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The Journal of Neuroscience, January 15, 2000, 20(2):639-648
Identification and Characterization of proSAAS, a Granin-Like Neuroendocrine Peptide Precursor that Inhibits Prohormone Processing
Lloyd D. Fricker1, Audra A. McKinzie2, Jilin Sun2, Eileen Curran2, Yimei Qian1, Lin Yan1, Scott D. Patterson3, Paul L. Courchesne3, Bill Richards2, Nancy Levin2, Nino Mzhavia4, Lakshmi A. Devi4, and James Douglass2 1 Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461, Departments of 2 Neuroendocrinology and 3 Mammalian Genomics, Amgen, Thousand Oaks, California 91360-1789, and 4 Department of Pharmacology, New York University School of Medicine, New York, New York 10016
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 among neurons. When expressed in AtT-20 cells, proSAAS is secreted via the regulated pathway and is also processed at paired-basic cleavage sites into smaller peptides. Overexpression of proSAAS in the AtT-20 cells substantially reduces the rate of processing of the endogenous prohormone proopiomelanocortin. Purified proSAAS inhibits prohormone convertase 1 activity with an IC50 of 590 nM but does not inhibit prohormone convertase 2. Taken together, proSAAS may represent an endogenous inhibitor of prohormone convertase 1.
Key words: carboxypeptidase E; prohormone convertase; 7B2; secretogranin; chromogranin; neuropeptide
Copyright © 2000 Society for Neuroscience 0270-6474/00/202639-10$05.00/0
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