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ar-aldose-reductase

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Increased accumulation of plasma AGEs in the <span class="search-highlight">aldose</span> <span class="search-highlight">reductase</span>–null mice. We...
Published: 03 August 2009
FIG. 5. Increased accumulation of plasma AGEs in the aldose reductase–null mice. Western blots of plasma from nondiabetic and diabetic wild- type and akr1b3 -null (aldose reductase–null) mice, probed with anti-argpyrimidine ( A ) and anti-CML ( B ) antibodies. Inset shows positive recognition of glyoxlyic acid–treated BSA. Bar graphs show the intensity of indicated anti-argpyrimidine- or anti-CML–positive bands normalized to Amido-Black–stained blots. Data are presented as means ± SE. * P < 0.01 vs. wild type (control), # P < 0.01 vs. aldose reductase–null (control), and § P < 0.01 vs. wild-type diabetic plasma. AR, aldose reductase; WT, wild type. FIG. 5. Increased accumulation of plasma AGEs in the aldose reductase–null mice. Western blots of plasma from nondiabetic and diabetic wild- type and akr1b3-null (aldose reductase–null) mice, probed with anti-argpyrimidine (A) and anti-CML (B) antibodies. Inset shows positive recognition of glyoxlyic acid–treated BSA. Bar graphs show the intensity of indicated anti-argpyrimidine- or anti-CML–positive bands normalized to Amido-Black–stained blots. Data are presented as means ± SE. *P < 0.01 vs. wild type (control), #P < 0.01 vs. aldose reductase–null (control), and §P < 0.01 vs. wild-type diabetic plasma. AR, aldose reductase; WT, wild type. More
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Increased AGE accumulation in the hearts of <span class="search-highlight">aldose</span> <span class="search-highlight">reductase</span>–null mice.  ...
Published: 03 August 2009
FIG. 6. Increased AGE accumulation in the hearts of aldose reductase–null mice. A : Western blots of heart homogenates from diabetic and nondiabetic wild-type and aldose reductase–null mice were probed with anti-argpyrimidine ( A ) and anti-CML ( B ) antibodies. Nondiabetic wild-type and aldose reductase–null hearts served as respective controls. The expression of aldose reductase, FR-1, and ALDR in the hearts of these mice was examined by Western blots developed using anti–aldose reductase, FR-1, and ALDR antibodies. Recombinant proteins were used as positive controls. Bar graphs show the intensity of the indicated anti-argpyrimidine- or anti-CML–positive bands normalized to GAPDH. Data are presented as means ± SE. * P < 0.01 vs. wild type (control), # P < 0.01 vs. aldose reductase null (control), and § P < 0.01 vs. wild-type diabetic. C : Immunohistochemical analyses of AGE accumulation in hearts of diabetic wild-type and aldose reductase–null mice. Sections were stained with anti-argpyrimidine antibody, and staining was quantified by image analysis. Group data shows the extent of staining quantified using the MetaMorph imaging software. Data are presented as means ± SE. * P < 0.01 vs. wild type (diabetic). AR, aldose reductase; RP, recombinant proteins; WT, wild type. (A high-quality color digital representation of this figure is available in the online issue.) FIG. 6. Increased AGE accumulation in the hearts of aldose reductase–null mice. A: Western blots of heart homogenates from diabetic and nondiabetic wild-type and aldose reductase–null mice were probed with anti-argpyrimidine (A) and anti-CML (B) antibodies. Nondiabetic wild-type and aldose reductase–null hearts served as respective controls. The expression of aldose reductase, FR-1, and ALDR in the hearts of these mice was examined by Western blots developed using anti–aldose reductase, FR-1, and ALDR antibodies. Recombinant proteins were used as positive controls. Bar graphs show the intensity of the indicated anti-argpyrimidine- or anti-CML–positive bands normalized to GAPDH. Data are presented as means ± SE. *P < 0.01 vs. wild type (control), #P < 0.01 vs. aldose reductase null (control), and §P < 0.01 vs. wild-type diabetic. C: Immunohistochemical analyses of AGE accumulation in hearts of diabetic wild-type and aldose reductase–null mice. Sections were stained with anti-argpyrimidine antibody, and staining was quantified by image analysis. Group data shows the extent of staining quantified using the MetaMorph imaging software. Data are presented as means ± SE. *P < 0.01 vs. wild type (diabetic). AR, aldose reductase; RP, recombinant proteins; WT, wild type. (A high-quality color digital representation of this figure is available in the online issue.) More
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Genetic ablation of <span class="search-highlight">aldose</span> <span class="search-highlight">reductase</span> exacerbates diabetic lesion formation ...
