Epigenetic regulation by lysine demethylase 5 (KDM5) enzymes in cancer

Lauren P. Blair; Jian Cao; Mike Ran Zou; Joyce Sayegh; Qin Yan

doi:10.3390/cancers3011383

Epigenetic regulation by lysine demethylase 5 (KDM5) enzymes in cancer

Lauren P. Blair, Jian Cao, Mike Ran Zou, Joyce Sayegh, Qin Yan

Research output: Contribution to journal › Review article › peer-review

129 Scopus citations

Abstract

Similar to genetic alterations, epigenetic aberrations contribute significantly to tumor initiation and progression. In many cases, these changes are caused by activation or inactivation of the regulators that maintain epigenetic states. Here we review our current knowledge on the KDM5/JARID1 family of histone demethylases. This family of enzymes contains a JmjC domain and is capable of removing tri- and di- methyl marks from lysine 4 on histone H3. Among these proteins, RBP2 mediates drug resistance while JARID1B is required for melanoma maintenance. Preclinical studies suggest inhibition of these enzymes can suppress tumorigenesis and provide strong rationale for development of their inhibitors for use in cancer therapy.

Original language	English (US)
Pages (from-to)	1383-1404
Number of pages	22
Journal	Cancers
Volume	3
Issue number	1
DOIs	https://doi.org/10.3390/cancers3011383
State	Published - Mar 2011
Externally published	Yes

All Science Journal Classification (ASJC) codes

Oncology
Cancer Research

Keywords

Cancer stem cell
Drug resistance
Histone demethylase
JARID1
KDM5
Lid
PLU1
RBP2
SMCX
SMCY

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10.3390/cancers3011383

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title = "Epigenetic regulation by lysine demethylase 5 (KDM5) enzymes in cancer",

abstract = "Similar to genetic alterations, epigenetic aberrations contribute significantly to tumor initiation and progression. In many cases, these changes are caused by activation or inactivation of the regulators that maintain epigenetic states. Here we review our current knowledge on the KDM5/JARID1 family of histone demethylases. This family of enzymes contains a JmjC domain and is capable of removing tri- and di- methyl marks from lysine 4 on histone H3. Among these proteins, RBP2 mediates drug resistance while JARID1B is required for melanoma maintenance. Preclinical studies suggest inhibition of these enzymes can suppress tumorigenesis and provide strong rationale for development of their inhibitors for use in cancer therapy.",

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author = "Blair, {Lauren P.} and Jian Cao and Zou, {Mike Ran} and Joyce Sayegh and Qin Yan",

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AU - Blair, Lauren P.

AU - Cao, Jian

AU - Zou, Mike Ran

AU - Sayegh, Joyce

AU - Yan, Qin

PY - 2011/3

Y1 - 2011/3

N2 - Similar to genetic alterations, epigenetic aberrations contribute significantly to tumor initiation and progression. In many cases, these changes are caused by activation or inactivation of the regulators that maintain epigenetic states. Here we review our current knowledge on the KDM5/JARID1 family of histone demethylases. This family of enzymes contains a JmjC domain and is capable of removing tri- and di- methyl marks from lysine 4 on histone H3. Among these proteins, RBP2 mediates drug resistance while JARID1B is required for melanoma maintenance. Preclinical studies suggest inhibition of these enzymes can suppress tumorigenesis and provide strong rationale for development of their inhibitors for use in cancer therapy.

AB - Similar to genetic alterations, epigenetic aberrations contribute significantly to tumor initiation and progression. In many cases, these changes are caused by activation or inactivation of the regulators that maintain epigenetic states. Here we review our current knowledge on the KDM5/JARID1 family of histone demethylases. This family of enzymes contains a JmjC domain and is capable of removing tri- and di- methyl marks from lysine 4 on histone H3. Among these proteins, RBP2 mediates drug resistance while JARID1B is required for melanoma maintenance. Preclinical studies suggest inhibition of these enzymes can suppress tumorigenesis and provide strong rationale for development of their inhibitors for use in cancer therapy.

KW - Cancer stem cell

KW - Drug resistance

KW - Histone demethylase

KW - JARID1

KW - KDM5

KW - Lid

KW - PLU1

KW - RBP2

KW - SMCX

KW - SMCY

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U2 - 10.3390/cancers3011383

DO - 10.3390/cancers3011383

M3 - Review article

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JO - Cancers

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Epigenetic regulation by lysine demethylase 5 (KDM5) enzymes in cancer

Abstract

All Science Journal Classification (ASJC) codes

Keywords

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