共查询到16条相似文献，搜索用时 31 毫秒
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脂肪甘油三酯脂肪酶(ATGL)是脂肪组织中参与脂肪分解的脂肪酶。ATGL也被称为TTS2.2、desnutrin、iPLA2ζ或PN- PLA2,在进化过程中较保守。ATGL拥有特异性的patatin结构域。空腹时ATGL表达上调,重新摄食后表达下降。基础水平、激素刺激和过表达时均可分解甘油三酯,表达被抑制时甘油三酯分解减少。在ob/ob和db/db肥胖小鼠模型中表达量下降,表明其与肥胖、2型糖尿病、胰岛素抵抗和心血管系统疾病等严重疾病的发生可能均有关联。ATGL基因剔除小鼠研究证实其在能量代谢中发挥的重要作用;同时表明ATGL是负责细胞脂肪代谢的重要的甘油三酯脂肪酶。本文综述了ATGL的最新研究进展。 相似文献
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脂肪甘油三酯脂肪酶(ATGL)是近年来研究发现的启动脂肪动员的又一关键脂肪酶. ATGL能特异性地水解甘油三酯(TAG)的第一酯键,被认为是TAG水解过程的限速酶. ATGL在脂肪组织和非脂肪组织脂代谢过程中都发挥着重要作用,其活性和表达在细胞内受到转录水平、翻译后水平等调控.ATGL介导的脂解过程可能与肥胖、糖尿病、脂肪肝等代谢疾病存在关联.本文主要就ATGL的结构特征、生物学功能及其调控机制进行综述,并对今后的研究方向和应用进行了展望. 相似文献
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激素敏感性脂肪酶HSL对生殖系统的整合调控 总被引：1，自引：0，他引：1
激素敏感性脂肪酶被认为是经典的脂肪分解限速酶,可特异水解甘油三酯,受儿茶酚胺等激素调控。近年来研究表明:HSL作用底物不仅有甘油三酯,还包括甘油二酯、甘油一酯、胆固醇酯等。然而,脂肪酶在生殖系统的功能并不清楚,基因敲除小鼠为证实HSL广泛存在于生殖系统提供良好模型,提示其可能在生殖系统生理及病理生理过程发挥重要调节作用,本文将着重介绍生殖系统中HSL基因与蛋白质结构并总结其在生殖系统的功能。 相似文献
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近来基因学方面的研究使人们意识到调控PPARγ的活性保持在一定范围内,能增强胰岛素敏感性的同时,不伴有脂肪的积聚,是治疗代谢综合征的有效策略。首先,分子和细胞学的研究表明PPARγ能够诱导脂肪细胞分化,并且调节与脂肪酸转运和代谢有关基因的转录。其次,人类基因组的研究发现PPARγ获得功能的突变(Pro115Gln)引起PPARγ过度活化,患者显著肥胖,但胰岛素敏感性没有降低。Phe388Leu、Pro467Leu、Arg425Cys的突变引起脂质代谢障碍、脂肪组织转移、严重的胰岛素抵抗。PPARγ活性同脂肪含量呈正相关,而同胰岛素抵抗无正相关性。再… 相似文献
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脂肪组织甘油三酯水解酶参与脂肪分解调控 总被引：2，自引：0，他引：2
循环中游离脂肪酸增高与肥胖、胰岛素抵抗和2型糖尿病密切相关,其主要来源于脂肪细胞内甘油三酯水解.调控脂肪分解的脂肪酶主要包括激素敏感脂肪酶(hormone-sensitive lipase,HSL)和最近发现的脂肪组织甘油三酯水解酶(adipose triglyceride lipase,ATGL),后者主要分布在脂肪组织,特异水解甘油三酯为甘油二酯,其转录水平受多种因素调控.CGI-58(属于α/β水解酶家族蛋白),可以活化ATGL,基础条件下该蛋白和脂滴包被蛋白(perilipin)紧密结合于脂滴表面,蛋白激酶A激活刺激脂肪分解时,CGI-58与perilipin分离,进而活化ATGL. 相似文献
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启动脂肪细胞脂动员过程的新成员ATGL 总被引：3，自引：0，他引：3
过去近20年里,激素敏感脂酶（HSL）一直被认为是脂肪细胞脂动员过程中唯一的脂肪水解限速酶,但随着HSL基因敲除鼠的出现,其限速作用受到了质疑.脂肪甘油三酯脂酶（adipose triglyceride lipase,ATGL)是随后发现的启动脂动员的又一个脂肪分解酶.本文就ATGL基因的结构和功能特征、表达及其调控途径和影响因素等方面的研究进展进行了综述,并对今后的研究方向和应用做了展望. 相似文献
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Meric Erikci Ertunc J?rgen Sikkeland Federico Fenaroli Gareth Griffiths Mathew P. Daniels Haiming Cao Fahri Saatcioglu G?khan S. Hotamisligil 《Journal of lipid research》2015,56(2):423-434
Adipocyte fatty acid binding protein 4, aP2, contributes to the pathogenesis of several common diseases including type 2 diabetes, atherosclerosis, fatty liver disease, asthma, and cancer. Although the biological functions of aP2 have classically been attributed to its intracellular action, recent studies demonstrated that aP2 acts as an adipokine to regulate systemic metabolism. However, the mechanism and regulation of aP2 secretion remain unknown. Here, we demonstrate a specific role for lipase activity in aP2 secretion from adipocytes in vitro and ex vivo. Our results show that chemical inhibition of lipase activity, genetic deficiency of adipose triglyceride lipase and, to a lesser extent, hormone-sensitive lipase blocked aP2 secretion from adipocytes. Increased lipolysis and lipid availability also contributed to aP2 release as determined in perilipin1-deficient adipose tissue explants ex vivo and upon treatment with lipids in vivo and in vitro. In addition, we identify a nonclassical route for aP2 secretion in exosome-like vesicles and show that aP2 is recruited to this pathway upon stimulation of lipolysis. Given the effect of circulating aP2 on glucose metabolism, these data support that targeting aP2 or the lipolysis-dependent secretory pathway may present novel mechanistic and translational opportunities in metabolic disease. 相似文献
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Yutaka Teranishi Atsuo Tanaka Masako Osumi Saburo Fukui 《Bioscience, biotechnology, and biochemistry》2013,77(6):1213-1220