Published: 03 August 2009
FIG. 7. Genetic ablation of aldose reductase exacerbates diabetic lesion formation and AGE accumulation. A : Photomicrographs of cross sections of innominate arteries of 20-week-old nondiabetic (control) and diabetic apoE -null and akr1b3-apoE –null mice. Sections were stained with hematoxylin and eosin, and the lesion area was quantified by image analysis. Data are presented as means ± SE. * P < 0.01 vs. apoE -null (control), # P < 0.01 vs. aldose reductase/ apoE –null (control) and § P < 0.01 vs. apoE -null (diabetic). Arterial sections of diabetic apoE -null and akr1b3-apoE –null mice stained with anti-argpyrimidine ( B ), anti-CML ( C ), and anti–3-deoxyglucosone imidazolone ( D ) antibodies. The extent of staining was quantified by image analysis. Data are presented as means ± SE. * P < 0.05 vs. apoE -null (diabetic). AR, aldose reductase. (A high-quality color digital representation of this figure is available in the online issue.) FIG. 7. Genetic ablation of aldose reductase exacerbates diabetic lesion formation and AGE accumulation. A: Photomicrographs of cross sections of innominate arteries of 20-week-old nondiabetic (control) and diabetic apoE-null and akr1b3-apoE–null mice. Sections were stained with hematoxylin and eosin, and the lesion area was quantified by image analysis. Data are presented as means ± SE. *P < 0.01 vs. apoE-null (control), #P < 0.01 vs. aldose reductase/apoE–null (control) and §P < 0.01 vs. apoE-null (diabetic). Arterial sections of diabetic apoE-null and akr1b3-apoE–null mice stained with anti-argpyrimidine (B), anti-CML (C), and anti–3-deoxyglucosone imidazolone (D) antibodies. The extent of staining was quantified by image analysis. Data are presented as means ± SE. *P < 0.05 vs. apoE-null (diabetic). AR, aldose reductase. (A high-quality color digital representation of this figure is available in the online issue.) More
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Genetic ablation of AKR1B3 (<span class="search-highlight">aldose</span> <span class="search-highlight">reductase</span>) diminishes the reduction of A...
Published: 03 August 2009
FIG. 4. Genetic ablation of AKR1B3 (aldose reductase) diminishes the reduction of AGE precursors. A : Rate of reduction of glyceraldehyde ( i ), methylglyoxal ( ii ), 3-deoxyglucosone ( iii ), and glyoxal ( iv ) in cardiac homogenates prepared from wild-type and akr1b3 -null mice. The enzyme activity was determined with glyceraldehyde (10 mmol/l), glyoxal (1 mmol/l), methylglyoxal (1 mmol/l), or deoxyglucosone (1 mmol/l) and 0.15 mmol/l NADPH, with or without 1 μmol/l sorbinil. Values are presented as means ± SE. * P < 0.05 vs. wild type ( n = 6). Inset shows the expression of the proteins in wild-type and aldose reductase–knockout mice. B : Rate of formation of S -d-lactoylglutathione ( i ) and S -glycolylglutathione ( ii ) in homogenates prepared from wild-type and akr1b3 -null hearts. Glyoxalase I activity was measured with methylglyoxal (1 mmol/l) or glyoxal (1 mmol/l) and GSH (1 mmol/l) in the absence or presence of glyoxalase I inhibitor BBGC (0.2 mmol/l). Inset to panel i shows Western blots developed from wild-type and akr1b3 -null (knockout) hearts using the anti–glyoxalase-I antibody. Data are means ± SE ( n = 6). * P < 0.01 