Identification and Characterization of the Cis-Elements Regulating the Rat AMOG (Adhesion Molecule on Glia)/Na,K-ATPase β2 Subunit Gene1

Kawakami, Kiyoshi; Suzuki-Yagawa, Y; Watanabe, Yuko; Nagano, Kenichi

doi:10.1093/oxfordjournals.jbchem.a123789

Cited by 14 publications

(6 citation statements)

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“…Sequence analysis revealed a potential TATA box (−29 bp); two Sp1 binding sites (−55 and −147 bp) and a serum response element (SRE: −263 bp) on the rat Atp1b2 promoter region (Kawakami et al, 1990 ). In addition, an AMOG regulatory element (AMRE: GAGGCGGGG at position −87 to −79 bp) and a functional Sp1 binding site (−147 to −142 bp) were found in rat Atp1b2 promoter regions (Kawakami et al, 1992 , 1993 ).…”

Section: Promoter Analysis Of Nak-atpase α- and β-Subunitsmentioning

confidence: 99%

Transcriptional regulators of Na,K-ATPase subunits

Langhans

2015

Front. Cell Dev. Biol.

101

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The Na,K-ATPase classically serves as an ion pump creating an electrochemical gradient across the plasma membrane that is essential for transepithelial transport, nutrient uptake and membrane potential. In addition, Na,K-ATPase also functions as a receptor, a signal transducer and a cell adhesion molecule. With such diverse roles, it is understandable that the Na,K-ATPase subunits, the catalytic α-subunit, the β-subunit and the FXYD proteins, are controlled extensively during development and to accommodate physiological needs. The spatial and temporal expression of Na,K-ATPase is partially regulated at the transcriptional level. Numerous transcription factors, hormones, growth factors, lipids, and extracellular stimuli modulate the transcription of the Na,K-ATPase subunits. Moreover, epigenetic mechanisms also contribute to the regulation of Na,K-ATPase expression. With the ever growing knowledge about diseases associated with the malfunction of Na,K-ATPase, this review aims at summarizing the best-characterized transcription regulators that modulate Na,K-ATPase subunit levels. As abnormal expression of Na,K-ATPase subunits has been observed in many carcinoma, we will also discuss transcription factors that are associated with epithelial-mesenchymal transition, a crucial step in the progression of many tumors to malignant disease.

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Section: Promoter Analysis Of Nak-atpase α- and β-Subunitsmentioning

confidence: 99%

Transcriptional regulators of Na,K-ATPase subunits

Langhans

2015

Front. Cell Dev. Biol.

101

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“…To reveal the molecular mechanisms of the tissue-specific, developmental, and hormonal regulation of Na,K-ATPase gene expression and of the coordinated regulation between the a-and 13-subunit genes, we have performed a systematic analysis of the genes encoding a-and 13-subunit isoforms, including their 5'-flanking regions where important regulatory functions reside (15,17,18,43). We cloned from the rat chromosome a 13.3-kb DNA fragment that included the Na,K-ATPase al subunit gene (ATPlA1) and 5' flanking region (EMBL/GenBank data library accession number X51461), and identified the transcription initiation site at 262 bp upstream from the translation initiation codon (43).…”

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confidence: 99%

“…CAT activity was assayed as described previously (10,17). The acetylated chloramphenicol was separated by thin-layer chromatography and analyzed by a radioanalytic imaging system (AMBIS System, Inc., San Diego, Calif.).…”

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confidence: 99%

Housekeeping Na,K-ATPase alpha 1 subunit gene promoter is composed of multiple cis elements to which common and cell type-specific factors bind.

Suzuki-Yagawa¹,

Kawakami²,

Nagano³

1992

Mol. Cell. Biol.

