Protein NO52—a constitutive nucleolar component sharing high sequence homologies to protein NO66

Eilbracht, Jens; Kneissel, Sandra; Hofmann, Astrid; Schmidt-Zachmann, Marion S.

doi:10.1016/j.ejcb.2004.12.022

Cited by 45 publications

(57 citation statements)

References 77 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A lung cancer-associated mineral dust-induced gene, mdig, has been previously identified and found to be able to foster proliferation of human bronchial epithelial cells. 2 This gene had also been independently identified in human promyelocytic leukemia HL60 cells as the myc-induced nuclear antigen 53 (mina53) and Xenopus laevis as nucleolar protein 52 (NO52), 3,4 respectively. However, it remains unclear how mdig gene regulates cell growth or proliferation that contributes to the development of lung cancer.…”

Section: Introductionmentioning

confidence: 99%

Lung cancer-associated JmjC domain protein mdig suppresses formation of tri-methyl lysine 9 of histone H3

Chang

Zhang

et al. 2009

Cell Cycle

View full text Add to dashboard Cite

Lung cancer is the most common cancer worldwide, accounting for 1.3 million cancer deaths annually. Despite extensive studies over the past decade, the detailed mechanism about the initiation and development of the lung cancer is still elusive. In the present report, we showed that overexpression of mdig is a common feature of the non-small cell lung cancer. Gene silencing or overexpression of mdig revealed that mdig is involved in demethylation of tri-methyl lysine 9 on histone H3, leading to an increase in ribosomal RNA expression. The transcriptional regulation of ribosomal RNA gene by mdig is achieved through abrogating tri-methyl lysine 9 on histone H3 and enhancing RNA polymerase I occupancy in the promoter region of the ribosomal RNA gene as demonstrated by chromatin immunoprecipitation. The pronounced expression of mdig in lung cancer tissues but not normal lung tissues, thus, suggests that mdig possesses oncogenic property through antagonizing tri-methyl lysine 9 on histone H3 and promoting ribosomal RNA synthesis.

show abstract

Section: Introductionmentioning

confidence: 99%

Lung cancer-associated JmjC domain protein mdig suppresses formation of tri-methyl lysine 9 of histone H3

Chang

Zhang

et al. 2009

Cell Cycle

View full text Add to dashboard Cite

show abstract

“…It is suggested that oxygenases also catalyze demethylation of N-ε-methyllysine histone residues (JmjC demethylases) (14) and lysyl 5-hydroxylation of splicing-related proteins (JMJD6) (15). Mdig/mina53 interacts with various ribosomal proteins and is involved in ribosome biogenesis (6) and ribosomal RNA transcription (12). It was confirmed…”

Section: Hydroxylation Of Ribosomal Proteinmentioning

confidence: 65%

“…It was later confirmed to be the same gene as the myc-induced nuclear antigen with an estimated molecular weight of 53 kDa (mina53) (5) and also the nuclear protein 52 (NO52) (6). Mdig/mina53 is located on chromosome 3 within a single open reading frame of 465 amino acids (4,5), and chiefly expressed in the cellular nuclei with part of the protein condensed in the nucleolus (5)(6)(7). However, the intracellular distribution of Mdig/mina53 may vary with cell cycle phases and different extracellular environments (8).…”

mentioning

confidence: 97%

“…Mineral dust-induced gene (Mdig ) is a lung cancer-related gene found in alveolar macrophages from coal miners exposed to mineral dusts in 2005 (4). It was later confirmed to be the same gene as the myc-induced nuclear antigen with an estimated molecular weight of 53 kDa (mina53) (5) and also the nuclear protein 52 (NO52) (6). Mdig/mina53 is located on chromosome 3 within a single open reading frame of 465 amino acids (4,5), and chiefly expressed in the cellular nuclei with part of the protein condensed in the nucleolus (5)(6)(7).…”

mentioning

confidence: 98%

See 1 more Smart Citation

From biological mechanisms to clinical implications: the role of mineral dust-induced gene in lung cancers

Zhang

Zhao

2017

J. Thorac. Dis.

View full text Add to dashboard Cite

“…Conditional knockdown revealed that depletion of FTSJ3 affects cell proliferation and causes pre-rRNA processing defects (43). Mina53 is involved in cell division (44) and is directly involved in ribosome biogenesis, most likely during the assembly process of pre-ribosomal particles (45). It may be important in cell growth and survival.…”

Section: Discussionmentioning

confidence: 99%

BMI-1 is important in bufalin-induced apoptosis of K562 cells

Lian

Wang

Wei

et al. 2014

Molecular Medicine Reports

View full text Add to dashboard Cite

Abstract. The purpose of this study was to analyze the effects of bufalin on the gene expression of K562 cells and on the expression of BMI-1 pathway constituents in K562 cell apoptosis. K562 cells were treated with bufalin, and the inhibition rate and apoptosis were detected by an MTT assay, flow cytometry and a microarray assay. BMI-1, p16 INK4a and p14 ARF were examined by quantitative polymerase chain reaction (qPCR). Bufalin induced significant changes in the gene expression of the K562 cells; 4296 genes were differentially expressed, 2185 were upregulated and 2111 were downregulated. The most upregulated genes were associated with transcription regulation, while the most downregulated genes were associated with the non-coding RNA metabolic processes and DNA repair. qPCR analysis demonstrated that BMI-1 was overexpressed in the K562 cells. Bufalin is able to downregulate BMI-1 expression levels in K562 cells prematurely and cause an increase in the expression levels of p16 INK4a and p14 ARF . Moreover, bufalin downregulated BCR/ABL expression levels in a time-dependent manner, and the expression of BCR/ABL was not associated with the upregulation or downregulation of BMI-1 expression. Bufalin may induce K562 cell apoptosis by downregulating BMI-1 expression levels and accordingly upregulating the expression levels of p16 INK4a and p14 ARF . Bufalin may also induce K562 cell apoptosis via downregulating BCR/ABL expression levels, and this pathway may be independent of the BMI-1 pathway.

show abstract

Protein NO52—a constitutive nucleolar component sharing high sequence homologies to protein NO66

Cited by 45 publications

References 77 publications

Lung cancer-associated JmjC domain protein mdig suppresses formation of tri-methyl lysine 9 of histone H3

Lung cancer-associated JmjC domain protein mdig suppresses formation of tri-methyl lysine 9 of histone H3

From biological mechanisms to clinical implications: the role of mineral dust-induced gene in lung cancers

BMI-1 is important in bufalin-induced apoptosis of K562 cells

Contact Info

Product

Resources

About