vs. wild-type (methylglyoxal or glyoxal) and # P < 0.01 vs. aldose reductase–null mice (methylglyoxal or glyoxal). Inset shows the expression of glyoxalase I in wild-type and aldose reductase–knockout mice. C : Computer simulations for the relative contributions of aldose reductase and glyoxalase I in the metabolism of glyoxal ( i ) and methylglyoxal ( ii ). Relative contribution of the enzymes was calculated on the basis of measurement of aldose reductase and glyoxalase I enzyme activities assuming that the concentration of AGE precursors is in steady state achieved between the processes of formation and those of elimination. AR, aldose reductase; WT, wild type. FIG. 4. Genetic ablation of AKR1B3 (aldose reductase) diminishes the reduction of AGE precursors. A: Rate of reduction of glyceraldehyde (i), methylglyoxal (ii), 3-deoxyglucosone (iii), and glyoxal (iv) in cardiac homogenates prepared from wild-type and akr1b3-null mice. The enzyme activity was determined with glyceraldehyde (10 mmol/l), glyoxal (1 mmol/l), methylglyoxal (1 mmol/l), or deoxyglucosone (1 mmol/l) and 0.15 mmol/l NADPH, with or without 1 μmol/l sorbinil. Values are presented as means ± SE. *P < 0.05 vs. wild type (n = 6). Inset shows the expression of the proteins in wild-type and aldose reductase–knockout mice. B: Rate of formation of S-d-lactoylglutathione (i) and S-glycolylglutathione (ii) in homogenates prepared from wild-type and akr1b3-null hearts. Glyoxalase I activity was measured with methylglyoxal (1 mmol/l) or glyoxal (1 mmol/l) and GSH (1 mmol/l) in the absence or presence of glyoxalase I inhibitor BBGC (0.2 mmol/l). Inset to panel i shows Western blots developed from wild-type and akr1b3-null (knockout) hearts using the anti–glyoxalase-I antibody. Data are means ± SE (n = 6). *P < 0.01 vs. wild-type (methylglyoxal or glyoxal) and #P < 0.01 vs. aldose reductase–null mice (methylglyoxal or glyoxal). Inset shows the expression of glyoxalase I in wild-type and aldose reductase–knockout mice. C: Computer simulations for the relative contributions of aldose reductase and glyoxalase I in the metabolism of glyoxal (i) and methylglyoxal (ii). Relative contribution of the enzymes was calculated on the basis of measurement of aldose reductase and glyoxalase I enzyme activities assuming that the concentration of AGE precursors is in steady state achieved between the processes of formation and those of elimination. AR, aldose reductase; WT, wild type. More
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Gene expression of <span class="search-highlight">aldose</span> <span class="search-highlight">reductase</span> (<span class="search-highlight">AR</span>), GAPDH, p53, and PARP on gestation...
Published: 01 December 2008
FIG. 3. Gene expression of aldose reductase (AR), GAPDH, p53, and PARP on gestational day 11 in the control (N) and manifestly diabetic (MD) groups containing 29 and 32 embryos, respectively. Nonmalformed and malformed N and MD offspring are denoted Nn (28 embryos), MDn (20 embryos), Nm (1 embryo)... More
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Inhibition of <span class="search-highlight">aldose</span> <span class="search-highlight">reductase</span> (<span class="search-highlight">AR</span>) prevents high glucose (HG)-induced acti...
