Coexpression of Proprotein Convertase SPC3 and the Neuroendocrine Precursor ProSAAS1

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Coexpression of Proprotein Convertase SPC3 and the Neuroendocrine Precursor ProSAAS1.

The subtilisin-like proprotein convertases are a family of serine proteinases involved in the processing of secreted proteins via cleavage at paired basic residues. Until recently, only one natural inhibitor had been demonstrated, the neuropeptide 7B2, which contains a C-terminal domain with inhibitory activity against SPC2. A novel granin-like peptide precursor, named proSAAS, has recently bee...

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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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Within the secretory pathway, the family of proprotein convertases cleave inactive precursors at paired basic residues to generate a myriad of biologically active peptides. Within the PC family, PC1/3 and PC2 are well known for their preferential expression within neuroendocrine cells. However, various data now indicate their potential expression in immune cells. The aim of our study was two fo...

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Subtilisin-related Proprotein Convertase Endoproteolytic Site*

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Seven secretory mammalian kexin-like subtilases have been identified that cleave a variety of precursor proteins at monobasic and dibasic residues. The recently characterized pyrolysin-like subtilase SKI-1 cleaves proproteins at nonbasic residues. In this work we describe the properties of a proteinase K-like subtilase, neural apoptosis-regulated convertase 1 (NARC-1), representing the ninth me...

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ژورنال

عنوان ژورنال: Endocrinology

سال: 2001

ISSN: 0013-7227,1945-7170

DOI: 10.1210/endo.142.9.8386