An autophagy-enhancing drug promotes degradation of mutant alpha1-antitrypsin Z and reduces hepatic fibrosis

Science. 2010 Jul 9;329(5988):229-32. doi: 10.1126/science.1190354. Epub 2010 Jun 3.

Abstract

In the classical form of alpha1-antitrypsin (AT) deficiency, a point mutation in AT alters the folding of a liver-derived secretory glycoprotein and renders it aggregation-prone. In addition to decreased serum concentrations of AT, the disorder is characterized by accumulation of the mutant alpha1-antitrypsin Z (ATZ) variant inside cells, causing hepatic fibrosis and/or carcinogenesis by a gain-of-toxic function mechanism. The proteasomal and autophagic pathways are known to mediate degradation of ATZ. Here we show that the autophagy-enhancing drug carbamazepine (CBZ) decreased the hepatic load of ATZ and hepatic fibrosis in a mouse model of AT deficiency-associated liver disease. These results provide a basis for testing CBZ, which has an extensive clinical safety profile, in patients with AT deficiency and also provide a proof of principle for therapeutic use of autophagy enhancers.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Autophagy / drug effects*
  • Carbamazepine / administration & dosage
  • Carbamazepine / pharmacology*
  • Carbamazepine / therapeutic use
  • Cell Line
  • Disease Models, Animal
  • Endoplasmic Reticulum / metabolism
  • HeLa Cells
  • Humans
  • Liver / drug effects
  • Liver / metabolism*
  • Liver / pathology
  • Liver Cirrhosis / drug therapy*
  • Liver Cirrhosis / etiology
  • Liver Cirrhosis / metabolism
  • Liver Cirrhosis / pathology
  • Mice
  • Mice, Transgenic
  • Mutant Proteins / chemistry
  • Mutant Proteins / metabolism
  • Phagosomes / drug effects
  • Phagosomes / ultrastructure
  • Phenotype
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Folding
  • Solubility
  • alpha 1-Antitrypsin / chemistry
  • alpha 1-Antitrypsin / genetics
  • alpha 1-Antitrypsin / metabolism*
  • alpha 1-Antitrypsin Deficiency / complications
  • alpha 1-Antitrypsin Deficiency / metabolism*
  • alpha 1-Antitrypsin Deficiency / pathology

Substances

  • Mutant Proteins
  • alpha 1-Antitrypsin
  • Carbamazepine
  • Proteasome Endopeptidase Complex