O-Glycosylation Modulates Proprotein Convertase Activation of Angiopoietin-like Protein 3
نویسندگان
چکیده
منابع مشابه
A systematic study of site-specific GalNAc-type O-glycosylation modulating proprotein convertase processing.
Site-specific GalNAc-type O-glycosylation is emerging as an important co-regulator of proprotein convertase (PC) processing of proteins. PC processing is crucial in regulating many fundamental biological pathways and O-glycans in or immediately adjacent to processing sites may affect recognition and function of PCs. Thus, we previously demonstrated that deficiency in site-specific O-glycosylati...
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A low-grade inflammatory state accompanies obesity and metabolic syndrome (MetS), which are risk factors for cardiovascular diseases (CVD) in children’s future lives. The aim of this study is to investigate possible associations of pentraxin 3 (PTX3), a promising new marker for CVDs, with angiopoietin-like proteins (ANGPTL) in morbid obese (MO) children and their potential uses in the prediagno...
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The proprotein convertases (PCs) are calcium-dependent proteases responsible for processing precursor proteins into their active forms in eukariotes. The PC1/3 is a pivotal enzyme of this family that participates in the proteolytic maturation of prohormones and neuropeptides inside the regulated secretory pathway. In this paper we demonstrate that mouse proprotein convertase 1/3 (mPC1/3) has a ...
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Angiopoietins are members of the vascular endothelial growth factor family. One family member, angiopoietin-like protein 3 (Angptl3), was recently shown to be predominantly expressed in the liver and to play an important role in regulating lipid metabolism. In this study, we show that the Angptl3 gene is a direct target of the liver X receptor (LXR). Mice fed a high cholesterol diet exhibited a...
متن کاملPrediction 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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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2010
ISSN: 0021-9258
DOI: 10.1074/jbc.m110.156950