Impaired reductive regeneration of ascorbic acid in the Goto–Kakizaki diabetic rat

Kashiba, Misato; Oka, Jun; Ichikawa, Rumi; Kageyama, Asako; Inayama, Takayo; Kageyama, Haruaki; Ishikawa, Takahiro; Nishikimi, Morimitsu; Inoue, Masayasu; Inoue, Shuji

doi:10.1042/bj3510313

Cited by 9 publications

(8 citation statements)

References 28 publications

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Section: Diabetesmentioning

confidence: 74%

“…Plasma and liver AA concentrations are significantly lower in the Goto‐Kakizaki diabetic rat than in controls [42]. NADPH‐dependent regeneration of AA from DHA is also suppressed in the liver of this diabetic rat [42]. Glucose‐6‐phosphate dehydrogenase activity provides NADPH for DHA reduction and a decrease in the activity of this enzyme in diabetic rat liver may account for the subnormal AA concentrations [43].…”

Section: Diabetesmentioning

confidence: 88%

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The physiological role of dehydroascorbic acid

2002

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Dehydroascorbic acid (DHA) is abundant in the human diet and also is generated from vitamin C (ascorbic acid, AA) in the lumen of the gastrointestinal tract. DHA is absorbed from the lumen of the small intestine and reduced to AA, which subsequently circulates in the blood. Utilization of AA as an antioxidant and enzyme cofactor causes its oxidation to DHA in extracellular £uid and cells. DHA has an important role in many cell types because it can be used to regenerate AA. Both physiological (e.g. insulin, insulin-like growth factor I, cyclic AMP) and pathological (e.g. oxidative stress, diabetes, sepsis) factors alter the transport and metabolic mechanisms responsible for this DHA recycling. ß 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

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Section: Diabetesmentioning

confidence: 74%

Section: Diabetesmentioning

confidence: 88%

The physiological role of dehydroascorbic acid

2002

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“…As regards to the other AKR subfamilies, their involvement of diabetes was reported in a few cases. For instance, Northern blot analysis revealed that expression of AKR1C9 (3α‐HSD) was suppressed in the Goto‐Kakizaki diabetic rat liver 37. As shown in Fig.…”

Section: Discussionmentioning

confidence: 88%

Sn_20.5□_3.5As₂₂I₈: A Largely Disordered Cationic Clathrate with a New Type of Superstructure and Abnormally Low Thermal Conductivity

Zaikina

Kovnir²,

Sobolev

et al. 2007

Chemistry A European J

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Sn(20.5)As(22)I(8), a new cationic clathrate, has been prepared by using an ampoule technique. According to the X-ray powder diffraction data, it crystallizes in the face-centered cubic space group F23 or Fm(-)3 with a unit-cell parameter of a=22.1837(4) A. Single-crystal X-ray data allowed solution of the crystal structure in the subcell with a unit-cell parameter of a(0)=11.092(1) A and the space group Pm(-)3n (R=5.7 %). Sn(20.5)As(22)I(8) (or Sn(20.5) square(3.5)As(22)I(8), accounting for the vacancies in the framework) possesses the clathrate-I type crystal structure, with iodine atoms occupying the cages of the cationic framework composed of tin and arsenic atoms. The crystal structure is strongly disordered. The main features are a random distribution of vacancies, and shifts of the tin and arsenic atoms away from their ideal positions. The coordination of the tin atoms has been confirmed by using (119)Sn Mössbauer spectroscopy. Electron diffraction and high-resolution electron microscopy (HREM) analyses have confirmed the presence of the superstructure ordering, which results in a doubling of the unit-cell parameter and a change of the space group from Pm(-)3n to either F23 or Fm(-)3. Analysis of the crystal structure has led to the construction of four ordering models for the superstructure, which have been corroborated by HREM, and has also led to the identification of disordered regions originating from overlap of the different types of ordered domains. Sn(20.5)As(22)I(8) is a diamagnetic semiconductor with an estimated band gap of 0.45 eV; it displays abnormally low thermal conductivity, with the room temperature value being just 0.5 W m(-1) K(-1).

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“…As regards to the other AKR subfamilies, their involvement of diabetes was reported in a few cases. For instance, Northern blot analysis revealed that expression of AKR1C9 (3a-HSD) was suppressed in the Goto-Kakizaki diabetic rat liver [37]. As shown in Fig.…”

Section: Discussionmentioning

confidence: 99%

A new approach to monitor expression of aldo–keto reductase proteins in mouse tissues

Ren

Tong

et al. 2009

Proteomics

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The aldo-keto reductase (AKR) proteins catalyze reduction of diverse aldehydes and play detoxification roles in many organisms. Since many substrates are shared among AKR, it is generally accepted that these enzymes can functionally compensate each other in response to oxidative stress. Their overall abundances are the important factor that partially reflects the capacity of antioxidant and detoxification in tissues. In this study, the strategy was proposed for generation of Pan-AKR antibodies to recognize most AKR proteins in mouse tissues. Derived from bioinformatic analysis, several consensus peptides with different potential antigenicities were synthesized, conjugated to hemocyanin from keyhole limpets and further delivered to rabbits to generate polyclonal antibodies. Three Pan-AKR antibodies exhibited the immune specificities and immune sensitivities, Pan-AKR-P1 for AKR1B and AKR1C, Pan-AKR-P3 for AKR1C and Pan-AKR-P4 for all the AKR proteins. Pan-AKR-P4 antibody was employed to 2-DE Western blot to examine the AKR abundances in mouse liver and kidney, resulting in seven immune-reactive spots from each tissue. Protein identification with MS revealed that most immune-positive spots were the members of AKR superfamily. Furthermore, Pan-AKR-P4 antibody was implemented to compare the different abundances of the AKR proteins in liver and kidney between normal and diabetic mice, suggesting that diabetes did cause some abnormal changes in the AKR protein abundances.

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Impaired reductive regeneration of ascorbic acid in the Goto–Kakizaki diabetic rat

Cited by 9 publications

References 28 publications

The physiological role of dehydroascorbic acid

The physiological role of dehydroascorbic acid

Sn_20.5□_3.5As₂₂I₈: A Largely Disordered Cationic Clathrate with a New Type of Superstructure and Abnormally Low Thermal Conductivity

A new approach to monitor expression of aldo–keto reductase proteins in mouse tissues

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Impaired reductive regeneration of ascorbic acid in the Goto–Kakizaki diabetic rat

Cited by 9 publications

References 28 publications

The physiological role of dehydroascorbic acid

The physiological role of dehydroascorbic acid

Sn20.5□3.5As22I8: A Largely Disordered Cationic Clathrate with a New Type of Superstructure and Abnormally Low Thermal Conductivity

A new approach to monitor expression of aldo–keto reductase proteins in mouse tissues

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Product

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Sn_20.5□_3.5As₂₂I₈: A Largely Disordered Cationic Clathrate with a New Type of Superstructure and Abnormally Low Thermal Conductivity