Minireview: Lipid Droplets in Lipogenesis and Lipolysis

脂滴包被蛋白 脂滴 脂肪甘油三酯脂肪酶 脂肪生成 细胞生物学 脂解 脂质代谢 生物 脂肪细胞 脂质氧化 化学 生物化学 脂肪组织 抗氧化剂
作者
Nicole A. Ducharme,Perry E. Bickel
出处
期刊:Endocrinology [The Endocrine Society]
卷期号:149 (3): 942-949 被引量:509
标识
DOI:10.1210/en.2007-1713
摘要

Organisms store energy for later use during times of nutrient scarcity. Excess energy is stored as triacylglycerol in lipid droplets during lipogenesis. When energy is required, the stored triacylglycerol is hydrolyzed via activation of lipolytic pathways. The coordination of lipid storage and utilization is regulated by the perilipin family of lipid droplet coat proteins [perilipin, adipophilin/adipocyte differentiation-related protein (ADRP), S3-12, tail-interacting protein of 47 kilodaltons (TIP47), and myocardial lipid droplet protein (MLDP)/oxidative tissues-enriched PAT protein (OXPAT)/lipid storage droplet protein 5 (LSDP5)]. Lipid droplets are dynamic and heterogeneous in size, location, and protein content. The proteins that coat lipid droplets change during lipid droplet biogenesis and are dependent upon multiple factors, including tissue-specific expression and metabolic state (basal vs. lipogenic vs. lipolytic). New data suggest that proteins previously implicated in vesicle trafficking, including Rabs, soluble N-ethylmaleimide sensitive factor attachment protein receptors (SNAREs), and motor and cytoskeletal proteins, likely orchestrate the movement and fusion of lipid droplets. Thus, rather than inert cytoplasmic inclusions, lipid droplets are now appreciated as dynamic organelles that are critical for management of cellular lipid stores. That much remains to be discovered is suggested by the recent identification of a novel lipase [adipocyte triglyceride lipase (ATGL)] and lipase regulator [Comparative Gene Identification-58 (CGI-58)], which has led to reconsideration of the decades-old model of lipolysis. Future discovery likely will be driven by the exploitation of model organisms and by human genetic studies.
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