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Article ; Online: Regional tumour glutamine supply affects chromatin and cell identity.

Højfeldt, Jonas W / Helin, Kristian

2016 Volume 18, Issue 10, Page(s) 1027–1029

Abstract: Limited perfusion of solid tumours produces a nutrient-deprived tumour core microenvironment. Low glutamine levels in the tumour core are now shown to lead to reduced levels of α-ketoglutarate and decreased histone demethylase activity, thereby promoting ...

Abstract	Limited perfusion of solid tumours produces a nutrient-deprived tumour core microenvironment. Low glutamine levels in the tumour core are now shown to lead to reduced levels of α-ketoglutarate and decreased histone demethylase activity, thereby promoting a less differentiated and more therapy-resistant state of the tumour cells.
MeSH term(s)	Animals ; Cell Differentiation/drug effects ; Cell Differentiation/physiology ; Chromatin/drug effects ; Chromatin/metabolism ; Glutamine/metabolism ; Glutamine/pharmacology ; Humans ; Ketoglutaric Acids/metabolism ; Neoplasms/drug therapy ; Neoplasms/pathology ; Tumor Microenvironment/drug effects ; Tumor Microenvironment/physiology
Chemical Substances	Chromatin ; Ketoglutaric Acids ; Glutamine (0RH81L854J) ; alpha-ketoglutaric acid (8ID597Z82X)
Language	English
Publishing date	2016-09-28
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/ncb3414
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Zs.A 5169: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 12: Show issues

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Article ; Online: MPP8 is essential for sustaining self-renewal of ground-state pluripotent stem cells.

Müller, Iris / Moroni, Ann Sophie / Shlyueva, Daria / Sahadevan, Sudeep / Schoof, Erwin M / Radzisheuskaya, Aliaksandra / Højfeldt, Jonas W / Tatar, Tülin / Koche, Richard P / Huang, Chang / Helin, Kristian

Nature communications

2021 Volume 12, Issue 1, Page(s) 3034

Abstract: Deciphering the mechanisms that control the pluripotent ground state is key for understanding embryonic development. Nonetheless, the epigenetic regulation of ground-state mouse embryonic stem cells (mESCs) is not fully understood. Here, we identify the ... ...

Abstract	Deciphering the mechanisms that control the pluripotent ground state is key for understanding embryonic development. Nonetheless, the epigenetic regulation of ground-state mouse embryonic stem cells (mESCs) is not fully understood. Here, we identify the epigenetic protein MPP8 as being essential for ground-state pluripotency. Its depletion leads to cell cycle arrest and spontaneous differentiation. MPP8 has been suggested to repress LINE1 elements by recruiting the human silencing hub (HUSH) complex to H3K9me3-rich regions. Unexpectedly, we find that LINE1 elements are efficiently repressed by MPP8 lacking the chromodomain, while the unannotated C-terminus is essential for its function. Moreover, we show that SETDB1 recruits MPP8 to its genomic target loci, whereas transcriptional repression of LINE1 elements is maintained without retaining H3K9me3 levels. Taken together, our findings demonstrate that MPP8 protects the DNA-hypomethylated pluripotent ground state through its association with the HUSH core complex, however, independently of detectable chromatin binding and maintenance of H3K9me3.
MeSH term(s)	Animals ; CRISPR-Cas Systems ; Cell Proliferation ; DNA Methylation ; Epigenesis, Genetic ; Gene Knock-In Techniques ; HEK293 Cells ; Histone-Lysine N-Methyltransferase ; Humans ; Long Interspersed Nucleotide Elements/genetics ; Mice ; Mouse Embryonic Stem Cells ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Pluripotent Stem Cells/metabolism ; Tumor Suppressor Protein p53/genetics
Chemical Substances	Mphosph8 protein, mouse ; Phosphoproteins ; Tumor Suppressor Protein p53 ; Histone-Lysine N-Methyltransferase (EC 2.1.1.43) ; SETDB1 protein, human (EC 2.1.1.43)
Language	English
Publishing date	2021-05-24
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-23308-4
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Histone lysine demethylases as targets for anticancer therapy.

Højfeldt, Jonas W / Agger, Karl / Helin, Kristian

Nature reviews. Drug discovery

2013 Volume 12, Issue 12, Page(s) 917–930

Abstract: It has recently been demonstrated that the genes controlling the epigenetic programmes that are required for maintaining chromatin structure and cell identity include genes that drive human cancer. This observation has led to an increased awareness of ... ...

