Wolins Nathan E, Brasaemle Dawn L, Bickel Perry E
Department of Medicine, Division of Endocrinology, Metabolism and Lipid Research, Washington University School of Medicine, Saint Louis, MO 63110, USA.
FEBS Lett. 2006 Oct 9;580(23):5484-91. doi: 10.1016/j.febslet.2006.08.040. Epub 2006 Sep 1.
Humans have evolved mechanisms of efficient fat storage to survive famine, but these mechanisms contribute to obesity in our current environment of plentiful food and reduced activity. Little is known about how animals package fat within cells. Five related structural proteins serve roles in packaging fat into lipid droplets. The proteins TIP47, S3-12, and OXPAT/MLDP/PAT-1 move from the cytosol to coat nascent lipid droplets during rapid fat storage. In contrast, perilipin and adipophilin constitutively associate with lipid droplets and play roles in sustained fat storage and regulation of lipolysis. Different tissues express different complements of these lipid droplet proteins. Thus, the tissue-specific complement of these proteins determines how tissues manage lipid stores.
人类已经进化出高效的脂肪储存机制以在饥荒中生存，但在我们当前食物丰富且活动减少的环境中，这些机制却导致了肥胖。关于动物如何在细胞内包装脂肪，我们知之甚少。五种相关的结构蛋白在将脂肪包装成脂滴的过程中发挥作用。在快速脂肪储存期间，TIP47、S3-12和OXPAT/MLDP/PAT-1蛋白从细胞质转移到新生脂滴表面进行包裹。相比之下，围脂滴蛋白和脂肪亲和蛋白持续与脂滴结合，并在持续的脂肪储存和脂解调节中发挥作用。不同组织表达这些脂滴蛋白的不同组合。因此，这些蛋白的组织特异性组合决定了组织如何管理脂质储存。
