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Article ; Online: Discovery of NSD2-Degraders from Novel and Selective DEL Hits.

LegaardAndersson, Jan / Christensen, Jesper / Kleine-Kohlbrecher, Daniela / Vacher Comet, Itys / Fullerton Støier, Jonatan / Antoku, Yasuko / Poljak, Visnja / Moretti, Loris / Dolberg, Johannes / Jacso, Tomas / Jensby Nielsen, Søren / Nørregaard-Madsen, Mads / Franch, Thomas / Helin, Kristian / Cloos, Paul A C

Chembiochem : a European journal of chemical biology

2023 Volume 24, Issue 24, Page(s) e202300515

Abstract: NSD2 is a histone methyltransferase predominantly catalyzing di-methylation of histone H3 on lysine K36. Increased NSD2 activity due to mutations or fusion-events affecting the gene encoding NSD2 is considered an oncogenic event and a driver in various ... ...

Abstract	NSD2 is a histone methyltransferase predominantly catalyzing di-methylation of histone H3 on lysine K36. Increased NSD2 activity due to mutations or fusion-events affecting the gene encoding NSD2 is considered an oncogenic event and a driver in various cancers, including multiple myelomas carrying t(4;14) chromosomal translocations and acute lymphoblastic leukemia's expressing the hyperactive NSD2 mutant E1099 K. Using DNA-encoded libraries, we have identified small molecule ligands that selectively and potently bind to the PWWP1 domain of NSD2, inhibit NSD2 binding to H3K36me2-bearing nucleosomes, but do not inhibit the methyltransferase activity. The ligands were subsequently converted to selective VHL1-recruiting NSD2 degraders and by using one of the most efficacious degraders in cell lines, we show that it leads to NSD2 degradation, decrease in K3 K36me2 levels and inhibition of cell proliferation.
MeSH term(s)	Histone-Lysine N-Methyltransferase/metabolism ; Histones/metabolism ; Nucleosomes ; Cell Line, Tumor ; Methylation
Chemical Substances	Histone-Lysine N-Methyltransferase (EC 2.1.1.43) ; Histones ; Nucleosomes
Language	English
Publishing date	2023-10-24
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2020469-3
ISSN	1439-7633 ; 1439-4227
ISSN (online)	1439-7633
ISSN	1439-4227
DOI	10.1002/cbic.202300515
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Characterization of aged osteocalcin fragments derived from bone resorption.

Cloos, Paul A C / Christgau, Stephan

Clinical laboratory

2004 Volume 50, Issue 9-10, Page(s) 585–598

Abstract: Introduction: Osteocalcin (OC) is a small bone matrix protein exclusively found in mineralized tissue. OC measured in serum or plasma provides an index of bone formation. In the present study a sensitive inhibition ELISA was established that could ... ...

Abstract	Introduction: Osteocalcin (OC) is a small bone matrix protein exclusively found in mineralized tissue. OC measured in serum or plasma provides an index of bone formation. In the present study a sensitive inhibition ELISA was established that could quantify fragments derived from the OC Mid-region in human urine. Methods: The ELISA was based on a monoclonal antibody directed against residues 21-29 of human OC (Mid-OC Urine ELISA). OC fragments were isolated from human urine by immunoaffinity chromatography. OC fragments were purified further by reversed phase high performance chromatography for characterization by N-terminal sequencing and mass-spectrometry. OC fragments were assayed in bone cell culture supernatants and in serum and urine from patients undergoing anti-resorptive bisphosphonate therapy using the Mid-OC urine ELISA. Results and conclusion: It was demonstrated that the release of OC fragments was highly correlated with osteoclast-mediated pit formation (r2= 0.89) and with an established marker of bone resorption (CTX; r2=0.91). Mid-OC values were decreased markedly after 3 and 10 days of anti-resorptive bisphosphonate treatment further indicating that the marker reflects bone resorption. The molecular characterization revealed that most of these molecules were less than 15 amino acids in length and many contained modified aspartyl residues (D-aspartyl and isoaspartyl) characteristic of aged proteins. The presence of such modifications shows that these molecules have resided in the bone matrix for an extended period and thus they cannot be derived directly from bone formation. In conclusion, these findings demonstrate that OC-fragments are released during osteoclastic bone resorption and that the quantification of specific age-modified OC fragments can provide an index of bone resorption.
MeSH term(s)	Adult ; Bone Resorption/urine ; Bone and Bones/metabolism ; Enzyme-Linked Immunosorbent Assay/methods ; Female ; Humans ; Male ; Middle Aged ; Osteitis Deformans/blood ; Osteitis Deformans/urine ; Osteocalcin/urine ; Peptide Fragments/urine
Chemical Substances	Peptide Fragments ; Osteocalcin (104982-03-8)
Language	English
Publishing date	2004
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1307629-2
ISSN	1433-6510 ; 0941-2131
ISSN	1433-6510 ; 0941-2131
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Ud II Zs.170: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Zs.MO 25: Show issues

