Coexpression of Proprotein Convertase SPC3 and the Neuroendocrine Precursor ProSAAS

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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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Tissue distribution and processing of proSAAS by proprotein convertases.

The conversion of inactive precursor proteins into bioactive neuropeptides and peptide hormones involves regulated secretory proteins such as prohormone convertases PC1 and PC2. The neuroendocrine protein 7B2 represents a specific binding protein for PC2, and the protein proSAAS, which interacts with PC1, exhibits certain structural and functional homologies with 7B2. With the intention of bett...

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Identification and characterization of proSAAS, a granin-like neuroendocrine peptide precursor that inhibits prohormone processing.

Five novel peptides were identified in the brains of mice lacking active carboxypeptidase E, a neuropeptide-processing enzyme. These peptides are produced from a single precursor, termed proSAAS, which is present in human, mouse, and rat. ProSAAS mRNA is expressed primarily in brain and other neuroendocrine tissues (pituitary, adrenal, pancreas); within brain, the mRNA is broadly distributed am...

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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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Lipopolysaccharide mediated regulation of neuroendocrine associated proprotein convertases and neuropeptide precursor processing in the rat spleen.

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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ژورنال

عنوان ژورنال: Endocrinology

سال: 2001

ISSN: 0013-7227

DOI: 10.1210/en.142.9.4141