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Na,K-ATPase al subunit gene (ATPlA1) is one of the housekeeping genes involved in homeostasis of Na+ and K+ in all animal cells. We identified and characterized the cis-acting elements that regulate the expression of ATPAL1. The region between -155 and -49 was determined as a positive regulatory region in five cultured cell lines of different tissue origins (MDCK, B103, L6, 3Y1, and HepG2). The region was divided into three subregions: from -120 to -106 (including the Spl binding site), from -102 to -61, and from -58 to -49 (including an Spl consensus sequence). Cell type-specific factors binding to the middle subregion (from -102 to -61) were detected by gel retardation analysis, using nuclear extracts prepared from MDCK and B103 cells. Two gel retardation complexes were formed in the B103 nuclear extract, and three were formed in the MDCK nuclear extract. DNA binding regions of these factors were located at -88 to -69 and differed from each other in DNase I footprinting experiments. These factors also showed different binding characteristics in gel retardation competition and methylation interference experiments. The identified cis element was named the ATPL1A regulatory element. The core sequence of this element is found in several other genes involved in cellular energy metabolism, suggesting that the sequence is a common regulatory element responsive to the state of energy metabolism.

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“…The transcription factor specificity protein 1 (Sp1) binds GC-rich motifs and regulates gene expression through protein–protein interactions (Shull et al, 1989 ; Samson and Wong, 2002 ). Based on previous works by Kawakami et al ( 1990 , 1992 ) and Avila et al ( 1998 ) that reported that Sp1 enhances the promoter activity of the β 2 subunit in rat neuroblastoma, in rat embryo cell lines and in human lymphocytes, we suspected that Sp1 could be at least one of the factors regulating this process. Therefore, we explored whether Sp1 was involved in the up-regulation of the β 2 subunit during the re-morphogenesis of ARPE-19 cells.…”

Section: Resultsmentioning

confidence: 91%

The Apical Localization of Na+, K+-ATPase in Cultured Human Retinal Pigment Epithelial Cells Depends on Expression of the β2 Subunit

et al. 2016

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Na+, K+-ATPase, or the Na+ pump, is a key component in the maintenance of the epithelial phenotype. In most epithelia, the pump is located in the basolateral domain. Studies from our laboratory have shown that the β1 subunit of Na+, K+-ATPase plays an important role in this mechanism because homotypic β1-β1 interactions between neighboring cells stabilize the pump in the lateral membrane. However, in the retinal pigment epithelium (RPE), the Na+ pump is located in the apical domain. The mechanism of polarization in this epithelium is unclear. We hypothesized that the apical polarization of the pump in RPE cells depends on the expression of its β2 subunit. ARPE-19 cells cultured for up to 8 weeks on inserts did not polarize, and Na+, K+-ATPase was expressed in the basolateral membrane. In the presence of insulin, transferrin and selenic acid (ITS), ARPE-19 cells cultured for 4 weeks acquired an RPE phenotype, and the Na+ pump was visible in the apical domain. Under these conditions, Western blot analysis was employed to detect the β2 isoform and immunofluorescence analysis revealed an apparent apical distribution of the β2 subunit. qPCR results showed a time-dependent increase in the level of β2 isoform mRNA, suggesting regulation at the transcriptional level. Moreover, silencing the expression of the β2 isoform in ARPE-19 cells resulted in a decrease in the apical localization of the pump, as assessed by the mislocalization of the α2 subunit in that domain. Our results demonstrate that the apical polarization of Na+, K+-ATPase in RPE cells depends on the expression of the β2 subunit.

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Identification and Characterization of the Cis-Elements Regulating the Rat AMOG (Adhesion Molecule on Glia)/Na,K-ATPase β2 Subunit Gene1

Cited by 14 publications

References 0 publications

Transcriptional regulators of Na,K-ATPase subunits

Transcriptional regulators of Na,K-ATPase subunits

Housekeeping Na,K-ATPase alpha 1 subunit gene promoter is composed of multiple cis elements to which common and cell type-specific factors bind.

The Apical Localization of Na+, K+-ATPase in Cultured Human Retinal Pigment Epithelial Cells Depends on Expression of the β2 Subunit

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