Kinetics of Glycoxidation of Bovine Serum Albumin by Glucose, Fructose and Ribose and Its Prevention by Food Components

Sadowska-Bartosz, Izabela; Galiniak, Sabina; Bartosz, Grzegorz

doi:10.3390/molecules191118828

Cited by 88 publications

(100 citation statements)

References 41 publications

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“…Since AR induces EMT marker expression, there would be an increased risk of PCO formation after diabetic cataract removal. In an potentially related area, it is interesting to note that fructose, the end product of AR polyol pathway, has been demonstrated to form advanced glycated end-products (AGEs) much faster than glucose [35]. Raghavan and colleagues recently reported that AGEs in lens capsule enhance EMT of LECs under TGF-β2 treatment [36, 37].…”

Section: Discussionmentioning

confidence: 99%

Influence of aldose reductase on epithelial-to-mesenchymal transition signaling in lens epithelial cells

Chang

Shieh

Petrash

2017

Chemico-Biological Interactions

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Cataract is the most frequent cause of blindness worldwide and is treated by surgical removal of the opaque lens to restore the light path to the retina. While cataract surgery is a safe procedure, some patients develop a complication of the surgery involving opacification and wrinkling of the posterior lens capsule. This process, called posterior capsule opacification (PCO), requires a second clinical treatment that can in turn lead to additional complications. Prevention of PCO is a current unmet need in the vision care enterprise. The pathogenesis of PCO involves the transition of lens epithelial cells to a mesenchymal phenotype, designated epithelial-to-mesenchymal transition (EMT). Our previous studies showed that transgenic mice designed for overexpression of human aldose reductase developed lens defects reminiscent of PCO. In the current study, we evaluated the impact of aldose reductase (AR) on expression of expression of EMT markers in the lens. Primary lens epithelial cells from AR-transgenic mice showed downregulated expression of Foxe3 and Pax6 and increased expression of α-SMA, fibronectin and snail, a pattern of gene expression typical of cells undergoing EMT. A role for AR in these changes was further confirmed when we observed that they could be normalized by treatment of cells with Sorbinil, an AR inhibitor. Smad-dependent and Smad-independent pathways are known to contribute to EMT. Interestingly, AR overexpression induced ERK but not Smad-2 activation. These results suggest that elevation of AR may lead to activation of ERK signaling and thus play a role in TGF-β/Smad independent induction of EMT in lens epithelial cells.

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Section: Discussionmentioning

confidence: 99%

Influence of aldose reductase on epithelial-to-mesenchymal transition signaling in lens epithelial cells

Chang

Shieh

Petrash

2017

Chemico-Biological Interactions

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“…In the diabetic eye, cataract [52] and retinopathy [53] are major complications causing vision loss. Other than oxidative stress, AR polyol pathway also accelerates advanced glycation end-product (AGE) formation by producing fructose, which forms AGE much faster than glucose [54]. A study observed the increase of AGE in retina causes ocular inflammation by inducing RMG activation [19].…”

Section: Discussionmentioning

confidence: 99%

Aldose reductase mediates retinal microglia activation

Chang

Shieh

Petrash

2016

Biochemical and Biophysical Research Communications

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Retinal microglia (RMG) are one of the major immune cells in charge of surveillance of inflammatory responses in the eye. In the absence of an inflammatory stimulus, RMG reside predominately in the ganglion layer and inner or outer plexiform layers. However, under stress RMG become activated and migrate into the inner nuclear layer (INL) or outer nuclear layer (ONL). Activated RMG in cell culture secrete pro-inflammatory cytokines in a manner sensitive to downregulation by aldose reductase inhibitors. In this study, we utilized CX3CR1GFP mice carrying AR mutant alleles to evaluate the role of AR on RMG activation and migration in vivo. When tested on an ARWT background, IP injection of LPS induced RMG activation and migration into the INL and ONL. However, this phenomenon was largely prevented by AR inhibitors or in AR null mice, or was exacerbated in transgenic mice that over-express AR. LPS-induced increases in ocular levels of TNF-α and CX3CL-1 in WT mice were substantially lower in AR null mice or were reduced by AR inhibitor treatment. These studies demonstrate that AR expression in RMG may contribute to the proinflammatory phenotypes common to various eye diseases such as uveitis and diabetic retinopathy.

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“…2, 9 These reactive carbonyl species (RCS), also knowns as AGE precursors, are much more reactive than reducing sugars. 10, 11 By continuing to react with proteins, these RCS irreversibly bind to the side chains of proteins, induce protein crosslinks, and lead to the formation of AGEs. While in general, RCS play a critical step in AGEs formation, glycation can also be catalyzed by free radicals and transition metals through oxidation.…”

Section: Introductionmentioning

confidence: 99%

Glucitol-core containing gallotannins inhibit the formation of advanced glycation end-products mediated by their antioxidant potential

Liu

Frost

et al. 2016

Food Funct.

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Glucitol-core containing gallotannins (GCGs) are polyphenols containing galloyl groups attached to a 1,5-anhydro-D-glucitol core, which is uncommon among naturally occurring plant gallotannins. GCGs have only been isolated from maple (Acer) species, including the red maple (Acer rubrum), a medicinal plant which along with the sugar maple (Acer saccharum), are the major sources of the natural sweetener, maple syrup. GCGs are reported to show antioxidant, α-glucosidase inhibitory, and antidiabetic effects, but their antiglycating potential is unknown. Herein, the inhibitory effects of five GCGs (containing 1–4 galloyls) on the formation of advanced glycation end-products (AGEs) were evaluated by MALD-TOF mass spectroscopy, and the BSA-fructose, and G.K. peptide-ribose assays. The GCGs showed superior activities compared to the synthetic antiglycating agent, aminoguanidine (IC50 15.8–151.3 vs. > 300 μM) at the early, middle, and late stages of glycation. Circular dichroism data revealed that the GCGs were able to protect the secondary structure of BSA protein from glycation. The GCGs did not inhibit AGEs formation by the trapping of reactive carbonyl species, namely, methylglyoxal, but showed free radical scavenging activities in the DPPH assay. The free radical quenching properties of the GCGs was further confirmed by electron paramagnetic resonance spectroscopy using ginnalin A (contains 2 galloyls) as a representative GCG. In addition, this GCG chelated ferrous iron, an oxidative catalyst of AGEs formation, supporting a potential antioxidant mechanism of antiglycating activity for these polyphenols. Therefore, GCGs should be further investigated for their antidiabetic potential given their antioxidant, α-glucosidase inhibitory, and antiglycating properties.

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Kinetics of Glycoxidation of Bovine Serum Albumin by Glucose, Fructose and Ribose and Its Prevention by Food Components

Cited by 88 publications

References 41 publications

Influence of aldose reductase on epithelial-to-mesenchymal transition signaling in lens epithelial cells

Influence of aldose reductase on epithelial-to-mesenchymal transition signaling in lens epithelial cells

Aldose reductase mediates retinal microglia activation

Glucitol-core containing gallotannins inhibit the formation of advanced glycation end-products mediated by their antioxidant potential

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