在白色脂肪组织的脂肪细胞(Adipocyte)中，PKA可以活化脂肪酶E(HSL)，促进将储存的甘油三酯水解为游离脂肪酸，发挥脂类分解作用(Lypolysis)。这是脂肪细胞释放储存的能量的主要途径。

HSL can be regulated by reversible phosphorylation; the evidence shows that HSL in adipocytes could be phosphorylated and activated by the cAMP-dependent protein kinase (PKA) in response to catabolic hormones such as corticotropin-releasing …

2024年1月12日 · Adipose tissue lipolysis is mediated by cAMP–protein kinase A (PKA)-dependent intracellular signalling. Here, we show that PKA targets p21-activated kinase 4 (PAK4), leading to its protein...

Consistent with this finding, the phosphorylation state of an established common effector of PKA and AMPK in the regulation of lipolysis, HSL, changed accordingly. Conditions that activated PKA-induced phosphorylation of HSL at Ser-660 and Ser-563 and suppressed phosphorylation of HSL at the AMPK site Ser-565 .

2001年11月30日 · Hormonally stimulated lipolysis occurs by activation of cyclic AMP-dependent protein kinase (PKA) which phosphorylates hormone-sensitive lipase (HSL) and increases adipocyte lipolysis. Evidence suggests that catecholamines not only can activate PKA, but also the mitogen-activated protein kinase pathway and extracellular signal-regulated kinase ...

Hormone-sensitive lipase (EC 3.1.1.79; HSL) is a key enzyme in the mobilization of fatty acids from stored triacylglycerols. HSL activity is controlled by phosphorylation of at least four serines. In rat HSL, Ser563, Ser659 and Ser660 are phosphorylated by protein kinase A …

HSL (hormone-sensitive lipase) is a key enzyme in the mobilization of fatty acids from acylglycerols in adipocytes as well as non-adipocytes. In adipocytes, catecholamines stimulate lipolysis mainly through PKA (protein kinase A)-mediated phosphorylation of HSL and perilipin, a protein coating the l …

2021年4月1日 · In the present study, we analyzed dynamic posttranslational modifications of HSL mediated by PKA and AMP-activated protein kinase (AMPK) as well as their effects on steroidogenesis in luteal cells. Our results revealed that AMPK acutely inhibits the stimulatory effects of LH/PKA on progesterone production without reducing levels of STAR ...

AMPK evoked inhibitory phosphorylation of HSL (Ser565). In contrast, LH/PKA decreased phosphorylation of AMPK at Thr172, a residue required for its activation. Additionally, LH/PKA increased phosphorylation of HSL at Ser563, which is crucial for enzyme activation, and decreased inhibitory phosphorylation of HSL at Ser565.

2021年4月1日 · HSL interacts with different LD-associated proteins, notably perilipins. In the basal state, perilipin 1 reduces the access of endogenous lipases to store lipids. Upon stimulated lipolysis, perilipin 1 is phosphorylated by PKA or PKG, allowing HSL/perilipin 1 interaction and thus HSL translocation at the LD surface [114].