Published: 01 November 2004
FIG. 4. Inhibition of aldose reductase (AR) prevents high glucose (HG)-induced activation of adhesion molecules. Growth-arrested VSMCs in normal glucose (NG) or HG or mannitol (M) were cultured in the absence or the presence of the aldose reductase inhibitors sorbinil or tolrestat (10 μmol/l each) for 24 h. Pooled total cell extracts were prepared from three separate incubations; the proteins were separated by SDS-PAGE and then subjected to Western blot analysis. Western blot analysis was carried out at least three times using either monoclonal antibodies raised against ICAM-1 and VCAM-1 or polyclonal antibodies raised against human aldose reductase. The blots were visualized using enhanced chemiluminescence. Bars represent means ± SE (n = 3); *P < 0.001 vs. HG cells. FIG. 4. Inhibition of aldose reductase (AR) prevents high glucose (HG)-induced activation of adhesion molecules. Growth-arrested VSMCs in normal glucose (NG) or HG or mannitol (M) were cultured in the absence or the presence of the aldose reductase inhibitors sorbinil or tolrestat (10 μmol/l each) for 24 h. Pooled total cell extracts were prepared from three separate incubations; the proteins were separated by SDS-PAGE and then subjected to Western blot analysis. Western blot analysis was carried out at least three times using either monoclonal antibodies raised against ICAM-1 and VCAM-1 or polyclonal antibodies raised against human aldose reductase. The blots were visualized using enhanced chemiluminescence. Bars represent means ± SE (n = 3); *P < 0.001 vs. HG cells. More
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Ablation of <span class="search-highlight">aldose</span> <span class="search-highlight">reductase</span> (<span class="search-highlight">AR</span>) by siRNA. The serum-starved VSMCs were tr...
Published: 01 November 2004
FIG. 5. Ablation of aldose reductase (AR) by siRNA. The serum-starved VSMCs were transfected with two different double-stranded aldose reductase-specific siRNAs to a final concentration of 100 nmol each and cultured for 48 h at 37°C. The VSMCs that were incubated with the transfection reagent (TR) only or with nonspecific RNA (control siRNA) were used as control. A: Aldose reductase activity determined using dl-glyceraldehyde and NADPH as substrates. Bars represent means ± SE (n = 4); *P < 0.001 vs. control siRNA transfected cells. B and C: Western blots after SDS-PAGE separation of 10 μg of VSMC cell protein developed using anti–aldose reductase or anti–glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibodies, respectively. FIG. 5. Ablation of aldose reductase (AR) by siRNA. The serum-starved VSMCs were transfected with two different double-stranded aldose reductase-specific siRNAs to a final concentration of 100 nmol each and cultured for 48 h at 37°C. The VSMCs that were incubated with the transfection reagent (TR) only or with nonspecific RNA (control siRNA) were used as control. A: Aldose reductase activity determined using dl-glyceraldehyde and NADPH as substrates. Bars represent means ± SE (n = 4); *P < 0.001 vs. control siRNA transfected cells. B and C: Western blots after SDS-PAGE separation of 10 μg of VSMC cell protein developed using anti–aldose reductase or anti–glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibodies, respectively. More
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Silencing of <span class="search-highlight">aldose</span> <span class="search-highlight">reductase</span> (<span class="search-highlight">AR</span>) mRNA by siRNA transfection attenuates hi...
Published: 01 November 2004
FIG. 6. Silencing of aldose reductase (AR) mRNA by siRNA transfection attenuates high glucose (HG)-induced NF-κB and AP-1 activation but does not affect SP-1 or OCT-1 activity. Expression of aldose reductase was silenced by incubating the cells with aldose reductase siRNA1 for 48 h at 37°C. Equal amounts of nuclear extracts, prepared from the aldose reductase-ablated VSMCs in normal glucose (NG) or stimulated with HG or mannitol (M) for 3 h, were subjected to EMSA using NF-κB (A), AP-1 (B), SP-1 (C), and OCT-1 (D) consensus sequences. Extract prepared from cells that were left untreated or treated with the transfection reagent (TR) or control siRNA were used as controls. FIG. 6. Silencing of aldose reductase (AR) mRNA by siRNA transfection attenuates high glucose (HG)-induced NF-κB and AP-1 activation but does not affect SP-1 or OCT-1 activity. Expression of aldose reductase was silenced by incubating the cells with aldose reductase siRNA1 for 48 h at 37°C. Equal amounts of nuclear extracts, prepared from the aldose reductase-ablated VSMCs in normal glucose (NG) or stimulated with HG or mannitol (M) for 3 h, were subjected to EMSA using NF-κB (A), AP-1 (B), SP-1 (C), and OCT-1 (D) consensus sequences. Extract prepared from cells that were left untreated or treated with the transfection reagent (TR) or control siRNA were used as controls. More
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Antisense ablation of <span class="search-highlight">aldose</span> <span class="search-highlight">reductase</span> prevents high-glucose–induced SMC gr...
