title: The adipokine zinc-α2-glycoprotein activates AMP kinase in human primary skeletal muscle cells.
abstract: BACKGROUND
  Zinc-α2-glycoprotein (ZAG) induces lipid mobilization in adipose tissue (AT) and stimulates energy utilization in AT and skeletal muscle by up-regulation of UCP isoforms and GLUT4.
  
  
  OBJECTIVE
  Our study aimed to investigate whether ZAG activates AMPKα, an important regulator of energy metabolism, in human skeletal muscle cells (SkMc).
  
  
  METHODS
  SkMc were treated with recombinant ZAG, and activation of AMPKα and ACC, protein abundance of GLUT4, and UCP2 and UCP3 gene expression were analysed.
  
  
  RESULTS
  Treatment of SkMc with ZAG induced short-time phosphorylation of AMPKα and ACC. Furthermore, AMPKα phosphorylation was elevated after 24 h, while for ACC no activation was observed. GLUT4 level was increased by 1.3-fold. However, UCP2 and UCP3 expression remained unaltered.
  
  
  CONCLUSIONS
  These results show that ZAG leads to phosphorylation of AMPKα and ACC, thereby activating a pathway central to the regulation of energy metabolism. This mechanism may be involved in mediating the effects of ZAG in relation to increased energy utilization.
authors: Institute of Clinical Biochemistry and Pathobiochemistry, German Diabetes Center, Duesseldorf, Germany. Kristin.Eckardt@ddz.uni-duesseldorf.de
authors: Kristin
authors: K
authors: Eckardt
authors: Annette
authors: A
authors: Schober
authors: Birgit
authors: B
authors: Platzbecker
authors: Tomas
authors: T
authors: Mracek
authors: Chen
authors: C
authors: Bing
authors: Paul
authors: P
authors: Trayhurn
authors: Juergen
authors: J
authors: Eckel
mesh_terms: D000103:Acetyl-CoA Carboxylase / Q000235:genetics / Q000378:metabolism; D000263:Adenylate Kinase / Q000235:genetics / Q000378:metabolism*; D054392:Adipokines / Q000235:genetics / Q000378:metabolism*; D000293:Adolescent; D000328:Adult; D015153:Blotting, Western; D018929:Cell Culture Techniques; D004591:Electrophoresis, Polyacrylamide Gel; D004734:Energy Metabolism / Q000502:physiology; D005260:Female; D015870:Gene Expression; D051275:Glucose Transporter Type 4 / Q000235:genetics / Q000378:metabolism; D057809:HEK293 Cells; D006801:Humans; D007473:Ion Channels / Q000235:genetics / Q000378:metabolism; D008297:Male; D024101:Mitochondrial Proteins / Q000235:genetics / Q000378:metabolism; D018482:Muscle, Skeletal / Q000166:cytology / Q000378:metabolism; D010766:Phosphorylation / Q000187:drug effects; D012333:RNA, Messenger / Q000032:analysis / Q000096:biosynthesis; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D029589:Seminal Plasma Proteins / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology*; D015398:Signal Transduction / Q000235:genetics; D000071246:Uncoupling Protein 2; D000071247:Uncoupling Protein 3; D015854:Up-Regulation / Q000187:drug effects; D055815:Young Adult; D000090203:Zn-Alpha-2-Glycoprotein
chemical_list: D054392:Adipokines; D051275:Glucose Transporter Type 4; D007473:Ion Channels; D024101:Mitochondrial Proteins; D012333:RNA, Messenger; D011994:Recombinant Proteins; C495692:SLC2A4 protein, human; D029589:Seminal Plasma Proteins; C000604389:UCP2 protein, human; C000604392:UCP3 protein, human; D000071246:Uncoupling Protein 2; D000071247:Uncoupling Protein 3; D000090203:Zn-Alpha-2-Glycoprotein; D000263:Adenylate Kinase; D000103:Acetyl-CoA Carboxylase