Results 151 to 160 of about 17,066 (197)

Inhibitors of proprotein convertases

Journal of Molecular Medicine, 2005
The 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, 2015
The 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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The activation and physiological functions of the proprotein convertases

The International Journal of Biochemistry & Cell Biology, 2008
The 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.
Nabil G, Seidah, Gaetan, Mayer, Ahmed, Zaid, Estelle, Rousselet, Nasha, Nassoury, Steve, Poirier, Rachid, Essalmani, Annik, Prat   +7 more
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FGF23 is processed by proprotein convertases but not by PHEX

Bone, 2004
X-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, Bettina, Lorenz-Depiereux, Hans, Zischka, Kenneth E, White, Michael J, Econs, Tim M, Strom   +5 more
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The biology and therapeutic targeting of the proprotein convertases

Nature Reviews Drug Discovery, 2012
The mammalian proprotein convertases constitute a family of nine secretory serine proteases that are related to bacterial subtilisin and yeast kexin. Seven of these (proprotein convertase 1 (PC1), PC2, furin, PC4, PC5, paired basic amino acid cleaving enzyme 4 (PACE4) and PC7) activate cellular and pathogenic precursor proteins by cleavage at single or
Nabil G, Seidah, Annik, Prat
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Characterization of proADAMTS5 processing by proprotein convertases

The International Journal of Biochemistry & Cell Biology, 2009
ADAMTS5 (aggrecanase-2), a key metalloprotease mediating cartilage destruction in arthritis, is synthesized as a zymogen, proADAMTS5. We report a detailed characterization of the propeptide excision mechanism and demonstrate that it is a major regulatory step with unusual characteristics. Using furin-deficient cells and a furin inhibitor, we found that
Jean-Michel, Longpré, Daniel R, McCulloch, Bon-Hun, Koo, J Preston, Alexander, Suneel S, Apte, Richard, Leduc   +5 more
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Proprotein Convertase PC3 Is Not a Transmembrane Protein

Biochemistry, 2005
Proprotein 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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Proprotein Convertases in Gynecological Cancers

Colloquium Series on Protein Activation and Cancer, 2012
ABSTRACT 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.P. Klein-Szanto, Jirong Zhang, Daniel Bassi   +2 more
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Curbing activation: proprotein convertases in homeostasis and pathology

The FASEB Journal, 2003
ABSTRACT The proprotein convertases (PCs) are a seven‐member family of endoproteases that activate proproteins by cleavage at basic motifs. Expression patterns for individual PCs vary widely, and all cells express several members. The list of substrates activated by PCs has grown to include neuropeptides, peptide hormones, growth and ...
Neil A, Taylor, Wim J M, Van De Ven, John W M, Creemers   +2 more
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Viral envelope glycoprotein processing by proprotein convertases

Antiviral Research, 2013
The proprotein convertases (PCs) are a family of nine mammalian enzymes that play key roles in the maintenance of cell homeostasis by activating or inactivating proteins via limited proteolysis under temporal and spatial control. A wide range of pathogens, including major human pathogenic viruses can hijack cellular PCs for their own purposes.
Pasquato Antonella, da Palma Joel Ramos, Galan Clara, Seidah Nabil G, Kunz Stefan   +4 more
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