Published: 01 April 2006
FIG. 2. Antisense ablation of aldose reductase prevents high-glucose–induced SMC growth. The VSMCs were either left untreated or treated with lipofectamine, aldose reductase (AR) antisense oligonucleotide, or scrambled oligonucleotides and cultured in normal (5.5 mmol/l) glucose (NG) or high (25 mmol/l) glucose (HG) for 24 h. Cell growth measured by counting the number of cells (A) and cell viability by MTT assay (OD562) (B). The bars represent means ± SE (n = 4). Inset of B shows a representative immunoblot of the control (C), lipofectamine-treated (L), scrambled oligonucleotide–treated (S), and aldose reductase antisense oligonucleotide–treated (A) SMCs probed with anti–aldose reductase antibodies. **P < 0.001 vs. cells transfected with the scrambled oligonucleotide. FIG. 2. Antisense ablation of aldose reductase prevents high-glucose–induced SMC growth. The VSMCs were either left untreated or treated with lipofectamine, aldose reductase (AR) antisense oligonucleotide, or scrambled oligonucleotides and cultured in normal (5.5 mmol/l) glucose (NG) or high (25 mmol/l) glucose (HG) for 24 h. Cell growth measured by counting the number of cells (A) and cell viability by MTT assay (OD562) (B). The bars represent means ± SE (n = 4). Inset of B shows a representative immunoblot of the control (C), lipofectamine-treated (L), scrambled oligonucleotide–treated (S), and aldose reductase antisense oligonucleotide–treated (A) SMCs probed with anti–aldose reductase antibodies. **P < 0.001 vs. cells transfected with the scrambled oligonucleotide. More
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AKR-catalyzed reduction of methylglyoxal in mouse heart.  <em>A</em>...
Published: 03 August 2009
FIG. 3. AKR-catalyzed reduction of methylglyoxal in mouse heart. A : Acetol generated in effluents of isolated wild-type (C57) or aldose reductase–transgenic hearts perfused with 20 μmol/l methylglyoxal. Acetol concentration was measured by GC-MS after derivatization with PFBHA and BSTFA. 13C3 Acetol was used as an internal standard. Data are presented as means ± SE. * P < 0.01 vs. wild type ( n = 4). B : Western blot analysis of cardiac myocytes isolated from adult male C57 mice probed with antibodies raised against AKR1B1 (aldose reductase), AKR1B8 (FR-1), and AKR1A4 (ALDR). Figure shows bands from three different mice. C : Rate of methylglyoxal reduction in homogenates prepared from hearts of wild-type mice ( n = 6) or mice with cardiac myocyte–specific transgene expressing AKR1B4 (rat aldose reductase; n = 6) or AKR1B8 (FR-1; n = 6). The enzyme activity was determined with 1 mmol/l methylglyoxal and 0.15 mmol/l NADPH, with or without 1 μmol/l sorbinil. Inset shows Western blots from wild-type and transgenic hearts developed with anti–aldose reductase and anti–FR-1 antibodies. * P < 0.01 vs. wild type (control), # P < 0.01 vs. aldose reductase–transgenic (control), and § P < 0.01 vs. FR1–transgenic (control). AR-TG, aldose reductase–transgenic; WT, wild type. FIG. 3. AKR-catalyzed reduction of methylglyoxal in mouse heart. A: Acetol generated in effluents of isolated wild-type (C57) or aldose reductase–transgenic hearts perfused with 20 μmol/l methylglyoxal. Acetol concentration was measured by GC-MS after derivatization with PFBHA and BSTFA. 13C3 Acetol was used as an internal standard. Data are presented as means ± SE. *P < 0.01 vs. wild type (n = 4). B: Western blot analysis of cardiac myocytes isolated from adult male C57 mice probed with antibodies raised against AKR1B1 (aldose reductase), AKR1B8 (FR-1), and AKR1A4 (ALDR). Figure shows bands from three different mice. C: Rate of methylglyoxal reduction in homogenates prepared from hearts of wild-type mice (n = 6) or mice with cardiac myocyte–specific transgene expressing AKR1B4 (rat aldose reductase; n = 6) or AKR1B8 (FR-1; n = 6). The enzyme activity was determined with 1 mmol/l methylglyoxal and 0.15 mmol/l NADPH, with or without 1 μmol/l sorbinil. Inset shows Western blots from wild-type and transgenic hearts developed with anti–aldose reductase and anti–FR-1 antibodies. *P < 0.01 vs. wild type (control), #P < 0.01 vs. aldose reductase–transgenic (control), and §P < 0.01 vs. FR1–transgenic (control). AR-TG, aldose reductase–transgenic; WT, wild type. More
Journal Articles
Journal: Diabetes
Diabetes 2006;55(7):1946–1953
Published: 01 July 2006
... in the peripheral nerves. Here, we used aldose reductase (AR)-deficient (AR−/−) and AR inhibitor (ARI)-treated mice to further understand the in vivo role of polyol pathway in the pathogenesis of diabetic neuropathy. Under normal conditions, there were no obvious differences in the innervation patterns...
