UHRF1 mediates cell migration and invasion of gastric cancer

Gastric cancer (GC) is a common highly aggressive malignant tumor in worldwide. Ubiquitin-like with PHD and ring-finger protein 1 (UHRF1) has a key role in several kinds of cancers development. However, the biology effect of UHRF1 on the tumorigenesis of GC remains unclear. In this research, the role of UHRF1 in the growth, migration, invasion and apoptosis and the underlying mechanisms were investigated in MGC803 and SGC7901 cells. The UHRF1 knockdown MGC803 and SGC7901 cell lines were used to investigate the roles of UHRF1 on GC cell growth, migration, invasion and apoptosis. The growth, migration and invasion rate of UHRF1 knockdown cells was lower than that of the control. Moreover, ROS generation and caspase-3/caspase-9 activities increased in UHRF1 knockdown cells. And mitochondrial membrane potential decreased in UHRF1 knockdown cells. These findings indicated that UHRF1 promoted the growth, migration and invasion of MGC803 and SGC7901 cells and inhibited apoptosis via a ROS-associated pathway.

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Clinical and experimental role of ring finger protein 180 on lymph node metastasis and survival in gastric cancer

British Journal of Surgery ◽

10.1002/bjs.10066 ◽

2016 ◽

Vol 103 (4) ◽

pp. 407-416 ◽

Cited By ~ 8

Author(s):

J. Deng ◽

H. Liang ◽

R. Zhang ◽

Y. Hou ◽

Y. Liu ◽

...

Keyword(s):

Gastric Cancer ◽

Lymph Node ◽

Lymph Node Metastasis ◽

Ring Finger ◽

Ring Finger Protein ◽

Node Metastasis ◽

Finger Protein

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Overexpression of RING Finger Protein 126 is Associated with Poor Prognosis and Contributes to the Progression of Lung Adenocarcinoma

10.21203/rs.3.rs-117735/v1 ◽

2020 ◽

Author(s):

Zhaona Sun ◽

Meiyuan Chen ◽

Ziping Li ◽

Hong Zhang

Keyword(s):

Lung Adenocarcinoma ◽

Expression Pattern ◽

Poor Prognosis ◽

Ring Finger ◽

High Expression ◽

Normal Lung ◽

Migration And Invasion ◽

Ring Finger Protein ◽

Finger Protein

Abstract BackgroundMore recently, E3 ubiquitin ligases are well-informed to be involved in tumor development, and genetic aberration of this family have been implicated in breast cancer and oral cancer. RING finger protein 126 (RNF126), a newly uncovered E3 ubiquitin ligase, targets multiple proteins to promote their degradation. This study aims to explore the expression pattern and functional role of RNF126 in lung adenocarcinoma (LAD). MethodsImmunohistochemical staining and real-time PCR were used to evaluate the expression pattern of RNF126 in normal lung tissue and LAD tissues. Western blot, cell proliferation and invasion assays were performed to investigate role of RNF126 in modulating LAD progression. Statistical analyses including Chi-square test, Kaplan-Meier test, Cox regression test, and Student’s t-test were conducted for both clinical and experimental data.ResultsWe find that both the mRNA and protein expression levels of RNF126 are elevated in LAD tissues, and its expression correlates with clinicopathologic features including tumor size and TNM stage. High expression of RNF126 indicates a poor prognosis of LAD patients. Gene perturbations reveal that RNF126 promotes LAD cells proliferation and xenograft growth. However, RNF126 exerts no significant effect on cell migration and invasion in LAD cells. ConclusionsOur clinical and cellular data suggest that targeting this molecule could potentially provide advantages for LAD patients with high expression of RNF126.

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Role of a novel pathogen-induced pepper C3–H–C4 type RING-finger protein gene, CaRFP1, in disease susceptibility and osmotic stress tolerance

Plant Molecular Biology ◽

10.1007/s11103-006-9110-2 ◽

2006 ◽

Vol 63 (4) ◽

pp. 571-588 ◽

Cited By ~ 41

Author(s):

Jeum Kyu Hong ◽

Hyong Woo Choi ◽

In Sun Hwang ◽

Byung Kook Hwang

Keyword(s):

Osmotic Stress ◽

Stress Tolerance ◽

Disease Susceptibility ◽

Protein Gene ◽

Ring Finger ◽

Ring Finger Protein ◽

Osmotic Stress Tolerance ◽

Finger Protein

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Circulating methylated Septin 9 and ring finger protein 180 for noninvasive diagnosis of early gastric cancer

Translational Cancer Research ◽

10.21037/tcr-20-1330 ◽

2020 ◽

Vol 9 (11) ◽

pp. 7012-7021

Author(s):

Chang-Qi Cao ◽

Lin Chang ◽

Qi Wu

Keyword(s):

Gastric Cancer ◽

Early Gastric Cancer ◽

Ring Finger ◽

Noninvasive Diagnosis ◽

Ring Finger Protein ◽

Septin 9 ◽

Finger Protein

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Arkadia (RING Finger Protein 111) Mediates Sumoylation-Dependent Stabilization of Nrf2 Through K48-Linked Ubiquitination

Cellular Physiology and Biochemistry ◽

10.1159/000488475 ◽

2018 ◽

Vol 46 (1) ◽

pp. 418-430 ◽

Cited By ~ 5

Author(s):

Deneshia J. McIntosh ◽

Treniqka S. Walters ◽

Ifeanyi J. Arinze ◽

Jamaine Davis

Keyword(s):

Gene Transcription ◽

Ring Finger ◽

Nuclear Body ◽

Promyelocytic Leukemia ◽

Heme Oxygenase 1 ◽

Ring Finger Protein ◽

Whole Cell ◽

Cell Lysates ◽

Finger Protein

Background/Aims: The transcription factor Nrf2 is a master regulator of the antioxidant defense system, protecting cells from oxidative damage. We previously reported that the SUMO-targeted E3 ubiquitin ligase (STUbL), RING finger protein 4 (RNF4) accelerated the degradation rate of Nrf2 in promyelocytic leukemia-nuclear body (PML-NB)-enriched fractions and decreased Nrf2-mediated gene transcription. The mechanisms that regulate Nrf2 nuclear levels are poorly understood. In this study, we aim to explore the role of the second mammalian STUbL, Arkadia/RNF111 on Nrf2. Methods: Arkadia mediated ubiquitination was detected using co-immunoprecipitation assays in which whole cell lysates were immunoprecipated with anti-Nrf2 antibody and Western blotted with anti-hemagglutinin (HA) antibody or anti-Lys-48 ubiquitin-specific antibody. The half-life of Nrf2 was detected in whole cell lysates and promyelocytic leukemia-nuclear body enriched fractions by cycloheximide-chase. Reporter gene assays were performed using the antioxidant response element (ARE)-containing promoter Heme oxygenase-1 (HO-1). Results: We show that Arkadia/RNF111 is able to ubiquitinate Nrf2 resulting in the stabilization of Nrf2. This stabilization was mediated through Lys-48 ubiquitin chains, contrary to traditionally degradative role of Lys-48 ubiquitination, suggesting that Lys-48 ubiquitination of Nrf2 protects Nrf2 from degradation thereby allowing Nrf2-dependent gene transcription. Conclusion: Collectively, these findings highlight a novel mechanism to positively regulate nuclear Nrf2 levels in response to oxidative stress through Arkadia-mediated K48-linked ubiquitination of Nrf2.

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