Signum Biosciences, Inc. is a biotechnology company in Monmouth Junction, NJ. It was founded in 2003 based on research done in the lab of Jeffry B. Stock, a professor at Princeton University, on compounds that can modulate protein phosphatase 2 (PP2). Gregory Stock, Stock's brother, served as the first CEO.
In 2011 Signum spun out a dermatology company, originally called Argyle Therapeutics but after 2012 called Signum Dermalogix. In 2012 Argyle licensed one of its compounds, SIG990, to Brickell Biotech for development as a drug to treat rosacea.
In 2015 Signum partnered with Nerium International to launch a dietary supplement called eicosanoyl-5-hydroxytryptamide (EHT). EHT is derived from coffee and inhibits demethylaton of the enzyme protein phosphatase 2 (PPP2CA; PP2A). EHT has shown neuroprotective effects in a mouse model of Parkinson's disease.
- Signum profile at Bloomerberg Page accessed April 10, 2015
- Signum Dermalogix Signum profile Page accessed April 10, 2015
- Gregory Stock's Blog Where are the New Therapeutics? Page accessed April 10, 2015
- Signum. July 12, 2010. Press release: Signum Biosciences, Inc. Announces Commercial Launch Of Arazine
- Signum. Nov 10 2011 Press Release: Signum Biosciences Enters Into Co-Development Agreement With GlaxoSmithKline
- NIH SBIR Program. Content posted or updated April 20, 2012 SBIR Success Stories: Signum Biosciences
- Argyle Therapeutics. April 17, 2012 Press release: Argyle Therapeutics Out-Licenses SIG990 to Brickell Biotech for Topical Treatment of Rosacea
- Neirum. April 10, 2015 Nerium Press Release: Nerium International Introduces New, Advanced Anti-Aging Product Focused on Optimal Brain Health
- Haas, M.J. Extracting PD therapy from coffee SciBX 4(21). May 26, 2011 doi:10.1038/scibx.2011.590
- Petr Heneberg. Protein Phosphatases in Parkinson's Disease. Chapter 7 in Emerging Drugs and Targets for Parkinson's Disease, Volume 34 of RSC drug discovery series. Edited by Ana Martinez and Carmen Gil. Royal Society of Chemistry, 2013 ISBN 9781849736176. Content on EHT, p. 162: "Activation of Balpha containing PP2A was reached by inhibiting PP2A demethylation mediated by eicosanoyl-5-hydrotytryptamide (EHT). EHT administration to alpha-synuclein transgenic mice reduced alpa-synuclein Ser129 phosphorylation, its subsequent aggregation, and ameliorated the associated neuropathology and behavioral aberrations. EHT action on PP2A is mediated by its antagonistic effect on PME. reported to occur at IC50 3.9µM."
- Taymans JM, Baekelandt V. Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of Parkinsonism. Front Genet. 2014 Nov 7;5:382. doi:10.3389/fgene.2014.00382. PMID 25426138. PMC 4224088 Content on EHT: "P2A enzymes have the particularity that their enzymatic activity is positively regulated by its methylation which is itself regulated via the opposing activities of a PP2A-specific methyltransferase and a PP2A-specific methylesterase (PME). Accordingly, treatment of mice with the PME inhibitor eicosanoyl-5-hydroxytryptamide (EHT) increases PP2A methylation as well as decreased α-syn-pS129 levels in brain and a concurrent reduction in synuclein pathology"