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• W4249046397 abstract "Organisms require a continuous energy supply for survival. Mammals store carbohydrates in muscle and liver as glycogen, which can be rapidly mobilized, but also rapidly exhausted, and thus can only sustain an organism for a limited time. A supplementary prolonged energy reserve for the whole-body is stored within adipocytes, the highly specialized cells of adipose tissue. Under conditions of excess nutrient intake, adipocytes store energy as triacylglycerides within intracellular lipid droplets. When energy demand exceeds intake, adipocytes respond by hydrolyzing triacylglycerides, releasing the stored energy into the systemic circulation as free fatty acids and glycerol. The cellular functions that balance adipose energy storage versus release are tightly regulated, where inhibitory and stimulatory cell surface receptors on responsive adipocytes direct a complex interplay among activating and inhibitory intracellular mediators. The lipid droplet surface protein Plin1 serves as a primary functional switch in adipocytes that regulates hydrolytic activity of triacylglycerides, a process often referred to as lipolysis. Differential receptor/transmembrane signaling defines the phosphorylation and regulatory state of Plin1 and adipose lipases. Unphosphorylated Plin1 restricts access of the hydrolytic lipases to lipid droplets to suppress lipolysis, whereas phosphorylated Plin1 recruits activated ATGL and HSL lipases to lipid droplet surfaces. Phosphorylation of Plin1 is, thus, the single most important regulatory factor for lipolysis in adipose cells in vivo, where stimulated cells exhibit 50–100-fold greater lipolytic activity to release stored energy, in comparison to quiescent, unstimulated adipocytes." @default.
• W4249046397 created "2022-05-12" @default.
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• W4249046397 date "2021-01-01" @default.
• W4249046397 modified "2023-09-24" @default.
• W4249046397 title "Lipids | Adipocyte Fat Mobilization: Regulatory Functions Involving Perilipin 1, Adipose Triglyceride Lipase, and Hormone-Sensitive Lipase" @default.
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• W4249046397 doi "https://doi.org/10.1016/b978-0-12-819460-7.00337-6" @default.
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