PT  - JOURNAL ARTICLE
AU  - Lloyd D. Fricker
AU  - Audra A. McKinzie
AU  - Jilin Sun
AU  - Eileen Curran
AU  - Yimei Qian
AU  - Lin Yan
AU  - Scott D. Patterson
AU  - Paul L. Courchesne
AU  - Bill Richards
AU  - Nancy Levin
AU  - Nino Mzhavia
AU  - Lakshmi A. Devi
AU  - James Douglass
TI  - Identification and Characterization of proSAAS, a Granin-Like Neuroendocrine Peptide Precursor that Inhibits Prohormone Processing
AID  - 10.1523/JNEUROSCI.20-02-00639.2000
DP  - 2000 Jan 15
TA  - The Journal of Neuroscience
PG  - 639--648
VI  - 20
IP  - 2
4099  - http://www.jneurosci.org/content/20/2/639.short
4100  - http://www.jneurosci.org/content/20/2/639.full
SO  - J. Neurosci.2000 Jan 15; 20
AB  - 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 nmbut does not inhibit prohormone convertase 2. Taken together, proSAAS may represent an endogenous inhibitor of prohormone convertase 1.