Abstract	It has recently been demonstrated that the genes controlling the epigenetic programmes that are required for maintaining chromatin structure and cell identity include genes that drive human cancer. This observation has led to an increased awareness of chromatin-associated proteins as potentially interesting drug targets. The successful introduction of DNA methylation and histone deacetylase (HDAC) inhibitors for the treatment of specific subtypes of cancer has paved the way for the use of epigenetic therapy. Here, we highlight key biological findings demonstrating the roles of members of the histone lysine demethylase class of enzymes in the development of cancers, discuss the potential and challenges of therapeutically targeting them, and highlight emerging small-molecule inhibitors of these enzymes.
MeSH term(s)	Animals ; Antineoplastic Agents/administration & dosage ; Drug Delivery Systems/methods ; Histone Deacetylase Inhibitors/administration & dosage ; Histone Deacetylase Inhibitors/chemistry ; Histone Demethylases/antagonists & inhibitors ; Histone Demethylases/chemistry ; Histone Demethylases/metabolism ; Humans ; Neoplasms/drug therapy ; Neoplasms/enzymology
Chemical Substances	Antineoplastic Agents ; Histone Deacetylase Inhibitors ; Histone Demethylases (EC 1.14.11.-)
Language	English
Publishing date	2013-11-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2062954-0
ISSN	1474-1784 ; 1474-1776
ISSN (online)	1474-1784
ISSN	1474-1776
DOI	10.1038/nrd4154
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Zs.A 5564: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Zs.MG 63: Show issues

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Article ; Online: Accurate H3K27 methylation can be established de novo by SUZ12-directed PRC2.

Højfeldt, Jonas W / Laugesen, Anne / Willumsen, Berthe M / Damhofer, Helene / Hedehus, Lin / Tvardovskiy, Andrey / Mohammad, Faizaan / Jensen, Ole N / Helin, Kristian

Nature structural & molecular biology

2018 Volume 25, Issue 3, Page(s) 225–232

Abstract: Polycomb repressive complex 2 (PRC2) catalyzes methylation on lysine 27 of histone H3 (H3K27) and is required for maintaining transcriptional patterns and cellular identity, but the specification and maintenance of genomic PRC2 binding and H3K27 ... ...

Abstract	Polycomb repressive complex 2 (PRC2) catalyzes methylation on lysine 27 of histone H3 (H3K27) and is required for maintaining transcriptional patterns and cellular identity, but the specification and maintenance of genomic PRC2 binding and H3K27 methylation patterns remain incompletely understood. Epigenetic mechanisms have been proposed, wherein pre-existing H3K27 methylation directs recruitment and regulates the catalytic activity of PRC2 to support its own maintenance. Here we investigate whether such mechanisms are required for specifying H3K27 methylation patterns in mouse embryonic stem cells (mESCs). Through re-expression of PRC2 subunits in PRC2-knockout cells that have lost all H3K27 methylation, we demonstrate that methylation patterns can be accurately established de novo. We find that regional methylation kinetics correlate with original methylation patterns even in their absence, and specification of the genomic PRC2 binding pattern is retained and specifically dependent on the PRC2 core subunit SUZ12. Thus, the H3K27 methylation patterns in mESCs are not dependent on self-autonomous epigenetic inheritance.
MeSH term(s)	Animals ; Cells, Cultured ; CpG Islands ; Embryonic Stem Cells/metabolism ; Histones/metabolism ; Kinetics ; Methylation ; Mice ; Polycomb Repressive Complex 2/metabolism
Chemical Substances	Histones ; Suz12 protein, mouse ; Polycomb Repressive Complex 2 (EC 2.1.1.43)
Language	English
Publishing date	2018-02-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2126708-X
ISSN	1545-9985 ; 1545-9993
ISSN (online)	1545-9985
ISSN	1545-9993
DOI	10.1038/s41594-018-0036-6
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Zs.A 4101: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Transforming ligands into transcriptional regulators: building blocks for bifunctional molecules.

Højfeldt, Jonas W / Van Dyke, Aaron R / Mapp, Anna K

Chemical Society reviews

2011 Volume 40, Issue 8, Page(s) 4286–4294

Abstract: The human body is comprised of several hundred distinct cell types that all share a common genomic template. This diversity arises from regulated expression of individual genes. The first critical step in this process is transcription and is governed by ... ...