Journal Articles
Journal: Diabetes
Diabetes 2009;58(11):2486–2497
Published: 03 August 2009
... vs. aldose reductase–null (control), and § P < 0.01 vs. wild-type diabetic plasma. AR, aldose reductase; WT, wild type. FIG. 5. Increased accumulation of plasma AGEs in the aldose reductase–null mice. Western blots of plasma from nondiabetic and diabetic wild- type and akr1b3-null...
Includes: Supplementary data
Journal Articles
Journal: Diabetes
Diabetes 2005;54(11):3119–3125
Published: 01 November 2005
..., and proliferation of blood vessels, were evident. These changes in the diabetic retina were associated with increased expression of aldose reductase (AR). To further understand the role of AR in the pathogenesis of diabetic retinopathy, we generated db/db mice with an AR null mutation (AR...
Journal Articles
Journal: Diabetes
Diabetes 2002;51(10):3095–3101
Published: 01 October 2002
...Deepak Chandra; Elias B. Jackson; Kota V. Ramana; Rocky Kelley; Satish K. Srivastava; Aruni Bhatnagar Increased glucose utilization by aldose reductase (AR) has been implicated in the development of diabetes complications. However, the mechanisms that regulate AR during diabetes remain unknown...
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Inhibition or RNA interference ablation of <span class="search-highlight">aldose</span> <span class="search-highlight">reductase</span> prevents high-g...
Published: 01 March 2005
FIG. 1. Inhibition or RNA interference ablation of aldose reductase prevents high-glucose-induced PKC activation: A: Serum-starved VSMCs were preincubated without or with 10 μmol/l sorbinil or tolrestat for 24 h and stimulated with high glucose (HG) or mannitol (M) for 3 h. After incubation, the cytosolic and membrane fractions were isolated, and the PKC activity associated with each of these fractions was measured as described in research design and methods. Bars represent the means ± SE (n = 4). #P < 0.001 vs. normal glucose (NG); **P < 0.001 vs. high glucose. B: The VSMCs were either left untreated (C), treated with RNAiFect transfection reagent (TR), or transiently transfected with aldose reductase (AR) siRNA or control nonspecific siRNA (Control RNAi; CR) and cultured for 48 h at 37°C. The cells were stimulated with high glucose or mannitol or 10 nmol/l of PMA (phorbol 12-myristate 13-acetate) for 3 h, and the membrane-bound PKC activity was measured. The aldose reductase-ablated VSMCs were incubated with high glucose for 24 h. The bars represent the means ± SE (n = 4). **P < 0.001 vs. control RNAi-transfected cells. Inset: Western blots of siRNA-transfected cells developed with rabbit polyclonal aldose reductase antibodies. FIG. 1. Inhibition or RNA interference ablation of aldose reductase prevents high-glucose-induced PKC activation: A: Serum-starved VSMCs were preincubated without or with 10 μmol/l sorbinil or tolrestat for 24 h and stimulated with high glucose (HG) or mannitol (M) for 3 h. After incubation, the cytosolic and membrane fractions were isolated, and the PKC activity associated with each of these fractions was measured as described in research design and methods. Bars represent the means ± SE (n = 4). #P < 0.001 vs. normal glucose (NG); **P < 0.001 vs. high glucose. B: The VSMCs were either left untreated (C), treated with RNAiFect transfection reagent (TR), or transiently transfected with aldose reductase (AR) siRNA or control nonspecific siRNA (Control RNAi; CR) and cultured for 48 h at 37°C. The cells were stimulated with high glucose or mannitol or 10 nmol/l of PMA (phorbol 12-myristate 13-acetate) for 3 h, and the membrane-bound PKC activity was measured. The aldose reductase-ablated VSMCs were incubated with high glucose for 24 h. The bars represent the means ± SE (n = 4). **P < 0.001 vs. control RNAi-transfected cells. Inset: Western blots of siRNA-transfected cells developed with rabbit polyclonal aldose reductase antibodies. More
Images
Inhibition/ablation of <span class="search-highlight">aldose</span> <span class="search-highlight">reductase</span> attenuates intracellular DAG format...