The catalase activities of the Candida cells grown on hydrocarbons were generally much higher than those of the cells grown on Iauryl alcohol, glucose or ethanol. Km values for hydrogen peroxide of the enzymes from the glucose- and the hydrocarbon-grown cells of Candida tropicalis were the same level. The enzyme activities of the yeasts were higher at the exponential growth phase, especially of the hydrocarbon-grown cells, than at the stationary phase. Profuse appearance of microbodies having homogeneous matrix surrounded by a single-layer membrane has also been observed electronmicroscopically in the hydrocarbon- grown cells of several Candida yeasts. Cytochemical studies using 3,3′-diaminobenzidine (DAB) revealed that the catalase activity was located in microbodies. These facts suggest that the catalase activities would be related to the hydrocarbon metabolism in the yeasts. 相似文献
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Lake AC Sun Y Li JL Kim JE Johnson JW Li D Revett T Shih HH Liu W Paulsen JE Gimeno RE 《Journal of lipid research》2005,46(11):2477-2487
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Anita Sahu-Osen Gabriela Montero-Moran Matthias Schittmayer Katarina Fritz Anna Dinh Yu-Fang Chang Derek McMahon Andras Boeszoermenyi Irina Cornaciu Deanna Russell Monika Oberer George M. Carman Ruth Birner-Gruenberger Dawn L. Brasaemle 《Journal of lipid research》2015,56(1):109-121
CGI-58/ABHD5 coactivates adipose triglyceride lipase (ATGL). In adipocytes, CGI-58 binds to perilipin 1A on lipid droplets under basal conditions, preventing interaction with ATGL. Upon activation of protein kinase A (PKA), perilipin 1A is phosphorylated and CGI-58 rapidly disperses into the cytoplasm, enabling lipase coactivation. Because the amino acid sequence of murine CGI-58 has a predicted PKA consensus sequence of RKYS239S240, we hypothesized that phosphorylation of CGI-58 is involved in this process. We show that Ser239 of murine CGI-58 is a substrate for PKA using phosphoamino acid analysis, MS, and immunoblotting approaches to study phosphorylation of recombinant CGI-58 and endogenous CGI-58 of adipose tissue. Phosphorylation of CGI-58 neither increased nor impaired coactivation of ATGL in vitro. Moreover, Ser239 was not required for CGI-58 function to increase triacylglycerol turnover in human neutral lipid storage disorder fibroblasts that lack endogenous CGI-58. Both CGI-58 and S239A/S240A-mutated CGI-58 localized to perilipin 1A-coated lipid droplets in cells. When PKA was activated, WT CGI-58 dispersed into the cytoplasm, whereas substantial S239A/S240A-mutated CGI-58 remained on lipid droplets. Perilipin phosphorylation also contributed to CGI-58 dispersion. PKA-mediated phosphorylation of CGI-58 is required for dispersion of CGI-58 from perilipin 1A-coated lipid droplets, thereby increasing CGI-58 availability for ATGL coactivation. 相似文献
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Brasaemle DL 《Journal of lipid research》2007,48(12):2547-2559
The majority of eukaryotic cells synthesize neutral lipids and package them into cytosolic lipid droplets. In vertebrates, triacylglycerol-rich lipid droplets of adipocytes provide a major energy storage depot for the body, whereas cholesteryl ester-rich droplets of many other cells provide building materials for local membrane synthesis and repair. These lipid droplets are coated with one or more of five members of the perilipin family of proteins: adipophilin, TIP47, OXPAT/MLDP, S3-12, and perilipin. Members of this family share varying levels of sequence similarity, lipid droplet association, and functions in stabilizing lipid droplets. The most highly studied member of the family, perilipin, is the most abundant protein on the surfaces of adipocyte lipid droplets, and the major substrate for cAMP-dependent protein kinase [protein kinase A (PKA)] in lipolytically stimulated adipocytes. Perilipin serves important functions in the regulation of basal and hormonally stimulated lipolysis. Under basal conditions, perilipin restricts the access of cytosolic lipases to lipid droplets and thus promotes triacylglycerol storage. In times of energy deficit, perilipin is phosphorylated by PKA and facilitates maximal lipolysis by hormone-sensitive lipase and adipose triglyceride lipase. A model is discussed whereby perilipin serves as a dynamic scaffold to coordinate the access of enzymes to the lipid droplet in a manner that is responsive to the metabolic status of the adipocyte. 相似文献