PCSK6 (proprotein convertase subtilisin/kexin type 6)

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Subtilisin-related Proprotein Convertase Endoproteolytic Site*

The human thyrotropin receptor (TSHR) undergoes proteolytic cleavage closely upstream to amino acid 317. Between residues 261 and 313 are three clusters of positively charged amino acids, arginines (Arg) and lysines (Lys), which are potential subtilisin-related proprotein convertase sites. We used oligonucleotide-directed mutagenesis to perform conservative amino acid substitutions within these...

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Prediction of proprotein convertase cleavage sites.

Many secretory proteins and peptides are synthesized as inactive precursors that in addition to signal peptide cleavage undergo post-translational processing to become biologically active polypeptides. Precursors are usually cleaved at sites composed of single or paired basic amino acid residues by members of the subtilisin/kexin-like proprotein convertase (PC) family. In mammals, seven members...

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

PC5 belongs to the proprotein convertase family and activates precursor proteins by cleavage at basic sites during their transit through the secretory pathway and/or at the cell surface. These precursors include prohormones, proreceptors, growth factors, adhesion molecules, and viral glycoproteins. The Pcsk5 gene encodes two alternatively spliced isoforms, the soluble PC5A and transmembrane PC5...

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Decidual differentiation of stromal cells promotes Proprotein Convertase 5/6 expression and lefty processing.

Lefty/Ebaf polypeptides, novel members of the TGF-beta superfamily, are involved in endometrial differentiation and embryo implantation. Recently, we showed that, during undisturbed estrous cycle, lefty is present in mouse uterine horn primarily in a precursor form. Here, we show that decidual differentiation of endometrial stroma leads to increased lefty (approximately 3.1- to 3.6-fold in vivo...

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Statins, plasma proprotein convertase subtilisin/kexin type 9 concentrations, and LDL lowering.

The discovery in 2003 that variants in the PCSK9 (proprotein convertase subtilisin/kexin type 9) gene cause autosomal dominant hypercholesterolemia revealed a new aspect of LDL cholesterol (LDL-C) metabolism (1). PCSK9, a protein of 692 amino acid residues produced at high concentrations in the liver, kidney, and intestine, has profound effects on LDL-C concentrations (2). Both gain-of-function...

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ژورنال

عنوان ژورنال: Atlas of Genetics and Cytogenetics in Oncology and Haematology

سال: 2017

ISSN: 1768-3262

DOI: 10.4267/2042/62490