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Article: Post-translational modifications of proteins: implications for aging, antigen recognition, and autoimmunity.

Cloos, Paul A C / Christgau, Stephan

Biogerontology

2004 Volume 5, Issue 3, Page(s) 139–158

Abstract: Proteins are complex organic molecules susceptible to numerous post-translational modifications occurring spontaneously during aging or as a consequence of physiologic or pathologic processes. Antigenicity and interactions of proteins with components of ... ...

Abstract	Proteins are complex organic molecules susceptible to numerous post-translational modifications occurring spontaneously during aging or as a consequence of physiologic or pathologic processes. Antigenicity and interactions of proteins with components of the immune system may be profoundly affected by post-translational modifications. Thus, modified self-antigens may be absent (not-tolerated) during early T-cell selection and trigger reactions by the immune system as they arise later in life. In turn, this may play a role in the initiation and pathogenesis of autoimmune diseases. This Review article presents an overview of protein modifications that have been shown to affect antigenicity and presentation of protein antigens in autoimmune diseases. The relevance of these observations is discussed, and the implications for future prophylactic and therapeutic interventions are outlined.
MeSH term(s)	Aging/metabolism ; Antigens/immunology ; Autoimmunity ; Glycosylation ; Humans ; Isomerism ; Major Histocompatibility Complex ; Oxidative Stress ; Phosphorylation ; Protein Processing, Post-Translational ; Proteins/immunology ; Proteins/metabolism ; Stereoisomerism
Chemical Substances	Antigens ; Proteins
Language	English
Publishing date	2004
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	2047160-9
ISSN	1389-5729
ISSN	1389-5729
DOI	10.1023/B:BGEN.0000031152.31352.8b
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Zs.A 5706: Show issues

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Article: Current and future applications of bone turnover markers.

Christgau, Stephan / Cloos, Paul A C

Clinical laboratory

2003 Volume 49, Issue 9-10, Page(s) 439–446

MeSH term(s)	Biomarkers ; Bone Remodeling ; Bone Resorption ; Female ; Humans ; Male ; Osteogenesis ; Reagent Kits, Diagnostic
Chemical Substances	Biomarkers ; Reagent Kits, Diagnostic
Language	English
Publishing date	2003
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	1307629-2
ISSN	1433-6510 ; 0941-2131
ISSN	1433-6510 ; 0941-2131
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Article: Non-enzymatic covalent modifications of proteins: mechanisms, physiological consequences and clinical applications.

Cloos, Paul A C / Christgau, Stephan

Matrix biology : journal of the International Society for Matrix Biology

2002 Volume 21, Issue 1, Page(s) 39–52

Abstract: Given the complexity of the biosynthetic machinery and the delicate chemical composition of proteins, it is remarkable that cells manage to produce and maintain normally functioning proteins under most conditions. However, it is now well known that ... ...