Abstract	The human body is comprised of several hundred distinct cell types that all share a common genomic template. This diversity arises from regulated expression of individual genes. The first critical step in this process is transcription and is governed by a large number of transcription factors. Small molecules that can alter transcription hold tremendous utility as chemical probes and therapeutics. To fully realize their potential, however, artificial transcription factors must be able to orchestrate protein recruitment at gene promoters just like their natural counterparts. This tutorial review surveys the discovery of small ligands (drug-like molecules and short peptides) that bind transcriptional coregulatory proteins, and thus comprise one of the two essential characteristics of a transcription factor. By joining these ligands to DNA-targeting moieties, one can construct a bifunctional molecule that recruits its protein target to specific genes and controls gene transcription.
MeSH term(s)	Gene Expression Regulation ; Histone Deacetylase Inhibitors/chemistry ; Histone Deacetylase Inhibitors/metabolism ; Humans ; Ligands ; Mediator Complex/chemistry ; Mediator Complex/metabolism ; Molecular Mimicry ; Peptides/chemistry ; Peptides/pharmacology ; Protein Binding ; Protein Structure, Tertiary ; Transcription Factors/chemistry ; Transcription Factors/metabolism ; Transcription, Genetic ; p300-CBP Transcription Factors/chemistry ; p300-CBP Transcription Factors/metabolism
Chemical Substances	Histone Deacetylase Inhibitors ; Ligands ; MED23 protein, human ; Mediator Complex ; Peptides ; Transcription Factors ; p300-CBP Transcription Factors (EC 2.3.1.48)
Language	English
Publishing date	2011-08
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1472875-8
ISSN	1460-4744 ; 0306-0012
ISSN (online)	1460-4744
ISSN	0306-0012
DOI	10.1039/c1cs15050b
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Transforming ligands into transcriptional regulators: building blocks for bifunctional molecules

Højfeldt, Jonas W / Van Dyke, Aaron R / Mapp, Anna K

Chemical Society reviews. 2011 July 14, v. 40, no. 8

2011

Abstract	The human body is comprised of several hundred distinct cell types that all share a common genomic template. This diversity arises from regulated expression of individual genes. The first critical step in this process is transcription and is governed by a large number of transcription factors. Small molecules that can alter transcription hold tremendous utility as chemical probes and therapeutics. To fully realize their potential, however, artificial transcription factors must be able to orchestrate protein recruitment at gene promoters just like their natural counterparts. This tutorial review surveys the discovery of small ligands (drug-like molecules and short peptides) that bind transcriptional coregulatory proteins, and thus comprise one of the two essential characteristics of a transcription factor. By joining these ligands to DNA-targeting moieties, one can construct a bifunctional molecule that recruits its protein target to specific genes and controls gene transcription.
Keywords	genes ; genomics ; humans ; ligands ; moieties ; peptides ; surveys ; therapeutics ; transcription (genetics) ; transcription factors
Language	English
Dates of publication	2011-0714
Size	p. 4286-4294.
Publishing place	The Royal Society of Chemistry
Document type	Article
ZDB-ID	1472875-8
ISSN	1460-4744 ; 0306-0012
ISSN (online)	1460-4744
ISSN	0306-0012
DOI	10.1039/c1cs15050b
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Article ; Online: Expanding the repertoire of small molecule transcriptional activation domains.

Casey, Ryan J / Desaulniers, Jean-Paul / Hojfeldt, Jonas W / Mapp, Anna K

Bioorganic & medicinal chemistry

2009 Volume 17, Issue 3, Page(s) 1034–1043

Abstract: Molecules that can reconstitute the function of transcriptional activators hold enormous potential as therapeutic agents and as mechanistic probes. Previously we described an isoxazolidine bearing functional groups similar to natural transcriptional ... ...

Abstract	Molecules that can reconstitute the function of transcriptional activators hold enormous potential as therapeutic agents and as mechanistic probes. Previously we described an isoxazolidine bearing functional groups similar to natural transcriptional activators that up-regulates transcription 80-fold at 1 microM in cell culture. In this study, we analyze analogs of this molecule to define key characteristics of small molecules that function as transcriptional activation domains in cells. Conformational rigidity is an important contributor to function as is an overall amphipathic substitution pattern. Using these criteria, we identified additional molecular scaffolds with excellent (approximately 60-fold) activity as transcriptional activation domains. These results point the way for the creation of new generations of small molecules with this function.
MeSH term(s)	Benzylisoquinolines/chemical synthesis ; Benzylisoquinolines/chemistry ; Benzylisoquinolines/pharmacology ; Cell Line ; HeLa Cells ; Humans ; Isoxazoles/chemical synthesis ; Isoxazoles/chemistry ; Isoxazoles/pharmacology ; Protein Structure, Tertiary ; Santonin/chemical synthesis ; Santonin/chemistry ; Santonin/pharmacology ; Trans-Activators/chemical synthesis ; Trans-Activators/chemistry ; Trans-Activators/pharmacology ; Transcription, Genetic/drug effects
Chemical Substances	Benzylisoquinolines ; Isoxazoles ; Trans-Activators ; Santonin (1VL8J38ERO) ; hydrastine (8890V3217X)
Language	English
Publishing date	2009-02-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1161284-8
ISSN	1464-3391 ; 0968-0896
ISSN (online)	1464-3391
ISSN	0968-0896
DOI	10.1016/j.bmc.2008.02.045
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Zs.A 3815: Show issues

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Article: A cleavable amino-thiol linker for reversible linking of amines to DNA.

