Suppression of AGE Precursor Formation Following Unilateral Ureteral Obstruction in Mouse Kidneys by Transgenic Expression of α-Dicarbonyl/<scp>L</scp>-Xylulose Reductase

Asami, Jun; Odani, Hiroko; Ishii, Aiko; Oide, Kayoko; Sudo, Takako; Nakamura, Atsushi; Miyata, Noriyuki; Otsuka, Noboru; Maeda, Kenji; Nakagawa, Junichi

doi:10.1271/bbb.60311

Cited by 12 publications

(18 citation statements)

References 24 publications

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“…The findings of this study also demonstrated that the known blocker of AGEs [10], AG, attenuated the adverse effects caused by glyoxal, a known AGE precursor in ECs [30]. …”

Section: Discussionmentioning

confidence: 60%

Hyperglycemic oxoaldehyde, glyoxal, causes barrier dysfunction, cytoskeletal alterations, and inhibition of angiogenesis in vascular endothelial cells: aminoguanidine protection

et al. 2009

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Vascular endothelium is vulnerable to the attack of glucose-derived oxoaldehydes (glyoxal and methylglyoxal) during diabetes, through the formation of advanced glycation end products (AGEs). Although aminoguanidine (AG) has been shown to protect against the AGE-induced adverse effects, its protection against the glyoxal-induced alterations in vascular endothelial cells (ECs) such as cytotoxicity, barrier dysfunction, and inhibition of angiogenesis has not been reported and we investigated this in the bovine pulmonary artery ECs (BPAECs). The results showed that glyoxal (1–10 mM) significantly induced cytotoxicity and mitochondrial dysfunction in a dose- and time-dependent (4–12 h) fashion in ECs. Glyoxal was also observed to significantly inhibit EC proliferation. The study also revealed that glyoxal induced EC barrier dysfunction (loss of trans-endothelial electrical resistance), actin cytoskeletal rearrangement, and tight junction alterations in BPAECs. Furthermore, the results revealed that glyoxal significantly inhibited in vitro angiogenesis on the Matrigel. For the first time, this study demonstrated that AG significantly protected against the glyoxal-induced cytotoxicity, barrier dysfunction, cytoskeletal rearrangement, and inhibition of angiogenesis in BPAECs. Therefore, AG appears as a promising protective agent in the treatment of AGE-induced vascular endothelial alterations and dysfunction during diabetes, presumably by blocking the reactivity of the sugar-derived dicarbonyls such as glyoxal and preventing the formation of AGEs.

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“…The findings of this study also demonstrated that the known blocker of AGEs [10], AG, attenuated the adverse effects caused by glyoxal, a known AGE precursor in ECs [30]. …”

Section: Discussionmentioning

confidence: 60%

Hyperglycemic oxoaldehyde, glyoxal, causes barrier dysfunction, cytoskeletal alterations, and inhibition of angiogenesis in vascular endothelial cells: aminoguanidine protection

et al. 2009

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“…In a search for carbonyl‐metabolizing enzymes that might contribute to the reduction of renal carbonyl stress, the role of Dcxr was investigated using rodent models including mice and rats (Sudo et al , ; Asami et al , ; Odani et al , ). High expression of mouse Dcxr in the brush border epithelium of renal tubules was described previously (Nakagawa et al , ) and implied a potential role in the detoxification of AGE‐precursors in the kidney.…”

Section: Catalytic Activity Of Human Dcxrmentioning

confidence: 99%

Human DCXR – another ‘moonlighting protein’ involved in sugar metabolism, carbonyl detoxification, cell adhesion and male fertility?

Ebert¹,

Kisiela²,

Maser³

2014

Biological Reviews

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Dicarbonyl/L-xylulose reductase (DCXR; SDR20C1), a member of the short-chain dehydrogenase/reductase (SDR) superfamily catalyzes the reduction of α-dicarbonyl compounds and monosaccharides. Its role in the metabolism of L-xylulose has been known since 1970, when essential pentosuria was found to be associated with DCXR deficiency. Despite its early discovery, our knowledge about the role of human DCXR in normal physiology and pathophysiology is still incomplete. Sporadic studies have demonstrated aberrant expression in several cancers, but their physiological significance is unknown. In reproductive medicine, where DCXR is commonly referred to as 'sperm surface protein P34H', it serves as marker for epididymal sperm maturation and is essential for gamete interaction and successful fertilization. DCXR exhibits a multifunctional nature, both acting as a carbonyl reductase and also performing non-catalytic functions, possibly resulting from interactions with other proteins. Recent observations associate DCXR with a role in cell adhesion, pointing to a novel function involving tumour progression and possibly metastasis. This review summarizes the current knowledge about human DCXR and its orthologs from mouse and Caenorhabditis elegans (DHS-21) with an emphasis on its multifunctional characteristics. Due to its close structural relationship with DCXR, carbonyl reductase 2 (Cbr2), a tetrameric enzyme found in several non-primate species is also discussed. Similar to human DCXR, Cbr2 from golden hamster (P26h) and cow (P25b) is essential for sperm-zona pellucida interaction and fertilization. Because of the apparent similarity of these two proteins and the inconsistent use of alternative names previously, we provide an overview of the systematic classification of DCXR and Cbr2 and a phylogenetic analysis to illustrate their ancestry.

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“…18,19) L-Xylulose is a ketopentose that is a metabolite in various prokaryotic and eukaryotic metabolic pathways. This carbohydrate exists at very low concentrations in nature and therefore can be termed a rare sugar.…”

Section: L-xylulosementioning

confidence: 99%

Cloning and Overexpression of the Xylitol Dehydrogenase Gene from Bacillus pallidus and Its Application to L-Xylulose Production

Takata

Poonperm

Morimoto

et al. 2010

Bioscience, Biotechnology, and Biochemistry

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Suppression of AGE Precursor Formation Following Unilateral Ureteral Obstruction in Mouse Kidneys by Transgenic Expression of α-Dicarbonyl/L-Xylulose Reductase

Cited by 12 publications

References 24 publications

Hyperglycemic oxoaldehyde, glyoxal, causes barrier dysfunction, cytoskeletal alterations, and inhibition of angiogenesis in vascular endothelial cells: aminoguanidine protection

Hyperglycemic oxoaldehyde, glyoxal, causes barrier dysfunction, cytoskeletal alterations, and inhibition of angiogenesis in vascular endothelial cells: aminoguanidine protection

Human DCXR – another ‘moonlighting protein’ involved in sugar metabolism, carbonyl detoxification, cell adhesion and male fertility?

Cloning and Overexpression of the Xylitol Dehydrogenase Gene from Bacillus pallidus and Its Application to L-Xylulose Production

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