Abstract	Given the complexity of the biosynthetic machinery and the delicate chemical composition of proteins, it is remarkable that cells manage to produce and maintain normally functioning proteins under most conditions. However, it is now well known that proteins are susceptible to various non-enzymatic covalent modifications (NECM) under physiological conditions. Such modifications can be of no or little importance to the protein or they can be absolutely detrimental. Often NECM are difficult to study due to the complex and technically demanding methods required to identify many of these modifications. Thus, the role of NECM has not yet been adequately resolved but recent research has allowed a better understanding of such modifications. The present review outlines the various forms of NECM that involve covalent modifications of proteins, and discusses their relevance, biological impact and potential applications in the study of protein turnover and diagnosis of disease.
MeSH term(s)	Animals ; Cross-Linking Reagents ; Glycation End Products, Advanced/chemistry ; Glycation End Products, Advanced/physiology ; Humans ; Isomerism ; Oxidation-Reduction ; Protein Conformation ; Proteins/chemistry ; Proteins/physiology
Chemical Substances	Cross-Linking Reagents ; Glycation End Products, Advanced ; Proteins
Language	English
Publishing date	2002-01-17
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	1183793-7
ISSN	1569-1802 ; 0945-053X
ISSN (online)	1569-1802
ISSN	0945-053X
DOI	10.1016/s0945-053x(01)00188-3
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Article ; Online: The Demethylase JMJD2C Localizes to H3K4me3-Positive Transcription Start Sites and Is Dispensable for Embryonic Development

Pedersen, Marianne Terndrup / Agger, Karl / Laugesen, Anne / Johansen, Jens V. / Cloos, Paul A. C. / Christensen, Jesper / Helin, Kristian

Molecular and Cellular Biology. 2014 Mar. 1, v. 34, no. 6 p.1031-1045

2014

Abstract: The histone demethylase JMJD2C, also known as KDM4C/GASC1, has activity against methylated H3K9 and H3K36 and is amplified and/or overexpressed in human cancers. By the generation of Jmjd2c knockout mice, we demonstrate that loss of Jmjd2c is compatible ... ...

Abstract	The histone demethylase JMJD2C, also known as KDM4C/GASC1, has activity against methylated H3K9 and H3K36 and is amplified and/or overexpressed in human cancers. By the generation of Jmjd2c knockout mice, we demonstrate that loss of Jmjd2c is compatible with cellular proliferation, embryonic stem cell (ESC) self-renewal, and embryonic development. Moreover, we report that JMJD2C localizes to H3K4me3-positive transcription start sites in both primary cells and in the human carcinoma KYSE150 cell line containing an amplification of the JMJD2C locus. Binding is dependent on the double Tudor domain of JMJD2C, which recognizes H3K4me3 but not H4K20me2/me3 in vitro, showing a binding specificity different from that of the double Tudor domains of JMJD2A and JMJD2B. Depletion of JMJD2C in KYSE150 cells has a modest effect on H3K9me3 and H3K36me3 levels but impairs proliferation and leads to deregulated expression of a subset of target genes involved in cell cycle progression. Taking these findings together, we show that JMJD2C is targeted to H3K4me3-positive transcription start sites, where it can contribute to transcriptional regulation, and report that the putative oncogene JMJD2C generally is not required for cellular proliferation or embryonic development.
Keywords	carcinoma ; cell cycle ; cell lines ; cell proliferation ; embryogenesis ; embryonic stem cells ; histone demethylases ; humans ; loci ; methylation ; oncogenes ; transcription (genetics)
Language	English
Dates of publication	2014-0301
Size	p. 1031-1045.
Publishing place	Taylor & Francis
Document type	Article ; Online
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.00864-13
Database	NAL-Catalogue (AGRICOLA)

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Zs.A 1666: Show issues

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Article: Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease.

