Nucleotide sequence of cDNA for human aldose reductase

Graham, Alexander; Hedge, Philip; Powell, Stephen Joseph; Riley, John; Brown, LC; Gammack, A.; Carey, Frank; Markham, Alexander F.

doi:10.1093/nar/17.20.8368

Cited by 31 publications

(13 citation statements)

References 2 publications

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“…The complex pattern obtained when a mouse genomic DNA Southern blot was hybridized with the mAR cDNA compared with the single band observed with the intron-2-specific probe confirms previous results obtained for human (29) and rat (18) genomes concerning the existence of AR pseudogenes.…”

Section: Discussionsupporting

confidence: 87%

Isolation of the Mouse Aldose Reductase Promoter and Identification of a Tonicity-responsive Element

Daoudal

Tournaire

Halere

et al. 1997

Journal of Biological Chemistry

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Aldose reductase (AR; EC 1.1.1.21) is an oxidoreductase that catalyzes the NADPH-dependent conversion of glucose to sorbitol, the first step of the polyol pathway. AR is of great interest due to its implication in the etiology of diabetic complications. In renal medullary cells, AR also plays an osmoregulatory role by accumulating sorbitol to maintain the intracellular osmotic balance during antidiuresis. We have previously cloned the AR cDNA from mouse kidney, and we report here the isolation of the mouse AR gene promoter. Transient transfection of chloramphenicol acetyltransferase reporter constructs containing various 5-flanking regions of the mouse AR gene in CV1 cells led to the identification of a sequence spanning base pairs ؊1053 to ؊1040, required for an enhancer activity in hypertonic compared with isotonic cell culture conditions. This sequence is similar to the tonicity-responsive element first characterized in the betaine-␥-aminobutyric acid transporter promoter.

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Section: Discussionsupporting

confidence: 87%

Isolation of the Mouse Aldose Reductase Promoter and Identification of a Tonicity-responsive Element

Daoudal

Tournaire

Halere

et al. 1997

Journal of Biological Chemistry

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“…Cells were harvested after 12, 24, and 36 h, and RNA was extracted for Northern blot analysis as described under "Materials and Methods." AR gene using AR cDNA as a probe in the secondary screening and by comparing part of their sequences with published data (29,30). One of the two clones (AR5) was found to span Ϫ15 to ϩ4 kb relative to the transcription start site of the AR gene.…”

Section: Resultsmentioning

confidence: 98%

Identification and Characterization of Multiple Osmotic Response Sequences in the Human Aldose Reductase Gene

Ko¹,

Ruepp²,

Bohren³

et al. 1997

Journal of Biological Chemistry

195

133

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Aldose reductase (AR) has been implicated in osmoregulation in the kidney because it reduces glucose to sorbitol, which can serve as an osmolite. Under hyperosmotic stress, transcription of this gene is induced to increase the enzyme level. This mode of osmotic regulation of AR gene expression has been observed in a number of nonrenal cells as well, suggesting that this is a common response to hyperosmotic stress. We have identified a 132-base pair sequence ϳ1 kilobase pairs upstream of the transcription start site of the AR gene that enhances the transcription activity of the AR promoter as well as that of the SV40 promoter when the cells are under hyperosmotic stress. Within this 132-base pair sequence, there are three sequences that resemble TonE, the tonicity response element of the canine betaine transporter gene, and the osmotic response element of the rabbit AR gene, suggesting that the mechanism of osmotic regulation of gene expression in these animals is similar. However, our data indicate that cooperative interaction among the three TonE-like sequences in the human AR may be necessary for their enhancer function.

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“…Recently, the human AR (hAR) and ratAR genes were cloned (16,17), and the hAR promoter region was carefully characterized (18). This last study also briefly examined the promoter region and a DNA fragment encompassing about 4.2 kilobases (kb) upstream for the presence of osmotic response.…”

mentioning

confidence: 99%

Cloning, genomic organization, and osmotic response of the aldose reductase gene.

Ferraris

Williams

Martin

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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Nucleotide sequence of cDNA for human aldose reductase

Cited by 31 publications

References 2 publications

Isolation of the Mouse Aldose Reductase Promoter and Identification of a Tonicity-responsive Element

Isolation of the Mouse Aldose Reductase Promoter and Identification of a Tonicity-responsive Element

Identification and Characterization of Multiple Osmotic Response Sequences in the Human Aldose Reductase Gene

Cloning, genomic organization, and osmotic response of the aldose reductase gene.

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