1, 2000. http://www.theses.fr/2000MON1T013.

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2

Chen, Chao-Min Amy. "Identification and characterization of I-mf, a novel myogenic repressor that interacts with MyoD family members /." Thesis, Connect to this title online; UW restricted, 1996. http://hdl.handle.net/1773/5060.

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