Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for...
Reexamination Certificate
2005-12-16
2010-06-22
Saidha, Tekchand (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
C435S069200, C435S199000, C536S023200
Reexamination Certificate
active
07741086
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 fromS. pombeto human and reveal dynamic regulation of histone methylation by both histone methylases and demethylases.
REFERENCES:
patent: 2003/0083283 (2003-05-01), Bennett et al.
patent: 1 693 383 (2006-08-01), None
patent: 1 704 859 (2006-09-01), None
patent: WO-2006/087206 (2006-08-01), None
Bannister et al., “Histone Methylation: Dynamic or Static?,” Cell, 109:801-806 (2002).
Chosed et al., “A Two-Way Street: LSD1 Regulates Chromatin Boundary Formation inS. pombeandDrosophila,” Molecular Cell, 26:160-162 (2007).
Di Stefano et al., “Mutation ofDrosophila Lsd1Disrupts H3-K4 Methylation, Resulting in Tissue-Specific Defects during Development,” Current Biology, 17:808-812 (2007).
Fang et al., “Expression of Dnmt1, demethylase, MeCP2 and methylation of tumor-related genes in human gastric cancer,” World J Gastroenterol., 10(23):3394-3398 (2004).
Garcia-Bassets et al., “Histone Methylation-Dependent Mechanisms Impose Ligand Dependency for Gene Activation by Nuclear Receptors,” Cell, 128:505-518 (2007).
Hakimi et al., “A Candidate X-linked Mental Retardation Gene Is a Component of a New Family of Histone Deacetylase-containing Complexes,” J Bio Chemistry, 278(9):7234-7239 (2003).
Hakimi et al., “A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes,” PNAS, 99(11)7420-7425 (2002).
Huang, Shi “Histone methyltransferases, diet nturients and tumour suppressors,” Nature Reviews, 2:469-476 (2002).
Huang et al., “Inhibition of lysine-specific demethylase 1 by polyamine analogues results in reexpression of aberrantly silenced genes,” PNAS, 104(19):8023-8023 (2007).
Humphrey et al., “Stable Histone Deacetylase Complexes Distinguished by the Presence of SANT Domain Proteins CoREST/kiaa0071 and Mta-L1,” J Bio Chemistry, 276(9):6817-6824 (2001).
Isogai et al., “Homo sapienscDNA FLJ43328 fis, clone NT2RI3004510,” Unpublished (2003), Abstract Only.
Kondo et al., “Epigenetic changes in colorectal cancer,” Cancer and Metastasis Reviews, 23:29-39 (2004).
Kubicek et al., “A Crack in Histone Lysine Methylation,” Cell, 119:903-906 (2004).
Lan et al., “S.pombeLSD1 Homologs Regulate heterochromatin Propagation and Euchromatic Gene Transcription,” Molecular Cell, 26:1-13 (2007).
Lan et al., “A histone H3 lysine 27 demethylase regulates animal posterior development,” Nature, 449:689-694 (2007).
Lan et al., Supplementary Information of Nature manuscript 2007-05-05498A, 1-13.
Lee et al., “An essential role for CoRest in nucleosomal histone 3 lysine 4 demethylation,” Nature, 437:432-435 (2005).
Metzger et al., “LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription,” Nature, 437:436-439 (2005).
Nagase et al., “Prediction of the coding sequences of unidentified human genes,” DNA Res. 5(1):31-39 (1998) Abstract Only.
Paik et al., “Enzymatic Demethylation of Calf Thymus Histones,” Biochemical and Biophysical Research Communications, 51(3):781-788 (1973).
Shi et al., “Histone Demethylation Mediated by the Nuclear Amine Oxidase Homolog LSD1,” Cell, 119:941-953 (2004).
Shi, “Taking LSD1 to a New High,” Cell 654-658 (2005).
Shi et al., “Regulation of LSD1 Histone Demethylase Activity by Its Associated Factors,” Molecular Cell, 19:1-8 (2005).
Shi et al., “Metabolic Enzymes and Coenzymes in Transcription—a Direct Link Between Metabolism and Transcription?,” Trends in Genetics 20(9):445-452 (2004).
Tsukada et al., “Histone Demethylation by a Family of JmjC Domain-Containing Proteins,” Nature (2006) 439:811 Epub Dec. 18, 2005.
Wang et al., “Human PAD4 Regulates Histone Arginine Methylation Levels via Demethylimination,” Science, 306:279-283 (2004).
Yamane et al., “JHDM2A, a JmjC-Containing H3K9 Demethylase, Facilitates Transcription Activation by Androgen Receptor,” Cell 125 (2006).
International Search Report for PCT/US2005/045987 mailed on Aug. 11, 2006.
Shi Yang
Shi Yujiang
Foley & Hoag LLP
President and Fellows of Harvard College
Saidha Tekchand
LandOfFree
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