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Proprotein Convertases in Health and Disease
New England Journal of Medicine, 2011Proteases that process larger precursor proteins into smaller functional proteins are involved in a wide range of physiologic processes. Derangements in the function of these enzymes play a role in many diseases.
Steven M. Opal, Andrew W. Artenstein
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Proprotein Convertases in Gynecological Cancers
Colloquium Series on Protein Activation and Cancer, 2012ABSTRACT Gynecological cancers include neoplasias of internal female genital organs, mainly ovarian, endometrial and cervical tumors, and cancers of the external female genital structures. Current scientific evidence indicates that both up- and down-regulation of the expression of PCs are part of the multiple changes occurring in these gynecological ...
Andres J. Klein-Szanto +2 more
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Current Opinion in Chemical Biology, 1998
The major endoproteolytic processing enzymes of the secretory pathway are the subtilisin-like proprotein convertases (SPCs). Furin (SPC1) has emerged as one of the major processing enzymes of the constitutive secretory pathway and its localization in the trans-Golgi network and mechanism of autoactivation have been studied in considerable detail ...
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The major endoproteolytic processing enzymes of the secretory pathway are the subtilisin-like proprotein convertases (SPCs). Furin (SPC1) has emerged as one of the major processing enzymes of the constitutive secretory pathway and its localization in the trans-Golgi network and mechanism of autoactivation have been studied in considerable detail ...
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Inhibitors of proprotein convertases
Journal of Molecular Medicine, 2005The discovery of mammalian subtilases, proprotein convertases (PCs) or subtilisin-like proprotein convertases (SPCs), in 1990 was a result of sustained efforts in searching for enzyme/s responsible for maturation of inactive protein precursors. Since then, seven PCs have so far been discovered that cleave at the carboxy-terminal of a basic amino acid ...
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Proprotein convertases in atherogenesis
Current Opinion in Lipidology, 2015The proprotein convertases subtilisin/kexin (PCSKs) are endoproteases identified as activators of precursors from hormones and peptides. On the basis of the variety of substrates and regulation in disease, they have been recognized as mediators in atherogenesis.
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Proprotein convertases: lessons from knockouts
The FASEB Journal, 2006The physiological role of the subtilisin/kexin-like proprotein convertases (PCs) in rodents has been examined through the use of knockout mice. This review will summarize the major in vivo defects that result from the disruption of the expression of their genes.
Fabien Calvo +6 more
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The activation and physiological functions of the proprotein convertases
The International Journal of Biochemistry & Cell Biology, 2008The mammalian secretory proprotein convertases are part of a family of nine serine proteinases of the subtilisin-type. Seven of them cleave after basic amino acids and are called PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7. The two other convertases SKI-1/S1P and PCSK9 are implicated in cholesterol and/or fatty acid metabolism.
Nasha Nassoury +7 more
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Proprotein Convertase PC3 Is Not a Transmembrane Protein
Biochemistry, 2005Proprotein convertase PC3 (also known as PC1) is an endopeptidase involved in proteolytic processing of peptide hormone precursors in granules of the regulated secretory pathway of endocrine cells. Lacking any extended hydrophobic segments, PC3 was considered to be a secretory protein only peripherally attached to the granule membrane.
Stettler, H., Suri, G., Spiess, M.
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FGF23 is processed by proprotein convertases but not by PHEX
Bone, 2004X-linked hypophosphatemia (XLH) and autosomal dominant hypophosphatemic rickets (ADHR) are characterized by renal phosphate wasting, rickets, and osteomalacia. ADHR is caused by gain of function mutations in the fibroblast growth factor 23 gene (FGF23). During secretion, FGF23 is processed at the C-terminus between amino acids 179 and 180. The cleavage
Anna Benet-Pagès +5 more
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Arthritis & Rheumatology, 2019
To determine the safety of proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitors in patients with statin‐associated anti–3‐hydroxy‐3‐methlyglutaryl coenzyme A reductase (anti‐HMGCR)–positive immune‐mediated necrotizing myopathy (IMNM).
E. Tiniakou +3 more
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To determine the safety of proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitors in patients with statin‐associated anti–3‐hydroxy‐3‐methlyglutaryl coenzyme A reductase (anti‐HMGCR)–positive immune‐mediated necrotizing myopathy (IMNM).
E. Tiniakou +3 more
semanticscholar +1 more source