Soluble hemojuvelin is released by proprotein convertase-mediated cleavage at a conserved polybasic RNRR site
نویسندگان
چکیده
منابع مشابه
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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Endoproteolytic processing of the 26-kDa protein precursor prodynorphin (proDyn) at paired and single basic residues is most likely carried out by the proprotein convertases (PCs); however, the role of PCs at single basic residues is unclear. In previous studies we showed that limited proDyn processing by PC1/PC3 at both paired and single basic residues resulted in the formation of 8- and 10-kD...
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ژورنال
عنوان ژورنال: Blood Cells, Molecules, and Diseases
سال: 2008
ISSN: 1079-9796
DOI: 10.1016/j.bcmd.2007.06.023