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Area of Science:

  • Lipid metabolism and cardiovascular disease genetics.
  • Molecular mechanisms of protein regulation.
  • Gene-environment interactions in metabolic disorders.

Background:

  • The PCSK7 gene, encoding proprotein convertase subtilisin-kexin type-7 (PC7), is located near genes regulating lipoprotein metabolism.
  • Genetic variations in PCSK7 are associated with plasma triglyceride (TG) levels.
  • A specific PC7 variant (R504H) is linked to significantly reduced TG.

Purpose of the Study:

  • To investigate the hypothesis that PC7 regulates apolipoprotein A-V (apoA-V) levels and activity.
  • To elucidate the molecular mechanism by which PC7 influences TG metabolism.
  • To explore the role of PC7 in vivo in the context of a high-fat diet.

Main Methods:

  • Studies in human hepatic (HuH7) cell lines to assess PC7-apoA-V interaction and degradation.
  • In vitro experiments using PC7 mutants and phosphomimetic variants.
  • Analysis of Pcsk7 knockout mice fed a high-fat diet.

Main Results:

  • Wild-type PC7 enhances the lysosomal degradation of apoA-V in hepatic cells.
  • PC7-induced apoA-V degradation is an ER-lysosomal communication process.
  • PC7 phosphorylation at Ser505, influenced by the R504H variant, reduces apoA-V degradation.
  • Pcsk7 knockout mice exhibit increased apoA-V levels and adipocyte lipoprotein lipase (LpL) activity on a high-fat diet.

Conclusions:

  • Liver PC7 promotes apoA-V degradation, thereby lowering plasma triglyceride levels.
  • PC7-mediated apoA-V degradation involves ER-lysosomal transport and is modulated by PC7 phosphorylation.
  • These findings establish an in vivo link between PC7, apoA-V, and TG storage in adipocytes, highlighting PC7 as a potential therapeutic target for hypertriglyceridemia.