The proprotein convertase (PC) PCSK9 is inactivated by furin and/or PC5/6A: functional consequences of natural mutations and post-translational modifications (Q24299848)

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English	The proprotein convertase (PC) PCSK9 is inactivated by furin and/or PC5/6A: functional consequences of natural mutations and post-translational modifications	scientific article

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scholarly article

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The proprotein convertase (PC) PCSK9 is inactivated by furin and/or PC5/6A: functional consequences of natural mutations and post-translational modifications (English)

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Proprotein convertase subtilisin/kexin type 5

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GOA release 2020-03-11

Furin, paired basic amino acid cleaving enzyme

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GOA release 2020-03-11

Proprotein convertase subtilisin/kexin type 9

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GOA release 2020-03-11

signal peptide processing

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GOA release 2020-03-11

object named as

Nabil G Seidah

5

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author name string

Suzanne Benjannet

1

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David Rhainds

2

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Josée Hamelin

3

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Nasha Nassoury

4

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language of work or name

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publication date

13 October 2006

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Journal of Biological Chemistry

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281

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30561-72

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41

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Human and mouse proteases: a comparative genomic approach

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Proprotein and prohormone convertases: a family of subtilases generating diverse bioactive polypeptides

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Precursor convertases in the secretory pathway, cytosol and extracellular milieu

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The secretory proprotein convertase neural apoptosis-regulated convertase 1 (NARC-1): liver regeneration and neuronal differentiation

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Mammalian subtilisin/kexin isozyme SKI-1: A widely expressed proprotein convertase with a unique cleavage specificity and cellular localization

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The proprotein convertases and their implication in sterol and/or lipid metabolism

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NARC-1/PCSK9 and its natural mutants: zymogen cleavage and effects on the low density lipoprotein (LDL) receptor and LDL cholesterol

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Functional characterization of Narc 1, a novel proteinase related to proteinase K

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Proprotein convertases [corrected] are responsible for proteolysis and inactivation of endothelial lipase

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Secreted site-1 protease cleaves peptides corresponding to luminal loop of sterol regulatory element-binding proteins.

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Adenoviral-mediated expression of Pcsk9 in mice results in a low-density lipoprotein receptor knockout phenotype

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Post-transcriptional regulation of low density lipoprotein receptor protein by proprotein convertase subtilisin/kexin type 9a in mouse liver.

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Overexpression of PCSK9 accelerates the degradation of the LDLR in a post-endoplasmic reticulum compartment

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The mystery of PCSK9.

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Mutations in PCSK9 cause autosomal dominant hypercholesterolemia

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Mutations in the PCSK9 gene in Norwegian subjects with autosomal dominant hypercholesterolemia

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A mutation in PCSK9 causing autosomal-dominant hypercholesterolemia in a Utah pedigree

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Novel mutations of the PCSK9 gene cause variable phenotype of autosomal dominant hypercholesterolemia

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Severe hypercholesterolemia in four British families with the D374Y mutation in the PCSK9 gene: long-term follow-up and treatment response

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Low LDL cholesterol in individuals of African descent resulting from frequent nonsense mutations in PCSK9.

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A spectrum of PCSK9 alleles contributes to plasma levels of low-density lipoprotein cholesterol.

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Missense mutations in the PCSK9 gene are associated with hypocholesterolemia and possibly increased response to statin therapy

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Dual regulation of the LDL receptor--some clarity and new questions

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Decreased plasma cholesterol and hypersensitivity to statins in mice lacking Pcsk9

1 reference

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Wild-type PCSK9 inhibits LDL clearance but does not affect apoB-containing lipoprotein production in mouse and cultured cells

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Combined analysis of oligonucleotide microarray data from transgenic and knockout mice identifies direct SREBP target genes

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Statins upregulate PCSK9, the gene encoding the proprotein convertase neural apoptosis-regulated convertase-1 implicated in familial hypercholesterolemia

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Novel putative SREBP and LXR target genes identified by microarray analysis in liver of cholesterol-fed mice

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Effect of mutations in the PCSK9 gene on the cell surface LDL receptors

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Post-translational processing of beta-secretase (beta-amyloid-converting enzyme) and its ectodomain shedding. The pro- and transmembrane/cytosolic domains affect its cellular activity and amyloid-beta production

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Comparative functional role of PC7 and furin in the processing of the HIV envelope glycoprotein gp160

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Alpha1-antitrypsin Portland inhibits processing of precursors mediated by proprotein convertases primarily within the constitutive secretory pathway

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The crystal structure of the proprotein processing proteinase furin explains its stringent specificity

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The prosegments of furin and PC7 as potent inhibitors of proprotein convertases. In vitro and ex vivo assessment of their efficacy and selectivity

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The cysteine-rich domain of the secreted proprotein convertases PC5A and PACE4 functions as a cell surface anchor and interacts with tissue inhibitors of metalloproteinases

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Deletion of the gene encoding proprotein convertase 5/6 causes early embryonic lethality in the mouse

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Furin at the cutting edge: from protein traffic to embryogenesis and disease

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The PC6B cytoplasmic domain contains two acidic clusters that direct sorting to distinct trans-Golgi network/endosomal compartments

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10.1074/JBC.M606495200

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