A biochemical &amp; biophysical study on in-vitro anti-glycating potential of iridin against d-Ribose modified BSA

Nabi, Rabia; Alvi, Sahir Sultan; Shah, Mohammad Shafi; Ahmad, Saheem; Faisal, Mohammad; Alatar, Abdulrahman A.; Khan, M. Salman

doi:10.1016/j.abb.2020.108373

Cited by 35 publications

(68 citation statements)

References 51 publications

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“…Protein bound CC, a global biomarker of protein oxidation, was assessed to determine the protein carbonyl groups in plasma [11,30]. The data from our in vivo experiment showed that the level of protein-bound CC was markedly elevated from 5.99 to 32.09 nmol/mg protein in DC rats.…”

Section: Rt Restores the Protein Bound Carbonyl Content In Stz-induced Diabetic Ratsmentioning

confidence: 88%

“…Persistent hyperglycemia in DM, if left untreated, contributes to the initiation, progression and development of distinct secondary complications of diabetes via the formation and accumulation of AGEs [1,9]. Moreover, inhibition of AGE formation, maintenance of redox homeostasis and lipid metabolism and regulation of RAGE expression and associated signaling are considered to be the most promising therapeutic strategies in diabetes and related complications [7,30]. Recently, we showed that RT potentially inhibits in vitro protein (bovine serum albumin and LDL) AGE formation as well as LDL-AGE-triggered AGE-RAGE signaling in HEK-293 cells [7,11].…”

Section: Discussionmentioning

confidence: 99%

“…In addition, the decreased level of FRAP in diabetic rats was also improved by the treatment with RT, and this could be attributed to the antioxidant potential of RT [7,11]. Increased production of free radicals in hyperglycemia results in the buildup of reactive carbonyl species (RCS), the global biomarker for the protein oxidation [11,30]. We also reported that the level of plasma protein-bound CC was markedly increased in experimental diabetes, however, repeated oral administration of RT significantly diminished the level of plasma CC in diabetic rats as a result of the potent antioxidant and antiglycation activities of RT; RT was previously shown to exhibit shielding effects against D-ribose-triggered in vitro protein-bound CC generation, as well as AGE-stimulated ROS production in HEK-293 cells [7,11].…”

Section: Discussionmentioning

confidence: 99%

“…The activity of paraoxonase-1 (PON-1) in plasma was assessed by the standard protocol and CH3COOC6H5 was used as the PON-1 substrate [19,29]. The plasma carbonyl content (CC), the product of protein glycation/oxidation, was estimated using the 2,4dinitrophenylhydrazine (DNPH) assay [11,30]. The OD was recorded at 360 nm and the CC level was calculated by applying a MEC of 22 x 10 3 M -1 cm -1 [30].…”

Section: Plasma Frap Pon-1 and Carbonyl Content Assaymentioning

confidence: 99%

“…The plasma carbonyl content (CC), the product of protein glycation/oxidation, was estimated using the 2,4dinitrophenylhydrazine (DNPH) assay [11,30]. The OD was recorded at 360 nm and the CC level was calculated by applying a MEC of 22 x 10 3 M -1 cm -1 [30].…”

Section: Plasma Frap Pon-1 and Carbonyl Content Assaymentioning

confidence: 99%

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Amelioration of neuropilin-1 and RAGE/matrix metalloproteinase-2 pathway-induced renal injury in diabetic rats by rosuvastatin

Nabi

Alvi

Alouffi

et al. 2021

Arch biol sci (Beogr)

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Advanced glycation end-products (AGEs) induce the production of reactive oxygen species (ROS) and extra cellular matrix (ECM) degradation via suppression of neuropilin-1 (NRP-1) and interaction with AGE-receptors (RAGE). This study aimed to reveal whether modulation of NRP-1 by rosuvastatin (RT) prevents AGE-induced renal injury via targeting RAGE/matrix metalloproteinase-2 (MMP-2) signaling in diabetic rats. Treatment with RT ameliorated the altered level of markers of glycemic control, renal injury, cholesterol, triglyceride (TG) and hepatic HMG-CoA reductase activity; the level of circulatory carboxymethyl-lysine (CML) and the accumulation of fluorogenic-AGEs in renal tissue was reduced; the expression of renal NRP-1, a checkpoint target, was stimulated; the transcription of RAGE, NF?B-2, TGF-?1 and MMP-2 was suppressed; the circulatory carbonyl content (CC) and paraoxonase-1 (PON-1) activity was ameliorated, and renal histopathological features were attenuated as evidenced by improved glomerular appearance, Bowman?s space and abundant podocytes in kidneys. In conclusion, RT exhibited the potential to counteract diabetes and AGE-induced renal pathologies via stimulation of NRP-1, suppression of RAGE, and of genes responsible for ECM disintegration (MMP-2) and the inflammatory response (NF?B-2).