Cloos, Paul A C / Christensen, Jesper / Agger, Karl / Helin, Kristian

Genes & development

2008 Volume 22, Issue 9, Page(s) 1115–1140

Abstract: The enzymes catalyzing lysine and arginine methylation of histones are essential for maintaining transcriptional programs and determining cell fate and identity. Until recently, histone methylation was regarded irreversible. However, within the last few ... ...

Abstract	The enzymes catalyzing lysine and arginine methylation of histones are essential for maintaining transcriptional programs and determining cell fate and identity. Until recently, histone methylation was regarded irreversible. However, within the last few years, several families of histone demethylases erasing methyl marks associated with gene repression or activation have been identified, underscoring the plasticity and dynamic nature of histone methylation. Recent discoveries have revealed that histone demethylases take part in large multiprotein complexes synergizing with histone deacetylases, histone methyltransferases, and nuclear receptors to control developmental and transcriptional programs. Here we review the emerging biochemical and biological functions of the histone demethylases and discuss their potential involvement in human diseases, including cancer.
MeSH term(s)	Aging ; Animals ; Cell Differentiation ; Histones/metabolism ; Humans ; Methylation ; Models, Biological ; Neoplasms/metabolism ; Neoplasms/pathology ; Oxidoreductases, N-Demethylating/classification ; Oxidoreductases, N-Demethylating/metabolism ; Phylogeny
Chemical Substances	Histones ; Oxidoreductases, N-Demethylating (EC 1.5.-)
Language	English
Publishing date	2008-05-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	806684-x
ISSN	1549-5477 ; 0890-9369
ISSN (online)	1549-5477
ISSN	0890-9369
DOI	10.1101/gad.1652908
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Zs.A 2292: 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 54: Show issues

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Article ; Online: Mutant FOXL2

Weis-Banke, Stine E / Lerdrup, Mads / Kleine-Kohlbrecher, Daniela / Mohammad, Faizaan / Sidoli, Simone / Jensen, Ole N / Yanase, Toshihiko / Nakamura, Tomoko / Iwase, Akira / Stylianou, Anthe / Abu-Rustum, Nadeem R / Aghajanian, Carol / Soslow, Robert / Da Cruz Paula, Arnaud / Koche, Richard P / Weigelt, Britta / Christensen, Jesper / Helin, Kristian / Cloos, Paul A C

Cancer research

2020 Volume 80, Issue 17, Page(s) 3466–3479

Abstract: The mutant protein ... ...

Abstract	The mutant protein FOXL2
MeSH term(s)	Cell Line, Tumor ; Cells, Cultured ; Epithelial-Mesenchymal Transition/genetics ; Female ; Forkhead Box Protein L2/genetics ; Forkhead Box Protein L2/metabolism ; Gene Expression Regulation, Neoplastic/genetics ; Granulosa Cell Tumor/genetics ; Granulosa Cell Tumor/metabolism ; Granulosa Cell Tumor/pathology ; Humans ; Mutation ; Smad Proteins/metabolism ; Smad2 Protein/metabolism ; Smad3 Protein/metabolism ; Smad4 Protein/metabolism
Chemical Substances	FOXL2 protein, human ; Forkhead Box Protein L2 ; SMAD2 protein, human ; SMAD3 protein, human ; SMAD4 protein, human ; Smad Proteins ; Smad2 Protein ; Smad3 Protein ; Smad4 Protein
Language	English
Publishing date	2020-07-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1432-1
ISSN	1538-7445 ; 0008-5472
ISSN (online)	1538-7445
ISSN	0008-5472
DOI	10.1158/0008-5472.CAN-20-0259
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Article: The emerging functions of histone demethylases.

Agger, Karl / Christensen, Jesper / Cloos, Paul A C / Helin, Kristian

Current opinion in genetics & development

2008 Volume 18, Issue 2, Page(s) 159–168

Abstract: Epigenetic information refers to heritable changes in gene function that are stable between cell divisions but which is not a result of changes in the DNA sequence. Part of the epigenetic mechanism has been ascribed to modifications of histones or DNA ... ...