Published: 01 March 2005
FIG. 5. Inhibition/ablation of aldose reductase attenuates intracellular DAG formation. A: Time-dependent changes in DAG formation measured in extracts of serum-starved VSMCs preincubated without or with 10 μmol/l sorbinil or tolrestat for 24 h and then incubated with 5.5 mmol/l (normal glucose [NG]) or 25 mmol/l glucose (high glucose [HG]) or normal glucose + mannitol (M; 19.5 mmol/l). B: Changes in DAG formation in cells untreated or treated with control siRNA, transfection reagent (TR), or aldose reductase (AR) siRNA for 48 h on exposure with high glucose. The DAG concentration in the extracts was measured in the membrane and cytosol using a radiometric assay kit. Data represent the means ± SE (n = 4). FIG. 5. Inhibition/ablation of aldose reductase attenuates intracellular DAG formation. A: Time-dependent changes in DAG formation measured in extracts of serum-starved VSMCs preincubated without or with 10 μmol/l sorbinil or tolrestat for 24 h and then incubated with 5.5 mmol/l (normal glucose [NG]) or 25 mmol/l glucose (high glucose [HG]) or normal glucose + mannitol (M; 19.5 mmol/l). B: Changes in DAG formation in cells untreated or treated with control siRNA, transfection reagent (TR), or aldose reductase (AR) siRNA for 48 h on exposure with high glucose. The DAG concentration in the extracts was measured in the membrane and cytosol using a radiometric assay kit. Data represent the means ± SE (n = 4). More
Meeting Abstracts
Journal: Diabetes
Diabetes 2020;69(Supplement_1):1080-P
Published: 01 June 2020
... of Aldose Reductase (AR) were unsuccessful, due to low AR binding affinity and off-target binding with Aldehyde Reductase (AldR), an enzyme critical for detoxification of aldehydes in the liver and normal hepatocyte function. This resulted in liver-related safety and tolerability issues with first...
Journal Articles
Journal: Diabetes
Diabetes 1974;23(5):460–468
Published: 01 May 1974
..., AR-A and AR-B, were isolated from renal papilla and formation. More recently, it was found both in vitro were characterized. These two forms were also found in brain, and in vivo that aldose reductase inhibitors prevented retina, pancreas, lens and optic nerve. AR-A and AR-B differed the sugar...
Journal Articles
Journal: Diabetes
Diabetes 2003;52(3):864–871
Published: 01 March 2003
...Irina G. Obrosova; Alexander G. Minchenko; Rukmini Vasupuram; Lauren White; Omorodola I. Abatan; Arno K. Kumagai; Robert N. Frank; Martin J. Stevens The study addressed the role for aldose reductase (AR) in 1) retinal oxidative stress and vascular endothelial growth factor (VEGF...
Meeting Abstracts
Journal: Diabetes
Diabetes 2022;71(Supplement_1):207-LB
Published: 01 June 2022
... (T2D) subjects. Increased cardiac aldose reductase (AR) activity has been correlated with impaired cardiac function and less effective energy metabolism in DbCM subjects. The aim of the present study was to evaluate the effect AT-001, a potent and selective AR inhibitor, on cardiac function, structure...