1423715-09-6 Usage
Description
SP2509 is a potent and reversible inhibitor of the histone demethylase LSD1 (KDM1A), with an IC50 of 13 nM. It selectively targets the active site of LSD1 and is inactive against closely related flavin enzymes, such as MAO A,B, lactate dehydrogenase, several CYP's, and hERG. LSD1 plays a crucial role in regulating the balance between self-renewal and differentiation of stem cells and is highly expressed in various cancers. SP2509 has been shown to promote autophagy in neuroblastoma cells and effectively inhibit LSD1-dependent cancer growth.
Uses
Used in Anticancer Applications:
SP2509 is used as an anti-leukemia agent for reducing the effect of LSD1 binding to CoREST, resulting in increased methylation of H3K4 and driving increased expression of p21, p27, and CCAAT/enhancer binding protein α in acute myeloid leukemia cells.
Used in Drug Development:
SP2509 is used as a research tool for studying the role of LSD1 in various cancers and its potential as a therapeutic target. It has demonstrated effective inhibition of LSD1-dependent cancer growth in multiple cancer cell lines, making it a valuable compound for drug development and understanding the underlying mechanisms of cancer progression.
Used in Stem Cell Research:
SP2509 is used as a research tool to investigate the role of LSD1 in regulating the balance between self-renewal and differentiation of stem cells. This can provide insights into the molecular mechanisms governing stem cell behavior and potentially lead to the development of novel therapeutic strategies for various diseases.
Used in Neuroblastoma Research:
SP2509 is used as a compound to study the promotion of autophagy in neuroblastoma cells. Understanding the role of autophagy in neuroblastoma and the potential of SP2509 in modulating this process can contribute to the development of targeted therapies for this type of cancer.
Biochem/physiol Actions
Cell permeable: yes
References
1) Sorna, et al. (2013), High-Throughput Virtual Screening Identifies Novel N’-(1-Phenylethylidene)-benzohydrazides as Potent, Specific, and Reversible LSD1 Inhibitors; J. Med. Chem. 56 9496
2) Hosseini and Minucci (2017) A comprehensive review of lysine-specific demethylase 1 and its roles in cancer; Epigenomics 9 1123
3) Fiskus et al. (2014), Highly effective combination of LSD1 (KDM1A) antagonist and pan-histone deacetylase inhibitor against human AML cells; Leukemia 28 2155
4) Wen et al. (2018), Novel combination of histone methylation modulators with therapeutic synergy against acute myeloid leukemia in vitro and in vivo; Cancer Lett. 413 35
5) Tsai et al. (2018), Stress-induced phosphoprotein 1 acts as a scaffold protein for glycogen synthase kinase-3 beta-mediated phosphorylation of lysine-specific demethylase 1; Oncogenesis 7 31
6) Lu et al. (2018), Hypoxia Promotes Resistance to EGFR Inhibition in NSCLC Cells via the Histone Demethylases LSD1 and PLU-1; Mol. Cancer Epub ahead of print June 22, 2018
7) Ambrosio et al. (2017), Lysine-specific demethylase LSD1 regulates autophagy in neuroblastoma through SESN2-dependent pathway; Oncogene 36 36701
Check Digit Verification of cas no
The CAS Registry Mumber 1423715-09-6 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,4,2,3,7,1 and 5 respectively; the second part has 2 digits, 0 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 1423715-09:
(9*1)+(8*4)+(7*2)+(6*3)+(5*7)+(4*1)+(3*5)+(2*0)+(1*9)=136
136 % 10 = 6
So 1423715-09-6 is a valid CAS Registry Number.
1423715-09-6Relevant articles and documents
High-throughput virtual screening identifies novel N ′-(1- phenylethylidene)-benzohydrazides as potent, specific, and reversible LSD1 inhibitors
Sorna, Venkataswamy,Theisen, Emily R.,Stephens, Bret,Warner, Steven L.,Bearss, David J.,Vankayalapati, Hariprasad,Sharma, Sunil
, p. 9496 - 9508 (2014/01/06)
Lysine specific demethylase 1 (LSD1) plays an important role in regulating histone lysine methylation at residues K4 and K9 on histone H3 and is an attractive therapeutic target in multiple malignancies. Here we report a structure-based virtual screen of