Abstract	Epigenetic information refers to heritable changes in gene function that are stable between cell divisions but which is not a result of changes in the DNA sequence. Part of the epigenetic mechanism has been ascribed to modifications of histones or DNA that affects the transcription of specific genes. In this context, post-translational modifications of histone tails, in particular methylation of lysines, are regarded as important for the storage of epigenetic information. Regulation of this information plays an important role during cellular differentiation where cells with different characteristic features evolve from the same ancestor, despite identical genomic material. The characterization of several enzymes catalyzing histone lysine methylation have supported this concept by showing the requirement of these enzymes for normal development and their involvement in diseases such as cancer. The recent identification of proteins with histone demethylase activity has shown that the methylated mark is much more dynamic than previously anticipated, thereby potentially challenging the concept of histone-methylation in stable epigenetic programming.
MeSH term(s)	Animals ; Histones/metabolism ; Humans ; Methylation ; Oxidoreductases, N-Demethylating/classification ; Oxidoreductases, N-Demethylating/genetics ; Oxidoreductases, N-Demethylating/metabolism ; Phylogeny
Chemical Substances	Histones ; Oxidoreductases, N-Demethylating (EC 1.5.-)
Language	English
Publishing date	2008-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1077312-5
ISSN	1879-0380 ; 0959-437X
ISSN (online)	1879-0380
ISSN	0959-437X
DOI	10.1016/j.gde.2007.12.003
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Article ; Online: The demethylase JMJD2C localizes to H3K4me3-positive transcription start sites and is dispensable for embryonic development.

Pedersen, Marianne Terndrup / Agger, Karl / Laugesen, Anne / Johansen, Jens V / Cloos, Paul A C / Christensen, Jesper / Helin, Kristian

Molecular and cellular biology

2014 Volume 34, Issue 6, Page(s) 1031–1045

Abstract	The histone demethylase JMJD2C, also known as KDM4C/GASC1, has activity against methylated H3K9 and H3K36 and is amplified and/or overexpressed in human cancers. By the generation of Jmjd2c knockout mice, we demonstrate that loss of Jmjd2c is compatible with cellular proliferation, embryonic stem cell (ESC) self-renewal, and embryonic development. Moreover, we report that JMJD2C localizes to H3K4me3-positive transcription start sites in both primary cells and in the human carcinoma KYSE150 cell line containing an amplification of the JMJD2C locus. Binding is dependent on the double Tudor domain of JMJD2C, which recognizes H3K4me3 but not H4K20me2/me3 in vitro, showing a binding specificity different from that of the double Tudor domains of JMJD2A and JMJD2B. Depletion of JMJD2C in KYSE150 cells has a modest effect on H3K9me3 and H3K36me3 levels but impairs proliferation and leads to deregulated expression of a subset of target genes involved in cell cycle progression. Taking these findings together, we show that JMJD2C is targeted to H3K4me3-positive transcription start sites, where it can contribute to transcriptional regulation, and report that the putative oncogene JMJD2C generally is not required for cellular proliferation or embryonic development.
MeSH term(s)	Animals ; Cell Cycle/genetics ; Cell Line ; Cell Line, Tumor ; Cell Proliferation ; Embryonic Development/genetics ; Embryonic Stem Cells/metabolism ; Female ; Histone Deacetylases/genetics ; Histone Deacetylases/metabolism ; Histones/genetics ; Histones/metabolism ; Humans ; Jumonji Domain-Containing Histone Demethylases/genetics ; Mice ; Mice, Inbred C57BL ; Protein Binding/genetics ; Transcription Initiation Site ; Transcription, Genetic/genetics
Chemical Substances	Histones ; Jumonji Domain-Containing Histone Demethylases (EC 1.14.11.-) ; Histone Deacetylases (EC 3.5.1.98)
Language	English
Publishing date	2014-01-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.00864-13
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