Induced release of membrane vesicles from rat adipocytes containing glycosylphosphatidylinositol-anchored microdomain and lipid droplet signalling proteins
Induced release of membrane vesicles from rat adipocytes containing glycosylphosphatidylinositol-anchored microdomain and lipid droplet signalling proteins
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DOI：
10.1016/j.cellsig.2008.10.021
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发表时间：
2009-02-01
影响因子：
4.8
通讯作者：
Kramer, Werner
中科院分区：
文献类型：
--
作者：
Mueller, Guenter;Jung, Christian;Kramer, Werner
哺乳动物脂肪细胞的脂质合成和降解受到胰岛素、脂肪酸、活性氧和药物的密切协调调节。相反，脂肪细胞的脂质生成或脂质分解状态通过可溶性脂肪细胞因子的分泌传递给其他组织。本研究报告了胰岛素、棕榈酸盐、H2O2和抗糖尿病磺酰脲类药物格列美脲诱导大鼠脂肪细胞释放典型的脂滴（LD）蛋白perilipin-A，以及典型的质膜微域（DIGs）蛋白，如caveolin-1和糖基磷脂酰肌醇（GPI）锚定蛋白Gce1和CD73。根据生化和形态学标准，这些LID和gpi蛋白被嵌入两种不同类型的含磷脂膜囊泡中，统称为脂质体。未发现脂肪体释放与细胞裂解或凋亡有因果关系。Gce1和CD73与脂肪体的相互作用显然依赖于它们完整的GPI锚点。caveolin-1、perilipin-A和CD73与磷脂（通过与膜联蛋白v结合）以及caveolin-1与CD73或perilipin-A（通过共免疫沉淀）的相互作用，表明它们在同一脂肪体囊泡内共定位。综上所述，某些增脂剂和抗增脂剂诱导原代大鼠脂肪细胞脂肪体中LD和DIGs蛋白亚群的特异性释放，包括某些gpi蛋白。考虑到(c) Gce1和CD73的amp降解活性以及perilipin-A和caveolin-1的ld形成功能，脂肪细胞释放脂质体的生理相关性可能依赖于脂肪生成和抗脂溶信息的细胞间传递。(c) 2008爱思唯尔公司版权所有。
Synthesis and degradation of lipids in mammalian adipocytes are tightly and coordinatedly regulated by insulin, fatty acids, reactive oxygen species and drugs. Conversely, the lipogenic or lipolytic state of adipocytes is communicated to other tissues by the secretion of soluble adipocytokines. Here we report that insulin, palmitate, H2O2 and the antidiabetic sulfonylurea drug glimepiride induce the release of the typical lipid droplet (LD) protein, perilipin-A, as well as typical plasma membrane microdomain (DIGs) proteins, such as caveolin-1 and the glycosylphosphatidylinositol (GPI)-anchored proteins, Gce1 and CD73 from rat adipocytes. According to biochemical and morphological criteria these LID and GPI-proteins are embedded within two different types of phospholipid-containing membrane vesicles, collectively called adiposomes. Adiposome release was not found to be causally related to cell lysis or apoptosis. The interaction of Gce1 and CD73 with the adiposomes apparently depends on their intact GPI anchor. Pull-down of caveolin-1, perilipin-A and CD73 together with phospholipids (via binding to annexin-V) as well as mutually of caveolin-1 with CD73 or perilipin-A (via coimmunoprecipitation) argues for their colocalization within the same adiposome vesicle.Taken together, certain lipogenic and anti-lipolytic agents induce the specific release of a subset of LD and DIGs proteins, including certain GPI-proteins, in adiposomes from primary rat adipocytes. Given the(c)AMP-degrading activities of Gce1 and CD73 and LD-forming function of perilipin-A and caveolin-1, the physiological relevance of the release of adiposomes from adipocytes may rely on the intercellular transfer of lipogenic and anti-lipolytic information. (c) 2008 Elsevier Inc. All rights reserved.