2019

Scientific Reports

Rocznik: 2019 | Tom: 9

artykuł naukowy

angielski

EN The modification of protein lysine residues by the thioester homocysteine (Hcy)-thiolactone has been implicated in cardiovascular and neurodegenerative diseases. However, only a handful of proteins carrying Hcy on specific lysine residues have been identified and quantified in humans or animals. In the present work, we developed a liquid chromatography/ mass spectrometry targeted assay, based on multiple reaction monitoring, for quantification of N-Hcy-Lys212 (K212Hcy) and N-Hcy-Lys525 (K525Hcy) sites in serum albumin in mice. Using this assay, we found that female (n = 20) and male (n = 13) Cbs(-/-) mice had significantly elevated levels of K212Hcy and K525Hcy modifications in serum albumin relative to their female (n = 19) and male (n = 17) Cbs(+/-) littermates. There was significantly more K212Hcy modification in Cbs(-/-) males than in Cbs(-/-) females (5.78 +/- 4.21 vs. 3.15 +/- 1.38 units, P = 0.023). Higher K212Hcy levels in males than in females were observed also in Cbs(+/-) mice (2.72 +/- 0.81 vs. 1.89 +/- 1.07 units, P = 0.008). In contrast, levels of the K525Hcy albumin modification were similar between males and females, both in Cbs(-/-) and Cbs(+/-) mice. These findings suggest that the sex-specific K212Hcy modification in albumin might have an important biological function in mice that is not affected by the Cbs genotype.

2669

10.1038/s41598-019-38784-4

http://www.nature.com/articles/s41598-019-38784-4

CC BY-ND (uznanie autorstwa - bez utworów zależnych)

ostateczna wersja opublikowana

02.2019

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