Development of Diagnostic Fragment Ion Library for Glycated Peptides of Human Serum Albumin: Targeted Quantification in Prediabetic, Diabetic, and Microalbuminuria Plasma by Parallel Reaction Monitoring, SWATH, and MSE.

Autor:	Korwar AM; From the §Mass-Spectrometry and Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India.;, Vannuruswamy G; From the §Mass-Spectrometry and Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India.;, Jagadeeshaprasad MG; From the §Mass-Spectrometry and Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India.;, Jayaramaiah RH; From the §Mass-Spectrometry and Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India.;, Bhat S; From the §Mass-Spectrometry and Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India.;, Regin BS; ‡Madras Diabetes Research Foundation, Chennai- 600 086, India., Ramaswamy S; From the §Mass-Spectrometry and Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India.;, Giri AP; From the §Mass-Spectrometry and Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India.;, Mohan V; ‡Madras Diabetes Research Foundation, Chennai- 600 086, India., Balasubramanyam M; ‡Madras Diabetes Research Foundation, Chennai- 600 086, India., Kulkarni MJ; From the §Mass-Spectrometry and Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India.; mj.kulkarni@ncl.res.in.
Jazyk:	angličtina
Zdroj:	Molecular & cellular proteomics : MCP [Mol Cell Proteomics] 2015 Aug; Vol. 14 (8), pp. 2150-9. Date of Electronic Publication: 2015 May 28.
DOI:	10.1074/mcp.M115.050518
Abstrakt:	Human serum albumin is one of the most abundant plasma proteins that readily undergoes glycation, thus glycated albumin has been suggested as an additional marker for monitoring glycemic status. Hitherto, only Amadori-modified peptides of albumin were quantified. In this study, we report the construction of fragment ion library for Amadori-modified lysine (AML), N(ε)-(carboxymethyl)lysine (CML)-, and N(ε)-(carboxyethyl)lysine (CEL)-modified peptides of the corresponding synthetically modified albumin using high resolution accurate mass spectrometry (HR/AM). The glycated peptides were manually inspected and validated for their modification. Further, the fragment ion library was used for quantification of glycated peptides of albumin in the context of diabetes. Targeted Sequential Window Acquisition of all THeoretical Mass Spectra (SWATH) analysis in pooled plasma samples of control, prediabetes, diabetes, and microalbuminuria, has led to identification and quantification of 13 glycated peptides comprised of four AML, seven CML, and two CEL modifications, representing nine lysine sites of albumin. Five lysine sites namely K549, K438, K490, K88, and K375, were observed to be highly sensitive for glycation modification as their respective m/z showed maximum fold change and had both AML and CML modifications. Thus, peptides involving these lysine sites could be potential novel markers to assess the degree of glycation in diabetes. (© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.)
Databáze:	MEDLINE
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