Zinc-α2-Glycoprotein Modulates AKT-Dependent Insulin Signaling in Human Adipocytes by Activation of the PP2A Phosphatase

• Published in: PloS one Vol. 10; no. 6; p. e0129644
• Main Authors: Ceperuelo-Mallafré, Victòria, Ejarque, Miriam, Duran, Xavier, Pachón, Gisela, Vázquez-Carballo, Ana, Roche, Kelly, Núñez-Roa, Catalina, Garrido-Sánchez, Lourdes, Tinahones, Francisco J., Vendrell, Joan, Fernández-Veledo, Sonia
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 11.06.2015; Public Library of Science (PLoS)
• Subjects: Activation; Adipocytes; Adipocytes - drug effects; Adipocytes - metabolism; Adipose tissue; Adrenergic receptors; Adult; AKT protein; Animal models; Antagonists; Body Mass Index; Carbohydrate metabolism; Carbohydrates; Catalysis; Cells, Cultured; Enzyme Activation; Female; Glucose; Glucose - metabolism; Glucose Transporter Type 1 - genetics; Glucose Transporter Type 1 - metabolism; Glucose Transporter Type 4 - genetics; Glucose Transporter Type 4 - metabolism; Glycoproteins; Humans; Insulin; Insulin - metabolism; Insulin Resistance; Male; Metabolism; Middle Aged; Molecular chains; Molecular modelling; Obesity; Patients; Phosphorylation; Plasma levels; Propranolol; Protein Phosphatase 2 - genetics; Protein Phosphatase 2 - metabolism; Proto-Oncogene Proteins c-akt - metabolism; Seminal Plasma Proteins - blood; Seminal Plasma Proteins - metabolism; Seminal Plasma Proteins - pharmacology; Signal Transduction - drug effects; Signal Transduction - genetics; Signaling; siRNA; Transcriptome; Zinc; Spain

Evidence from mouse models suggests that zinc-α2-glycoprotein (ZAG) is a novel anti-obesity adipokine. In humans, however, data are controversial and its physiological role in adipose tissue (AT) remains unknown. Here we explored the molecular mechanisms by which ZAG regulates carbohydrate metabolis...