Dataset Information

Quantification of glycated human serum albumin peptides

ABSTRACT: Human serum albumin is the most abundant plasma protein with a large number of lysine and arginine residues. Hence, it is highly susceptible to glycation in vivo. In hyperglycemic conditions, such as diabetes, the level of HSA glycation increases. Here we quantified glycated HSA peptides in a subject population of healthy and type 2 diabetes with and without nephropathy to assess its performance for the diagnosis of diabetic nephropathy compared to HbA1c.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Plasma

SUBMITTER: Arvindkumar Chaurasiya

LAB HEAD: Mahesh J Kulkarni

PROVIDER: PXD040028 | Pride | 2023-07-20

REPOSITORIES: Pride

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Publications

Elevated Level of Glycated KQTALVELVK Peptide of Albumin Is Associated with the Risk of Diabetic Nephropathy.

Chaurasiya Arvindkumar H AH Jaiswal Meera R MR Bayatigeri Santhakumari S Kahar Shweta S Tiwari Shalbha S Unnikrishnan Ambika G AG Kulkarni Mahesh J MJ

ACS omega 20230601 23

Diabetic nephropathy is a leading cause of end-stage renal disease. Hence, early detection of diabetic nephropathy is essential to mitigate the disease burden. Microalbuminuria, the currently used diagnostic marker of diabetic nephropathy, is not efficient in detecting it at an early stage. Therefore, we explored the utility of glycated human serum albumin (HSA) peptides for risk prediction of diabetic nephropathy. Three glycation-sensitive HSA peptides, namely, FKDLGEENFK, KQTALVELVK, and KVPQV ...[more]

PMID: 37332825

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Project description:Advanced Glycation End-Products (AGEs) are a heterogeneous group of compounds resulting from the non-enzymatic condensation between reducing sugars and amino groups, primarily lysine and arginine moieties (Perrone et al., 2020). The in vivo glycation of proteins is part of normal metabolism, but pathological implications, as well as molecular aging (e.g. protein conformation changes, inflammaging), have been associated with its occurrence (Briceno Noriega et al., 2022). In addition to the important deleterious effects of the endogenous formation of AGEs, the amount acquired from the diet is the subject of concern. In industrial or household cooking processes, the development of appealing aromas, flavors, and colors goes hand-in-hand with the formation of dietary AGEs (dAGEs) (Lund & Ray, 2017). It is well documented that thermally processed foods are a key dietary source of these neo-formed compounds, and high exposure to dAGEs has been associated with the pathogenesis of chronic non-communicable diseases (e.g. diabetes, obesity, and heart failure) (Clarke et al., 2016). Endogenous and dAGEs are thought to exert their pro-inflammatory and pro-oxidative effects at least in part through binding with the Receptor for Advanced Glycation End-products (RAGE) (Nogueira Silva Lima et al., 2021). Our goal here was to compare the efficiency of different reducing agents and carbonyl compounds for dCML fortification of bovine serum albumin (BSA) using a novel combination of quantitative and qualitative methods. Isotope-dilution, high-performance liquid chromatography with tandem mass spectrometric detection (HPLC-MS/MS), western-blot, fluorescence, and proteomics analyses using matrix-assisted laser desorption ionization with time-of-flight MS (MALDI-TOF) and LC with high-resolution MS (LC-HRMS) were all employed to provide an extensive characterization of the possible modifications of BSA promoted by different carbonyl compounds. We further studied the efficiency of the incorporation of protein-bound dCML into mouse feed pellets, their stability over different storage periods, as well as clearance of dCML in mouse feces.

			Action	DRS
	Diabetic.csv	Csv
	Diabetic.zip	Other
	Diabetic_nephropathy.csv	Csv
	Diabetic_nephropathy.zip	Other
	Healthy.csv	Csv