Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
US7741086B2 · kind B2 · utility
Assignee
Inventors
Key dates
| Filing date | Dec 16, 2005 |
| Grant date | Jun 22, 2010 |
| Priority date | — |
| Expiry date | Dec 20, 2025 |
Classification
- Technology area (CPC G)Physics
- CPC primaryG01N2500/02
- WIPO fieldPharmaceuticals
- WIPO sectorChemistry
Abstract
LSD1, a homolog of nuclear amine oxidases, functions as a histone demethylase and transcriptional co-repressor. LSD1 specifically demethylates histone H3 lysine 4, which is linked to active transcription. Lysine demethylation occurs via an oxidation reaction that generates formaldehyde. Importantly, RNAi inhibition of LSD1 causes an increase in H3 lysine 4 methylation and concomitant de-repression of target genes, suggesting that LSD1 represses transcription via histone demethylation. The results thus identify a histone demethylase conserved from S. pombe to human and reveal dynamic regulation of histone methylation by both histone methylases and demethylases.
Source: USPTO / EPO open patent data. Objective bibliographic and citation counts.