Journal
JOURNAL OF NEUROSCIENCE
Volume 20, Issue 2, Pages 639-648Publisher
SOC NEUROSCIENCE
DOI: 10.1523/JNEUROSCI.20-02-00639.2000
Keywords
carboxypeptidase E; prohormone convertase; 7B2; secretogranin; chromogranin; neuropeptide
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Funding
- NIDA NIH HHS [K02DA-00194, R01DA04494] Funding Source: Medline
- NINDS NIH HHS [R01NS-26880] Funding Source: Medline
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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.
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