Højfeldt, Jonas W / Blakskjaer, Peter / Gothelf, Kurt V

The Journal of organic chemistry

2006 Volume 71, Issue 25, Page(s) 9556–9559

Abstract: A cleavable heterobifunctional cross-linker for the reversible conjugation of amines to thiol-modified DNA has been developed and tested. The succinimidyl 2-(vinylsulfonyl)ethyl carbonate (SVEC) was prepared in three steps and tested for its ability to ... ...

Abstract	A cleavable heterobifunctional cross-linker for the reversible conjugation of amines to thiol-modified DNA has been developed and tested. The succinimidyl 2-(vinylsulfonyl)ethyl carbonate (SVEC) was prepared in three steps and tested for its ability to react with amines and thiols. The linker was efficient for binding leucine to a thiol-modified DNA sequence and for releasing the amino acid at pH 11.8.
MeSH term(s)	Amines/chemistry ; DNA/chemistry ; Magnetic Resonance Spectroscopy ; Mass Spectrometry ; Sulfhydryl Compounds/chemistry
Chemical Substances	Amines ; Sulfhydryl Compounds ; DNA (9007-49-2)
Language	English
Publishing date	2006-12-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	123490-0
ISSN	1520-6904 ; 0022-3263
ISSN (online)	1520-6904
ISSN	0022-3263
DOI	10.1021/jo0619736
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Zs.A 4473: Show issues

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Article ; Online: Bifunctional ligands allow deliberate extrinsic reprogramming of the glucocorticoid receptor.

Højfeldt, Jonas W / Cruz-Rodríguez, Osvaldo / Imaeda, Yasuhiro / Van Dyke, Aaron R / Carolan, James P / Mapp, Anna K / Iñiguez-Lluhí, Jorge A

Molecular endocrinology (Baltimore, Md.)

2014 Volume 28, Issue 2, Page(s) 249–259

Abstract: Therapies based on conventional nuclear receptor ligands are extremely powerful, yet their broad and long-term use is often hindered by undesired side effects that are often part of the receptor's biological function. Selective control of nuclear ... ...

Abstract	Therapies based on conventional nuclear receptor ligands are extremely powerful, yet their broad and long-term use is often hindered by undesired side effects that are often part of the receptor's biological function. Selective control of nuclear receptors such as the glucocorticoid receptor (GR) using conventional ligands has proven particularly challenging. Because they act solely in an allosteric manner, conventional ligands are constrained to act via cofactors that can intrinsically partner with the receptor. Furthermore, effective means to rationally encode a bias for specific coregulators are generally lacking. Using the (GR) as a framework, we demonstrate here a versatile approach, based on bifunctional ligands, that extends the regulatory repertoire of GR in a deliberate and controlled manner. By linking the macrolide FK506 to a conventional agonist (dexamethasone) or antagonist (RU-486), we demonstrate that it is possible to bridge the intact receptor to either positively or negatively acting coregulatory proteins bearing an FK506 binding protein domain. Using this strategy, we show that extrinsic recruitment of a strong activation function can enhance the efficacy of the full agonist dexamethasone and reverse the antagonist character of RU-486 at an endogenous locus. Notably, the extrinsic recruitment of histone deacetylase-1 reduces the ability of GR to activate transcription from a canonical GR response element while preserving ligand-mediated repression of nuclear factor-κB. By providing novel ways for the receptor to engage specific coregulators, this unique ligand design approach has the potential to yield both novel tools for GR study and more selective therapeutics.
MeSH term(s)	Calcium-Binding Proteins/genetics ; Calcium-Binding Proteins/metabolism ; Dexamethasone/pharmacology ; HEK293 Cells ; Histone Deacetylase 1/metabolism ; Humans ; Ligands ; Mifepristone/pharmacology ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; Protein Binding ; Receptors, Glucocorticoid/agonists ; Receptors, Glucocorticoid/antagonists & inhibitors ; Receptors, Glucocorticoid/physiology ; Tacrolimus/pharmacology ; Transcriptional Activation
Chemical Substances	Calcium-Binding Proteins ; Ligands ; Neoplasm Proteins ; Receptors, Glucocorticoid ; S100P protein, human ; Mifepristone (320T6RNW1F) ; Dexamethasone (7S5I7G3JQL) ; HDAC1 protein, human (EC 3.5.1.98) ; Histone Deacetylase 1 (EC 3.5.1.98) ; Tacrolimus (WM0HAQ4WNM)
Language	English
Publishing date	2014-01-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	639167-9
ISSN	1944-9917 ; 0888-8809
ISSN (online)	1944-9917
ISSN	0888-8809
DOI	10.1210/me.2013-1343
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Zs.A 2261: Show issues

