Promotion effect of salt on intramuscular neutral lipid hydrolysis during dry-salting process of porcine (biceps femoris) muscles by inducing phosphorylation of ATGL, HSL and their regulatory proteins of Perilipin1, ABHD5 and G0S2
Promotion effect of salt on intramuscular neutral lipid hydrolysis during dry-salting process of porcine (biceps femoris) muscles by inducing phosphorylation of ATGL, HSL and their regulatory proteins of Perilipin1, ABHD5 and G0S2
复制标题
盐诱导ATGL、HSL及其调节蛋白Perilipin1、ABHD5和G0S2磷酸化对猪（股二头肌）肌肉干盐腌过程中肌内中性脂质水解的促进作用
DOI：
10.1016/j.foodchem.2021.131597
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发表时间：
2021-12-07
期刊：
影响因子：
8.8
通讯作者：
Jin, Guofeng
中科院分区：
文献类型：
--
作者：
Pan, Jiajing;Zhao, Shilin;Jin, Guofeng
为深入了解盐对股二头肌肌内甘油三酯（TG）水解的影响机制，研究了干腌过程中脂肪甘油三酯脂肪酶（ATGL）和激素敏感脂肪酶（HSL）及其调节蛋白的TG水解、TG水解活性和磷酸化水平的变化对不同盐含量（0%、1%、3%、5%）和腌制时间（第1天和第3天）下的Perilipin 1、ABHD 5、G 0 S2进行分析。结果表明，干腌处理显著提高了TG水解酶的活性和水解度（P < 0.05），其中以3%盐处理效果最为显著。SDS-PAGE和Western-blot结果进一步证明，盐对肌内脂肪细胞TG水解的促进作用主要是通过激活蛋白激酶活性和蛋白磷酸化过程实现的。因此，ATGL和HSL被激活，同时，TG水解关键开关perilipin 1也被磷酸化修饰打开。
Towards a better understanding of the formation mechanism of salt on intramuscular triglyceride (TG) hydrolysis occurring in biceps femoris (BF) muscles during dry-salting process, the changes of TG hydrolysis, TG hydrolysis activity and phosphorylation of adipose triglyceride lipase (ATGL) and hormone sensitive lipase (HSL) as well as their regulatory proteins (Perilipin1, ABHD5, G0S2) with different salt content (0%, 1%, 3%, 5%) and salting time (the first and third day) were analyzed. The results showed that dry-salting significantly increased the TG hydrolase activity and hydrolysis extent with salting process proceed (P < 0.05), especially upon the treatment with 3% amount of salt. The SDS-PAGE and Western-blot results further demonstrated that the promotion of salt on TG hydrolysis in intramuscular adipocytes was mainly attributed to the activation of protein kinase activity and protein phosphorylation process. Accordingly, the ATGL and HSL were activated, and meanwhile, the TG hydrolysis pivotal switch perilipin1 was also turned on by phosphorylation modification.