Glyoxal induced glycative insult suffered by immunoglobulin G and fibrinogen proteins: A comparative physicochemical characterization to reveal structural perturbations

Alouffi, Sultan; Shahab, Uzma; Khan, Saif; Khan, M. Salman; Khanam, Afreen; Akasha, Rihab; Shahanawaz, S.D.; Arif, Hussain; Tahir, Iram Khan; Rehman, Shahnawaz; Ahmad, Saheem

doi:10.1016/j.ijbiomac.2022.02.093

Cited by 7 publications

(7 citation statements)

References 95 publications

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“…However, a negligible amount of ketoamine was detected for N‐IgG. The decrease in Amadori products revealed their transformation to AGEs 22 …”

Section: Resultsmentioning

confidence: 98%

Section: Resultsmentioning

confidence: 99%

“…Besides superoxide anions, hydroxyl radicals are also generated during the conversion of ketoamines to protein carbonyls via the Fenton reaction and add fuel to the fire by increasing oxidative stress. 22 Thus, hydroxyl radicals in the D-rib-IgG samples were quantified by thiobarbituric acid. With 10 and 100 mM D-ribose, the levels of TBARs were found to be 1.17 ± 0.2 µmol ml −1 and 2.92 ± 0.31 µmol ml −1 in D-rib-IgG, respectively.…”

Section: Thiobarbituric Acid Reactive Substance (Tbars) Assaymentioning

confidence: 99%

“…It has a half‐life (21–25 days) longer than all other isotypes and is the most extensively studied class of IgG 21 . Glycation‐induced IgG‐AGEs are known to be correlated with rheumatoid arthritis and recent physicochemical characterization studies confirmed glyoxal‐(GO‐) induced structural perturbations in IgG protein 22 . Furthermore, IgG possesses 80 lysine and 38 arginine residues in its structure that render it an easy target for glycating agents (Figure 1).…”

Section: Introductionmentioning

confidence: 99%

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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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“…However, a negligible amount of ketoamine was detected for N‐IgG. The decrease in Amadori products revealed their transformation to AGEs 22 …”

Section: Resultsmentioning

confidence: 98%

Section: Resultsmentioning

confidence: 99%

Section: Thiobarbituric Acid Reactive Substance (Tbars) Assaymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

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

Ahmad

Alshaghdali

Rehman

et al. 2022

Cell Biochemistry & Function

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“…All the protein samples with CR stock were taken in the molar ratio 1:2 and incubated for 30 min under dark condition. Absorption spectra were taken at wavelength 400–700 nm by using spectrophotometer in 1 cm path length cuvette 29 …”

Section: Methodsmentioning

confidence: 99%

Antiglycation potential of plant based TiO₂ nanoparticle in D‐ribose glycated BSA in vitro

Alenazi

Saleem

Khaja

et al. 2022

Cell Biochemistry & Function

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Biosynthetic procedure is one of the best alternatives, inexpensive and ecologically sound for the synthesis of titanium dioxide (TiO2) nanoparticles using a methanolic extract of medicinal plant. The main prospect of this study was to investigate the antiglycation activity of the TiO2 nanoparticles (TNP) prepared by ethanolic leaf extract of the Coleus scutellarioides. In this study, biosynthesized TNP characterized with UV‐Visible spectroscopy, X‐ray diffraction, Fourier transform infrared spectroscopy and scanning electron microscope. These TNP were further investigated with respect to their antiglycation property and it was checked in the mixture of d‐ribose glycated bovine serum albumin (BSA) by measuring ketoamine, carbonyl content, Advanced glycation end products (AGEs) and aggregation of protein instigated by glycation process. The inhibitory effect of TNP to restore the structure of BSA in presence of d‐ribose were also characterize by biophysical techniques mentioned above. Therefore, the findings of this study suggest repurposing of TNP for its antiglycation property that could be helpful in prevention of glycation instigated AGEs formation and structural loss of proteins.

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Generation of autoantibodies against glycated fibrinogen: Role in diabetic nephropathy and retinopathy

Khanam,

Alouffi,

Alyahyawi

et al. 2024

Analytical Biochemistry

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Glyoxal induced glycative insult suffered by immunoglobulin G and fibrinogen proteins: A comparative physicochemical characterization to reveal structural perturbations

Cited by 7 publications

References 95 publications

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

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

Antiglycation potential of plant based TiO₂ nanoparticle in D‐ribose glycated BSA in vitro

Generation of autoantibodies against glycated fibrinogen: Role in diabetic nephropathy and retinopathy

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Glyoxal induced glycative insult suffered by immunoglobulin G and fibrinogen proteins: A comparative physicochemical characterization to reveal structural perturbations

Cited by 7 publications

References 95 publications

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

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

Antiglycation potential of plant based TiO2 nanoparticle in D‐ribose glycated BSA in vitro

Generation of autoantibodies against glycated fibrinogen: Role in diabetic nephropathy and retinopathy

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Product

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Antiglycation potential of plant based TiO₂ nanoparticle in D‐ribose glycated BSA in vitro