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Article ; Online: EZH2 is a potential therapeutic target for H3K27M-mutant pediatric gliomas.

Mohammad, Faizaan / Weissmann, Simon / Leblanc, Benjamin / Pandey, Deo P / Højfeldt, Jonas W / Comet, Itys / Zheng, Chunqin / Johansen, Jens Vilstrup / Rapin, Nicolas / Porse, Bo T / Tvardovskiy, Andrey / Jensen, Ole N / Olaciregui, Nagore G / Lavarino, Cinzia / Suñol, Mariona / de Torres, Carmen / Mora, Jaume / Carcaboso, Angel M / Helin, Kristian

Nature medicine

2017 Volume 23, Issue 4, Page(s) 483–492

Abstract: Diffuse intrinsic pontine glioma (DIPG) is an aggressive brain tumor that is located in the pons and primarily affects children. Nearly 80% of DIPGs harbor mutations in histone H3 genes, wherein lysine 27 is substituted with methionine (H3K27M). H3K27M ... ...

Abstract	Diffuse intrinsic pontine glioma (DIPG) is an aggressive brain tumor that is located in the pons and primarily affects children. Nearly 80% of DIPGs harbor mutations in histone H3 genes, wherein lysine 27 is substituted with methionine (H3K27M). H3K27M has been shown to inhibit polycomb repressive complex 2 (PRC2), a multiprotein complex responsible for the methylation of H3 at lysine 27 (H3K27me), by binding to its catalytic subunit EZH2. Although DIPGs with the H3K27M mutation show global loss of H3K27me3, several genes retain H3K27me3. Here we describe a mouse model of DIPG in which H3K27M potentiates tumorigenesis. Using this model and primary patient-derived DIPG cell lines, we show that H3K27M-expressing tumors require PRC2 for proliferation. Furthermore, we demonstrate that small-molecule EZH2 inhibitors abolish tumor cell growth through a mechanism that is dependent on the induction of the tumor-suppressor protein p16
MeSH term(s)	Animals ; Benzamides/pharmacology ; Brain Neoplasms/genetics ; Brain Stem Neoplasms/genetics ; CRISPR-Cas Systems ; Cell Line, Tumor ; Cell Proliferation/genetics ; Chromatin Immunoprecipitation ; Chromatography, Liquid ; Cyclin-Dependent Kinase Inhibitor p16/drug effects ; Cyclin-Dependent Kinase Inhibitor p16/genetics ; Disease Models, Animal ; Enhancer of Zeste Homolog 2 Protein/antagonists & inhibitors ; Enhancer of Zeste Homolog 2 Protein/genetics ; Gene Knockout Techniques ; Glioblastoma/genetics ; Glioma/genetics ; Histones/genetics ; Humans ; Immunohistochemistry ; In Situ Hybridization, Fluorescence ; Indazoles/pharmacology ; Mice ; Mice, SCID ; Molecular Targeted Therapy ; Mutation ; Neoplasm Transplantation ; Neural Stem Cells ; Polycomb Repressive Complex 2/genetics ; Pyridones/pharmacology ; Tandem Mass Spectrometry ; Tumor Suppressor Protein p14ARF/drug effects ; Tumor Suppressor Protein p14ARF/genetics
Chemical Substances	Benzamides ; Cyclin-Dependent Kinase Inhibitor p16 ; GSK343 ; Histones ; Indazoles ; Pyridones ; Tumor Suppressor Protein p14ARF ; EZH2 protein, human (EC 2.1.1.43) ; Enhancer of Zeste Homolog 2 Protein (EC 2.1.1.43) ; Ezh2 protein, mouse (EC 2.1.1.43) ; Polycomb Repressive Complex 2 (EC 2.1.1.43) ; tazemetostat (Q40W93WPE1)
Language	English
Publishing date	2017-02-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	1220066-9
ISSN	1546-170X ; 1078-8956
ISSN (online)	1546-170X
ISSN	1078-8956
DOI	10.1038/nm.4293
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