脂连蛋白(英语:adiponectin,亦称为脂联素)是一种主要由脂肪细胞分泌的蛋白质激素,由ADIPOQ基因所编码[5],含244个氨基酸。成人体内的脂联素水平与脂肪储量负相关[来源请求]

脂联素
已知的结构
PDB直系同源搜索: PDBe RCSB
识别号
别名ADIPOQ;, ACDC, ACRP30, ADIPQTL1, ADPN, APM-1, APM1, GBP28, adiponectin, C1Q and collagen domain containing, Adiponectin
外部IDOMIM605441 MGI106675 HomoloGene3525 GeneCardsADIPOQ
基因位置(人类
3号染色体
染色体3号染色体[1]
3号染色体
脂联素的基因位置
脂联素的基因位置
基因座3q27.3起始186,842,704 bp[1]
终止186,858,463 bp[1]
RNA表达模式
查阅更多表达数据
直系同源
物种人类小鼠
Entrez
Ensembl
UniProt
mRNA​序列

NM_001177800
​NM_004797

NM_009605

蛋白序列

NP_001171271
​NP_004788

NP_033735

基因位置​(UCSC)Chr 3: 186.84 – 186.86 MbChr 16: 22.97 – 22.98 Mb
PubMed​查找[3][4]
维基数据
查看/编辑人类查看/编辑小鼠

结构

脂联素包含244个氨基酸,可分为4个结构域。从其N端起算,第一个是使其定位于细胞外的信号序列,第二个区域较短且在物种间高度变异,第三个65个氨基酸的区域与胶原蛋白相似,最后一个是脂联素的球状结构域。总的上看,这一蛋白与补体片段C1q英语C1q相似。其中球状结构域的三维结构已经测定,结构上与TNFα非常相似,但在氨基酸序列上却差异巨大[6]

受体

脂联素可与几种受体结合,两种受体与G蛋白偶联受体同源性,一种属于钙粘蛋白家族[7][8]

这些受体影响下游靶标AMP激酶英语AMP-activated protein kinase,这是一个重要的细胞代谢率控制点。受体的表达与胰岛素水平相关,并且在糖尿病小鼠模型中降低,特别是在骨骼肌和脂肪组织中[9][10]

参考文献

  1. ^ 1.0 1.1 1.2 GRCh38: Ensembl release 89: ENSG00000181092 - Ensembl, May 2017
  2. ^ 2.0 2.1 2.2 GRCm38: Ensembl release 89: ENSMUSG00000022878 - Ensembl, May 2017
  3. ^ Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine. 
  4. ^ Mouse PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine. 
  5. ^ Maeda K, Okubo K, Shimomura I, Funahashi T, Matsuzawa Y, Matsubara K. cDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose Most abundant Gene transcript 1). Biochem. Biophys. Res. Commun. April 1996, 221 (2): 286–9. PMID 8619847. doi:10.1006/bbrc.1996.0587. 
  6. ^ Shapiro L, Scherer PE. The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor. Curr. Biol. March 1998, 8 (6): 335–8. PMID 9512423. doi:10.1016/S0960-9822(98)70133-2. 
  7. ^ Yamauchi T, Kamon J, Ito Y, Tsuchida A, Yokomizo T, Kita S, Sugiyama T, Miyagishi M, Hara K, Tsunoda M, Murakami K, Ohteki T, Uchida S, Takekawa S, Waki H, Tsuno NH, Shibata Y, Terauchi Y, Froguel P, Tobe K, Koyasu S, Taira K, Kitamura T, Shimizu T, Nagai R, Kadowaki T. Cloning of adiponectin receptors that mediate antidiabetic metabolic effects. Nature. 2003, 423 (6941): 762–9. PMID 12802337. doi:10.1038/nature01705. 
  8. ^ Hug C, Wang J, Ahmad NS, Bogan JS, Tsao TS, Lodish HF. T-cadherin is a receptor for hexameric and high-molecular-weight forms of Acrp30/adiponectin. Proc. Natl. Acad. Sci. U.S.A. 2004, 101 (28): 10308–13. PMC 478568 . PMID 15210937. doi:10.1073/pnas.0403382101. 
  9. ^ Fang X, Sweeney G. Mechanisms regulating energy metabolism by adiponectin in obesity and diabetes. Biochem. Soc. Trans. 2006, 34 (Pt 5): 798–801. PMID 17052201. doi:10.1042/BST0340798. 
  10. ^ Bonnard C, Durand A, Vidal H, Rieusset J. Changes in adiponectin, its receptors and AMPK activity in tissues of diet-induced diabetic mice. Diabetes Metab. 2008, 34 (1): 52–61. PMID 18222103. doi:10.1016/j.diabet.2007.09.006.