Institute of Toxicology, Core Unit Proteomics, Hannover Medical School, Carl-Neuberg-Strasse 1, 30625, Hannover, Germany.
Clinic for Pediatric Kidney, Liver and Metabolic Diseases, Hannover Medical School, 30623, Hannover, Germany.
Amino Acids. 2022 Dec;54(12):1611-1619. doi: 10.1007/s00726-022-03197-7. Epub 2022 Aug 17.
We measured free and proteinic concentrations of native and modified amino acids from post-translational modifications (PTMs) and correlated them with the activity of SIRT1 and SIRT3 in the pellet and aqueous phases of human breast milk samples of ten lactating women during the neonatal period. SIRT1 and SIRT3 correlated directly with citrullination, asymmetric dimethylation and glycation of L-arginine, hydroxylation and glycation of L-lysine. SIRT1 and SIRT3 correlated inversely with the hydroxylation of L-proline. SIRT1 and SITR3 tended to correlate inversely with oxidative stress measured as malondialdehyde. Our study suggests that SIRT1 and SIRT3 may modulate PTMs in human breast milk cells.
我们测量了来自翻译后修饰（PTMs）的天然和蛋白质氨基酸的游离和蛋白浓度，并将其与新生儿期 10 位哺乳期妇女母乳样本的颗粒相和水相中的 SIRT1 和 SIRT3 的活性相关联。SIRT1 和 SIRT3 与 L-精氨酸的瓜氨酸化、不对称二甲基化和糖化、L-赖氨酸的羟基化和糖化直接相关。SIRT1 和 SIRT3 与 L-脯氨酸的羟基化呈负相关。SIRT1 和 SITR3 与作为丙二醛测量的氧化应激呈负相关趋势。我们的研究表明，SIRT1 和 SIRT3 可能调节人乳细胞中的 PTMs。
