ArticleThe Biochemical journal2004
Effect of dicarbonyl-induced browning on alpha-crystallin chaperone-like activity: physiological significance and caveats of in vitro aggregation assays.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
33 citing papers in PubMed, 118 citations in OpenAlex.
- Review
- The Role of Immune Cells and Signaling Pathways in Diabetic Eye Disease: A Comprehensive Review.Biomedicines · 2024Review
- Pro-Inflammatory Characteristics of Extracellular Vesicles in the Vitreous of Type 2 Diabetic Patients.Biomedicines · 2024Article
- An overview on glycation: molecular mechanisms, impact on proteins, pathogenesis, and inhibition.Biophysical reviews · 2024Review
- Current Approach to the Pathogenesis of Diabetic Cataracts.International journal of molecular sciences · 2023Review
- Substrate Protein Interactions and Methylglyoxal Modifications Reduce the Aggregation Propensity of Human Alpha-A-Crystallin G98R Mutant.Frontiers in molecular biosciences · 2022Article
- Protein posttranslational modification (PTM) by glycation: Role in lens aging and age-related cataractogenesis.Experimental eye research · 2021Review
- A review on mechanism of inhibition of advanced glycation end products formation by plant derived polyphenolic compounds.Molecular biology reports · 2021Review
- Silk Fibroin/Collagen/Chitosan Scaffolds Cross-Linked by a Glyoxal Solution as Biomaterials toward Bone Tissue Regeneration.Materials (Basel, Switzerland) · 2020Article
- Glyoxal modification mediates conformational alterations in silk fibroin: Induction of fibrillation with amyloidal features.Journal of biosciences · 2020Article
- Review
- Formation of Pentosidine Cross-Linking in Myoglobin by Glyoxal: Detection of Fluorescent Advanced Glycation End Product.Journal of fluorescence · 2017Article
- Oxidative Stress Mediated Cytotoxicity of Glycated Albumin: Comparative Analysis of Glycation by Glucose Metabolites.Journal of fluorescence · 2015Article
- Prevention of protein glycation by natural compounds.Molecules (Basel, Switzerland) · 2015Review
- Advanced glycation end products and diabetic complications.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2014Review
- Ribosylation of bovine serum albumin induces ROS accumulation and cell death in cancer line (MCF-7).European biophysics journal : EBJ · 2013Article
- In vitro study on structural alteration of myoglobin by methylglyoxal.The protein journal · 2013Article
- Molten globule of hemoglobin proceeds into aggregates and advanced glycated end products.PloS one · 2013Article
- The combined effect of acetylation and glycation on the chaperone and anti-apoptotic functions of human α-crystallin.Biochimica et biophysica acta · 2013Article
- Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alpha-crystallin is a member of the small heat-shock protein family and functions like a molecular chaperone, and may thus help in maintaining the transparency of the eye lens by protecting the lens proteins from various stress conditions. Non-enzymic glycation of long-lived proteins has been implicated in several age- and diabetes-related complications, including cataract. Dicarbonyl compounds such as methylglyoxal and glyoxal have been identified as the predominant source for the formation of advanced glycation end-products in various tissues including the lens. We have investigated the effect of non-enzymic browning of alpha-crystallin by reactive dicarbonyls on its molecular chaperone-like function. Non-enzymic browning of bovine alpha-crystallin in vitro caused, along with altered secondary and tertiary structures, cross-linking and high-molecular-mass aggregation. Notwithstanding these structural changes, methylglyoxal- and glyoxal-modified alpha-crystallin showed enhanced anti-aggregation activity in various in vitro aggregation assays. Paradoxically, increased chaperone-like activity of modified alpha-crystallin was not associated with increased surface hydrophobicity and rather showed less 8-anilinonaphthalene-l-sulphonic acid binding. In contrast, the chaperone-like function of modified alpha-crystallin was found to be reduced in assays that monitor the prevention of enzyme inactivation by UV-B and heat. Moreover, incubation of bovine lens with methylglyoxal in organ culture resulted in cataract formation with accumulation of advanced glycation end-products and recovery of alpha-crystallin in high proportions in the insoluble fraction. Furthermore, soluble alpha-crystallin from methylglyoxal-treated lenses showed decreased chaperone-like activity. Thus, in addition to describing the effects of methylglyoxal and glyoxal on structure and chaperone-like activity, our studies also bring out an important caveat of aggregation assays in the context of the chaperone function of alpha-crystallin.
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