PCSK9: Hepatocyte-specific role dissected

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Familial hypercholesterolemia (FH) is a monogenic genetic disorder that affects in its heterozygous form 1:500 of the population. It is associated with mutations in low-density lipoprotein receptor (LDLR), apolipoprotein B and proprotein convertase subtilisin/kexin type 9 (PCSK9) genes. PCSK9 normally directs lysosomal degradation of LDLR and has been proposed as an attractive target of cholesterol-lowering therapy. In a paper published in Hepatology, Zaid and colleagues analyze the liver-specific role of PCSK9 and reveal its crucial part in liver regeneration. They show that the liver is the major site of expression and source of circulating PCSK9; still extra-hepatic tissues depend on their own expression to regulate LDLR activity. PCSK9 deficiency is also associated with retarded hepatic recovery after partial hepatectomy.

PCSK9 belongs to a family of enzymes responsible for the tissue-specific processing of various precursor proteins including growth factors and neuropeptides. Unlike the other members of the family, it is only involved in its autocatalytic processing and has no other known substrates. By binding on the EGF-A domain of the LDLR, it acts as a chaperone and targets the receptor for degradation [1]. According to previous studies, gain- and loss-of-function mutations in PCSK9 can cause hypercholesterolemia and hypocholesterolemia respectively [2]. Zaid et al. show that PCSK9 is primarily expressed in the liver, within which hepatocytes are the only cell population responsible for its synthesis. Using Cre/loxP recombination they created total (-/-) and hepatocyte-specific (f/f Alb-Cre, Cre under the control of the albumin promoter) knockouts, which allow a closer look at the liver-specific role of PCSK9. This rev...

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