Nonenzymatic glycation alters protein structure and stability. A study of two eye lens crystallins.

Luthra, Manni; Balasubramanian, D.

doi:10.1016/s0021-9258(17)46819-0

Cited by 118 publications

(13 citation statements)

References 47 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This observation is in agreement with the results of previous study suggesting that glycation in general improves the conformational stability of protein [43].…”

Section: Aggregation Propensity Of the Glycated And Non-glycated Lens Crystallins Under Stress Conditionssupporting

confidence: 94%

“…3C, while glycation of lens α-Cry results in significant increment in the ellipticity value of this band, only a little variation was observed between CD signal intensities of glycated and non-glycated TSPs. In fact, circular dichroism spectroscopy revealed that glycation increases β-sheet content of α-Cry to a significant level which is in agreement with the result of previous report [43]. Due to non-enzymatic glycation, while beta-sheet content of α-Cry increases from 34.45 to 40.36; the alpha-helix content of this protein indicates an important reduction from 9.05 to 5.92.…”

Section: ►Fig3 To Be Inserted Here◄supporting

confidence: 91%

“…Glycation has been already indicated to increase conformational stability against chemically induced denaturation [43]. In order to determine the impact of glycation on structural stability of TSPs and α-Cry, the conformational stability of different crystallin samples was investigated, using chemical unfolding method.…”

Section: Comparing Stability Of the Glycated And Non-glycated Forms Of Tsps And α-Crymentioning

confidence: 99%

See 2 more Smart Citations

Assessment of structure, stability and aggregation of soluble lens proteins and alpha-crystallin upon non-enzymatic glycation: The pathomechanisms underlying cataract development in diabetic patients

Yousefi

Javadi

Amirghofran

et al. 2016

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

Total soluble lens proteins (TSPs) and α-crystallin (α-Cry) were individually subjected to the long-term glycation in the presence of d-glucose. The glycated and non-glycated protein counterparts were incubated under different stress conditions and compared according to their structure, stability and aggregation propensity by various spectroscopic techniques and gel mobility shift analyses. Extensive glycation of the lens proteins was accompanied with structural alteration, reduction in their surface hydrophobicity and increment of their surface tension. Our results suggest that glycation causes lens crystallins to partially resist against structural alteration and aggregation/fibrillation under both thermal and thermochemical systems. The conformational stability of lens crystallins was increased upon glycation, showing the reason behind resistance of glycated proteins against stress-induced structural alteration and aggregation. Due to the resistance of glycated lens crystallins against aggregation, the role of this modification in development of senile cataract can be explained with the associated damaging consequences highlighted in this article.

show abstract

“…This observation is in agreement with the results of previous study suggesting that glycation in general improves the conformational stability of protein [43].…”

Section: Aggregation Propensity Of the Glycated And Non-glycated Lens Crystallins Under Stress Conditionssupporting

confidence: 94%

Section: ►Fig3 To Be Inserted Here◄supporting

confidence: 91%

Section: Comparing Stability Of the Glycated And Non-glycated Forms Of Tsps And α-Crymentioning

confidence: 99%

See 1 more Smart Citation

Assessment of structure, stability and aggregation of soluble lens proteins and alpha-crystallin upon non-enzymatic glycation: The pathomechanisms underlying cataract development in diabetic patients

Yousefi

Javadi

Amirghofran

et al. 2016

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

show abstract

“…Glycation of proteins eventualize in a complex series of reactions known as Maillard reactions [5] which terminate in the form of stable irreversibly misfolded adducts -the Advanced Glycation End (AGE) products [6]. Glycation has been associated with severely altered structure and functionality of native proteins [7] including formation of covalent cross-links with nearby proteins [8]. AGE formation and accumulation has a diverse spectrum of diseases encompassing several physiological maladies such as arteriosclerosis, renal failure, diabetic complications and Alzheimer disease [9].…”