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Section: Rt Restores the Protein Bound Carbonyl Content In Stz-induced Diabetic Ratsmentioning

confidence: 88%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Plasma Frap Pon-1 and Carbonyl Content Assaymentioning

confidence: 99%

Section: Plasma Frap Pon-1 and Carbonyl Content Assaymentioning

confidence: 99%

See 3 more Smart Citations

Amelioration of neuropilin-1 and RAGE/matrix metalloproteinase-2 pathway-induced renal injury in diabetic rats by rosuvastatin

Nabi

Alvi

Alouffi

et al. 2021

Arch biol sci (Beogr)

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Nonenzymatic glycosylation of isolated human immunoglobulin‐G by D‐ribose

Ahmad

Alshaghdali

Rehman

et al. 2022

Cell Biochemistry & Function

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Glycation is vital in terms of its damaging effect on macromolecules resulting in the formation of end products, which are highly reactive and cross‐linked irreversible structures, known as advanced glycation end products (AGEs). The continuous accumulation of AGEs is associated with severe diabetes and its associated ailments. Saccharides with their reducing ends can glycate amino acid side chains of proteins, among them glucose is well‐known for its potent glycating capability. However, other reducing sugars can be more reactive glycating agents than glucose. The D‐ribose is a pentose sugar‐containing an active aldehyde group in its open form and is responsible for affecting the biological processes of the cellular system. D‐ribose, a key component of many biological molecules, is more reactive than most reducing sugars. Protein glycation by reducing monosaccharides such as D‐ribose promotes the accelerated formation of AGEs that could lead to cellular impairments and dysfunctions. Also, under a physiological cellular state, the bioavailability rate of D‐ribose is much higher than that of glucose in diabetes, which makes this species much more active in protein glycation as compared with D‐glucose. Due to the abnormal level of D‐ribose in the biological system, the glycation of proteins with D‐ribose needs to be analyzed and addressed carefully. In the present study, human immunoglobulin G (IgG) was isolated and purified via affinity column chromatography. D‐ribose at 10 and 100 mM concentrations was used as glycating agent, for 1–12 days of incubation at 37°C. The postglycation changes in IgG molecule were characterized by UV‐visible and fluorescence spectroscopy, nitroblue tetrazolium assay, and various other physicochemical analyses for the confirmation of D‐ribose mediated IgG glycation.

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Metformin encapsulated gold nanoparticles (MTF‐GNPs): A promising antiglycation agent

Alenazi

Saleem

Khaja

et al. 2022

Cell Biochemistry & Function

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The generation of advanced glycation end products (AGEs) through nonenzymatic protein glycation contributes to the pathogenesis of long‐lived diabetic problems. Metformin (MTF) is the very first drug having antihyperglycemic effects on type II diabetes mellitus which also possess interaction with dicarbonyl compounds and blocks the formation of AGEs. In the current study, MTF is bioconjugated with glycation‐derived synthesized gold nanoparticles (GNPs) of significant size. Additionally, using various biophysical and biochemical approaches, we investigated the antiglycating capacity MTF‐GNPs in contrast to MTF against d‐ribose‐derived glycation of bovine serum albumin. Our key findings via utilizing various assays demonstrated that MTF‐GNPs were able to inhibit AGEs development by reducing hyperchromicity, early glycation products, carbonyl content, hydxoxymethylfurfural content, production of fluorescent AGEs, normalizing the loss of secondary structure (i.e., α‐helix and β‐sheets) of proteins, elevating the levels of free lysine and free arginine more efficiently compared to pure MTF. Based on these results, we concluded that MTF‐GNPs possess a considerable antiglycation property and may be developed as an outstanding anti‐AGEs treatment drug. Further in vivo and clinical research are necessary to determine the therapeutic effects of MTF‐GNPs against AGE‐related and metabolic disorders.

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A biochemical & biophysical study on in-vitro anti-glycating potential of iridin against d-Ribose modified BSA

Cited by 35 publications

References 51 publications

Amelioration of neuropilin-1 and RAGE/matrix metalloproteinase-2 pathway-induced renal injury in diabetic rats by rosuvastatin

Amelioration of neuropilin-1 and RAGE/matrix metalloproteinase-2 pathway-induced renal injury in diabetic rats by rosuvastatin

Nonenzymatic glycosylation of isolated human immunoglobulin‐G by D‐ribose

Metformin encapsulated gold nanoparticles (MTF‐GNPs): A promising antiglycation agent

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