Characterization of glycation adducts on human serum albumin by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.

Characterization of glycation adducts on human serum albumin by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Research Abstract Details 

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Characterization of glycation adducts on human serum albumin by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Abstract Text:

Chunling Wa,Ronald L Cerny,William A Clarke,David S Hage,Chunling Wa,Ronald L Cerny,William A Clarke,David S Hage,

BACKGROUND: Non-enzymatic glycation of human serum albumin (HSA) is associated with the long-term complications of diabetes. We examined the structure and location of modifications on minimally-glycated HSA and considered their possible impact on the binding of drugs to this protein. METHODS: Minimally-glycated and normal HSA (used as a control) were digested with trypsin, Glu-C or Lys-C, followed by fractionation of the resulting peptides and their analysis by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) to determine the structures and locations of glycation adducts. RESULTS: Several specific lysine and arginine residues were identified as modification sites in minimally-glycated HSA. Residues K12, K51, K199, K205, K439 and K538 were found to be modified through the formation of fructosyl-lysine, while the modification of K159 and K286 involved the formation of pyrraline or N(epsilon)-carboxymethyl-lysine, respectively. Lysine K378 was found to give N(epsilon)-carboxyethyl-lysine in some forms of glycated HSA but fructosyl-lysine in other forms. Residues R160 and R472 produced a modification based on N(epsilon)-(5-hydro-4-imidazolon-2-yl)ornithine. Lysine R222 was modified to produce argpyrimidine, N(epsilon)-[5-(2,3,4-trihydroxybutyl)-5-hydro-4-imidazolon-2-yl]ornithine or tetrahydropyrimidine. CONCLUSIONS: With the exception of K12, K199, K378, K439 and K525, all of the observed sites of modification for minimally-glycated HSA were new to this current study. The fact that many of these glycation-related modifications are located at or near known drug binding sites on HSA explains why some differences have been previously noted in the binding of certain drugs to normal vs glycated HSA.

Characterization of glycation adducts on human serum albumin by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Publishing Authors By Initials

C Wa,RL Cerny,WA Clarke,DS Hage,C Wa,RL Cerny,WA Clarke,DS Hage,

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Characterization of glycation adducts on human serum albumin by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Clinica chimica acta; international journal of cli

VOLUME: 385

Page Numbers: 48-60

Journal Abbreviation: Clin. Chim. Acta

ISSN: 0009-8981

DAY: 23

MONTH: 06

YEAR: 2007

Characterization of glycation adducts on human serum albumin by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Information

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LANGUAGE: eng

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Grant and Affiliation Information for Characterization of glycation adducts on human serum albumin by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.

AFFILIATION: Department of Chemistry, University of Nebraska, Lincoln, NE 68588-0304, United States.

Country: Netherlands

AGENCY: United States NCRR

GRANT: RR015468-001

ACRONYM: RR

MEDLINETA: Clin Chim Acta

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