ArticleEuropean biophysics journal : EBJ2013
Ribosylation of bovine serum albumin induces ROS accumulation and cell death in cancer line (MCF-7).
Article in European biophysics journal : EBJ, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 31 citations in OpenAlex.
- Article
- D-Ribose-Induced Glycation and Its Attenuation by the Aqueous Extract ofMedicina (Kaunas, Lithuania) · 2022Article
- Structural and Functional Characterization of Covalently Modified Proteins Formed By a Glycating Agent, Glyoxal.ACS omega · 2021Article
- Understanding the Role of Protein Glycation in the Amyloid Aggregation Process.International journal of molecular sciences · 2021Review
- Increased AGE-RAGE ratio in idiopathic pulmonary fibrosis.Respiratory research · 2016Article
- Aggregation as a consequence of glycation: insight into the pathogenesis of arthritis.European biophysics journal : EBJ · 2016Article
- Glycation in Demetalated Superoxide Dismutase 1 Prevents Amyloid Aggregation and Produces Cytotoxic Ages Adducts.Frontiers in molecular biosciences · 2016Article
- Oxidative Stress Mediated Cytotoxicity of Glycated Albumin: Comparative Analysis of Glycation by Glucose Metabolites.Journal of fluorescence · 2015Article
- Nimbolide Induces ROS-Regulated Apoptosis and Inhibits Cell Migration in Osteosarcoma.International journal of molecular sciences · 2015Article
- Differential effects of glycation on protein aggregation and amyloid formation.Frontiers in molecular biosciences · 2014Review
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Formation of advanced glycation end products (AGE) is crucially involved in the several pathophysiologies associated with ageing and diabetes, for example arthritis, atherosclerosis, chronic renal insufficiency, Alzheimer's disease, nephropathy, neuropathy, and cataracts. Because of devastating effects of AGE and the significance of bovine serum albumin (BSA) as a transport protein, this study was designed to investigate glycation-induced structural modifications in BSA and their functional consequences in breast cancer cell line (MCF-7). We incubated D-ribose with BSA and monitored formation of D-ribose-glycated BSA by observing changes in the intensity of fluorescence at 410 nm. NBT (nitro blue tetrazolium) assay was performed to confirm formation of keto-amine during glycation. Absorbance at 540 nm (fructosamine) increased markedly with time. Furthermore, intrinsic protein and 8-anilino-1-naphthalenesulfonate (ANS) fluorescence revealed marked conformational changes in BSA upon ribosylation. In addition, a fluorescence assay with thioflavin T (ThT) revealed a remarkable increase in fluorescence at 485 nm in the presence of glycated BSA. This suggests that glycation with D-ribose induced aggregation of BSA into amyloid-like deposits. Circular dichroism (CD) study of native and ribosylated BSA revealed molten globule formation in the glycation pathway of BSA. Functional consequences of ribosylated BSA on cancer cell line, MCF-7 was studied by MTT assay and ROS estimation. The results revealed cytotoxicity of ribosylated BSA on MCF-7 cells.
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