Ex vivo instability of glycated albumin: A role for autoxidative glycation.

Abstract:

:Ex vivo protein modifications occur within plasma and serum (P/S) samples due to prolonged exposure to the thawed state-which includes temperatures above -30 °C. Herein, the ex vivo glycation of human serum albumin from healthy and diabetic subjects was monitored in P/S samples stored for hours to months at -80 °C, -20 °C, and room temperature, as well as in samples subjected to multiple freeze-thaw cycles, incubated at different surface area-to-volume ratios or under different atmospheric compositions. A simple dilute-and-shoot method utilizing trap-and-elute LC-ESI-MS was employed to determine the relative abundances of the glycated forms of albumin-including forms of albumin bearing more than one glucose molecule. Significant increases in glycated albumin were found to occur within hours at room temperature, and within days at -20 °C. These increases continued over a period of 1-2 weeks at room temperature and over 200 days at -20 °C, ultimately resulting in a doubling of glycated albumin in both healthy and diabetic patients. It was also shown that samples stored at lower surface area-to-volume ratios or incubated under a nitrogen atmosphere experienced less rapid glucose adduction of albumin-suggesting a role for oxidative glycation in the ex vivo glycation of albumin.

journal_name

Arch Biochem Biophys

authors

Jeffs JW,Ferdosi S,Yassine HN,Borges CR

doi

10.1016/j.abb.2017.07.004

subject

Has Abstract

pub_date

2017-09-01 00:00:00

pages

36-42

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(17)30340-5

journal_volume

629

pub_type

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