Abstracts (poster) - Wissenschaft Online

Soyoung Lim, Johannes Schulte, Hans-Ulrich Schildhaus, Uta Flucke, Phillip Kahl,
Roland Schüle, Reinhard Büttner, Jutta Kirfel
Functional role of Lysine-specific histone methylase-1 in
carcinogenesis
Mutations in the molecular pathways that regulate cell proliferation, differentiation, and
cell death all contribute to cancer formation. Enzymes that covalently modify histones
affect these pathways by controlling the dynamic remodelling of the chromatin structure.
While acetylation of histone is generally related to transcriptional activation, methylation
at the lysine residue either activates or represses gene transcription depending on the
sites of methylation or the number of methyl groups. LSD1 (Lysine-Specific Histone
Demethylase), which is the first discovered lysine-specific histone demethylase, can
function as both a histone diMe H3-K4 and a diMe H3-K9 demethylase. Since the
catalytic domain of LSD1 has sequence homology to monoaminoxidase (MAO) and uses
the same demethylating mechanism, the possible inhibitory effect of MAO inhibitors
(MAOIs) on LSD1 was suggested.
Recently, it has been shown that changes in global levels of individual histone
modification are associated with cancer and that these changes are predictive of clinical
outcome. We showed that LSD1 is highly expressed in different types of cancer,
suggesting the relevance of LSD1 with tumour malignancy in various tumour types. The
potential use of LSD1 as prognostic or even diagnostic marker in different types of
cancer will be evaluated. In addition, the inhibitory effect of clinically used MAOIs will be
tested in vitro and in vivo and discussed.
contact:
Soyoung Lim
Bonn Medical School
Institute of Pathology
limsoyoung@gmx.de
Sigmund-Freud Str. 25
53127 Bonn (Germany)