Section: Introductionmentioning

confidence: 99%

Ribosylation induced structural changes in Bovine Serum Albumin: understanding high dietary sugar induced protein aggregation and amyloid formation

Das

Basak

Pramanik

et al. 2020

Heliyon

View full text Add to dashboard Cite

Non-enzymatic glycation of proteins is believed to be the root cause of high dietary sugar associated pathophysiological maladies. We investigated the structural changes in protein during progression of glycation using ribosylated Bovine Serum Albumin (BSA). Non enzymatic attachment of about 45 ribose molecules to BSA resulted in gradual reduction of hydrophobicity and aggregation as indicated by red-shifted tryptophan fluorescence, reduced ANS binding and lower anisotropy of FITC-conjugated protein. Parallely, there was a significant decrease of alpha helicity as revealed by Circular Dichroism (CD) and Fourier transformed-Infra Red (FT-IR) spectra. The glycated proteins assumed compact globular structures with enhanced Thioflavin-T binding resembling amyloids. The gross structural transition affected by ribosylation led to enhanced thermostability as indicated by melting temperature and Transmission Electron Microscopy. At a later stage of glycation, the glycated proteins developed non-specific aggregates with increase in size and loss of amyloidogenic behaviour. A parallel non-glycated control incubated under similar conditions indicated that amyloid formation and associated changes were specific for ribosylation and not driven by thermal denaturation due to incubation at 37 °C. Functionality of the glycated protein was significantly altered as probed by Isothermal Titration Calorimetry using polyphenols as substrates. The studies demonstrated that glycation driven globular amyloids form and persist as transient intermediates during formation of misfolded glycated adducts. To the best of our knowledge, the present study is the first systematic attempt to understand glycation associated changes in a protein and provides important insights towards designing therapeutics for arresting dietary sugar induced amyloid formation.

show abstract

“…Age related modifications of -crystallin induce alterations in lens crystallin interactions, which can be responsible for the increase in light scattering in old and cataractous lenses [18][19][20][21]. Alterations include both changes in the secondary structure and in the state of aggregation [22], [23].…”

mentioning

confidence: 99%

Mimicking cataract-induced visual dysfunction by means of protein denaturation in egg albumen

2016

View full text Add to dashboard Cite

Received XX Month XXXX; revised XX Month, XXXX; accepted XX Month XXXX; posted XX Month XXXX (Doc. ID XXXXX); published XX Month XXXX As the world's population ages, cataract-induced visual dysfunction and blindness is on the increase. This is a significant global problem. The most common symptoms of cataracts are glared and blurred vision. Usually, people with cataract have trouble seeing or reading at distance or in low light and also their color perception is altered. Furthermore, cataract is a sneaky disease as it is usually a very slow but progressive process, which creates adaptation so that patients find it difficult to recognize. Moreover, for the doctors it can be very difficult to explain and give comprehensive answers to the patients' symptoms. We built and tested an optic device that uses egg albumen to mimic the optical degradation of the crystalline related cataracts and that is able to visualize how the cataract impairs vision. At best of our knowledge, it is the first experimental system developed at this aim. This can be a valuable tool, which can be of help in education for students in medical sciences as well as to provide a method to illustrate the patients how their vision is affected by cataract progression process.

show abstract

Nonenzymatic glycation alters protein structure and stability. A study of two eye lens crystallins.

Cited by 118 publications

References 47 publications

Assessment of structure, stability and aggregation of soluble lens proteins and alpha-crystallin upon non-enzymatic glycation: The pathomechanisms underlying cataract development in diabetic patients

Assessment of structure, stability and aggregation of soluble lens proteins and alpha-crystallin upon non-enzymatic glycation: The pathomechanisms underlying cataract development in diabetic patients

Ribosylation induced structural changes in Bovine Serum Albumin: understanding high dietary sugar induced protein aggregation and amyloid formation

Mimicking cataract-induced visual dysfunction by means of protein denaturation in egg albumen

Contact Info

Product

Resources

About