We are analyzing https://link.springer.com/article/10.1007/s00109-007-0172-7.

Title:
The proprotein convertases are potential targets in the treatment of dyslipidemia | Journal of Molecular Medicine
Description:
The family of the secretory proprotein convertases (PCs) comprises seven basic amino acid (aa)-specific subtilisin-like serine proteinases known as PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7, and two other PCs, SKI-1 (subtilisin-kexin isozyme-1)/S1P (site-1 protease) and PCSK9 (proprotein convertase subtilisin kexin 9) that cleave at nonbasic residues. Except for the testicular PC4, all the other convertases are expressed in brain and peripheral organs and play a critical role in various functions including the production of diverse neuropeptides as well as growth factors and receptors, the regulation of cellular adhesion/migration, cholesterol and fatty acid homeostasis, and growth/differentiation of progenitor cells. Some of these convertases process proteins that are implicated in pathologies, including cancer malignancies, tissue regeneration, and viral infections. The implication of some of these convertases in sterol/lipid metabolism has only recently been appreciated. SKI-1/S1P activates the synthesis of cholesterol and fatty acids as well as the LDL receptor (LDLR), whereas PCSK9 inactivates the LDLR. Moreover, furin, PC5 and/or, PACE4 inactivates endothelial and lipoprotein lipases. Humans and mice exhibiting either a gain or loss of function of PCSK9 through specific point mutations or knockouts develop hypercholesterolemia and hypocholesterolemia phenotypes, respectively. A PCSK9 inhibitor in combination with statins offers a most promising therapeutic target to treat cardiovascular disorders including dyslipidemias. Specific inhibitors/modulators of the other PCs should find novel therapeutic applications in the control of PC-regulated pathologies.
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Keywords {🔍}

google, scholar, pubmed, cas, article, seidah, proprotein, pcsk, biol, convertase, chretien, convertases, chem, cell, furin, cholesterol, benjannet, mol, processing, regulation, mutations, genet, prat, usa, lipoprotein, mouse, proc, natl, acad, sci, growth, metabolism, ldl, gene, activation, marcinkiewicz, mice, hypercholesterolemia, van, skisp, lipid, hum, basak, human, analysis, protease, cells, receptor, thomas, cleavage,

Topics {✒️}

pdgf-bb involves pi3-kinase/p70 matrix metalloproteinase mt1-mmp/mmp-2 human c-fes/fps reveals pro-platelet-derived growth factor tgf-beta1 involves furin-convertase month download article/chapter low-density lipoprotein cholesterol membrane-bound transcription factor female sib-pair cohort autosomal-dominant hypercholesterolemia related compartment-specfific autoproteolytic removal post-endoplasmic reticulum compartment endoplasmic reticulum/early golgi proprotein convertase ski-1/s1p sterol-regulated luminal protease processing-incompetent cell line subtilisin-kexin isozyme-1 proprotein convertase activity knockouts develop hypercholesterolemia low density lipoprotein full article pdf zymogen cleavage sterol/lipid metabolism growth factor-1 receptor proprotein convertase pc5a basic amino acid atherogenic lipoprotein particles lipoprotein metabolism upregulated subcellular compartments privacy choices/manage cookies human adrenal cortex human ski-1/s1p rat subtilisin/kexin furin proprotein convertase proprotein convertase furin clinical research institute proprotein convertase pcsk9 klein-szanto aj proprotein convertase pc5 candidate processing enzyme convertase ski-1/s1p low ldl cholesterol roebroek aj proprotein convertase family host cellular factor autosomal dominant hypercholesterolemia dyslipidemia review published promising therapeutic target membrane-bound atf6 secretory proprotein convertases

Questions {❓}

Lowering LDL—not only how low, but how long?
Olsson AG (2006) Are lower levels of low-density lipoprotein cholesterol beneficial?

Schema {🗺️}

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         headline:The proprotein convertases are potential targets in the treatment of dyslipidemia
         description:The family of the secretory proprotein convertases (PCs) comprises seven basic amino acid (aa)-specific subtilisin-like serine proteinases known as PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7, and two other PCs, SKI-1 (subtilisin-kexin isozyme-1)/S1P (site-1 protease) and PCSK9 (proprotein convertase subtilisin kexin 9) that cleave at nonbasic residues. Except for the testicular PC4, all the other convertases are expressed in brain and peripheral organs and play a critical role in various functions including the production of diverse neuropeptides as well as growth factors and receptors, the regulation of cellular adhesion/migration, cholesterol and fatty acid homeostasis, and growth/differentiation of progenitor cells. Some of these convertases process proteins that are implicated in pathologies, including cancer malignancies, tissue regeneration, and viral infections. The implication of some of these convertases in sterol/lipid metabolism has only recently been appreciated. SKI-1/S1P activates the synthesis of cholesterol and fatty acids as well as the LDL receptor (LDLR), whereas PCSK9 inactivates the LDLR. Moreover, furin, PC5 and/or, PACE4 inactivates endothelial and lipoprotein lipases. Humans and mice exhibiting either a gain or loss of function of PCSK9 through specific point mutations or knockouts develop hypercholesterolemia and hypocholesterolemia phenotypes, respectively. A PCSK9 inhibitor in combination with statins offers a most promising therapeutic target to treat cardiovascular disorders including dyslipidemias. Specific inhibitors/modulators of the other PCs should find novel therapeutic applications in the control of PC-regulated pathologies.
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            Human Genetics
            Internal Medicine
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         Human mutations
         Mouse knockouts
         Precursor inactivation
         Proprotein convertase
         Subcellular localization
         Zymogen activation
         Molecular Medicine
         Human Genetics
         Internal Medicine
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