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Article ; Online: Molecular markers associated with cognitive impairment in centenarians.

Stevnsner, Tinna / Sanchez-Roman, Ines

Aging

2022 Volume 14, Issue 10, Page(s) 4191–4192

MeSH term(s)	Aged, 80 and over ; Centenarians ; Cognition ; Cognitive Dysfunction/epidemiology ; Cognitive Dysfunction/genetics ; Humans ; Mental Status and Dementia Tests
Language	English
Publishing date	2022-05-18
Publishing country	United States
Document type	Journal Article
ISSN	1945-4589
ISSN (online)	1945-4589
DOI	10.18632/aging.204094
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Article ; Online: Measuring the Activity of DNA Repair Enzymes in Isolated Mitochondria.

Ferrando, Beatriz / Møller, Ian Max / Stevnsner, Tinna

Methods in molecular biology (Clifton, N.J.)

2021 Volume 2363, Page(s) 321–334

Abstract: Nuclear, mitochondrial and plastidic DNA is constantly exposed to conditions, such as ultraviolet radiation or reactive oxygen species, which will induce chemical modifications to the nucleotides. Unless repaired, these modifications can lead to ... ...

Abstract	Nuclear, mitochondrial and plastidic DNA is constantly exposed to conditions, such as ultraviolet radiation or reactive oxygen species, which will induce chemical modifications to the nucleotides. Unless repaired, these modifications can lead to mutations, so the nucleus, mitochondria and plastids each contains a number of DNA repair systems. We here describe assays for measuring the enzyme activities associated with the base-excision repair pathway in potato tuber mitochondria. As the name implies, this pathway involves removing a modified base and replacing it with an undamaged base. Activity of each of the enzymes involved, DNA glycosylase, apurinic/apyrimidinic endonuclease, DNA polymerase and DNA ligase can be measured by incubating a mitochondrial extract with a specifically designed oligonucleotide. After incubation, the reaction mixture is separated on a polyacrylamide gel, and the amounts of specific products formed is estimated by autoradiography, which makes it possible to calculate the enzymatic activity.
MeSH term(s)	DNA Glycosylases/genetics ; DNA Glycosylases/metabolism ; DNA Repair ; DNA Repair Enzymes/genetics ; DNA, Mitochondrial ; DNA-(Apurinic or Apyrimidinic Site) Lyase/genetics ; DNA-(Apurinic or Apyrimidinic Site) Lyase/metabolism ; Mitochondria/genetics ; Mitochondria/metabolism ; Ultraviolet Rays
Chemical Substances	DNA, Mitochondrial ; DNA Glycosylases (EC 3.2.2.-) ; DNA-(Apurinic or Apyrimidinic Site) Lyase (EC 4.2.99.18) ; DNA Repair Enzymes (EC 6.5.1.-)
Language	English
Publishing date	2021-01-11
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-1653-6_21
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Article: Phosphorylation of the Human DNA Glycosylase NEIL2 Is Affected by Oxidative Stress and Modulates Its Activity.

Myrup Holst, Camilla / Brøndum Andersen, Nanna / Thinggaard, Vibeke / Tilken, Mine / Lautrup, Sofie / Tesauro, Cinzia / Stevnsner, Tinna

Antioxidants (Basel, Switzerland)

2023 Volume 12, Issue 2

Abstract: The DNA glycosylase NEIL2 plays a central role in maintaining genome integrity, in particular during oxidative stress, by recognizing oxidized base lesions and initiating repair of these via the base excision repair (BER) pathway. Post-translational ... ...

Abstract	The DNA glycosylase NEIL2 plays a central role in maintaining genome integrity, in particular during oxidative stress, by recognizing oxidized base lesions and initiating repair of these via the base excision repair (BER) pathway. Post-translational modifications are important molecular switches that regulate and coordinate the BER pathway, and thereby enable a rapid and fine-tuned response to DNA damage. Here, we report for the first time that human NEIL2 is regulated by phosphorylation. We demonstrate that NEIL2 is phosphorylated by the two kinases cyclin-dependent kinase 5 (CDK5) and protein kinase C (PKC) in vitro and in human SH-SY5Y neuroblastoma cells. The phosphorylation of NEIL2 by PKC causes a substantial reduction in NEIL2 repair activity, while CDK5 does not directly alter the enzymatic activity of NEIL2 in vitro, suggesting distinct modes of regulating NEIL2 function by the two kinases. Interestingly, we show a rapid dephosphorylation of NEIL2 in response to oxidative stress in SH-SY5Y cells. This points to phosphorylation as an important modulator of NEIL2 function in this cellular model, not least during oxidative stress.
Language	English
Publishing date	2023-02-02
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2704216-9
ISSN	2076-3921
ISSN	2076-3921
DOI	10.3390/antiox12020355
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Article ; Online: Phosphorylation of the Human DNA Glycosylase NEIL2 Is Affected by Oxidative Stress and Modulates Its Activity

Myrup Holst, Camilla / Brøndum Andersen, Nanna / Thinggaard, Vibeke / Tilken, Mine / Lautrup, Sofie / Tesauro, Cinzia / Stevnsner, Tinna

Antioxidants. 2023 Feb. 02, v. 12, no. 2

2023

Abstract	The DNA glycosylase NEIL2 plays a central role in maintaining genome integrity, in particular during oxidative stress, by recognizing oxidized base lesions and initiating repair of these via the base excision repair (BER) pathway. Post-translational modifications are important molecular switches that regulate and coordinate the BER pathway, and thereby enable a rapid and fine-tuned response to DNA damage. Here, we report for the first time that human NEIL2 is regulated by phosphorylation. We demonstrate that NEIL2 is phosphorylated by the two kinases cyclin-dependent kinase 5 (CDK5) and protein kinase C (PKC) in vitro and in human SH-SY5Y neuroblastoma cells. The phosphorylation of NEIL2 by PKC causes a substantial reduction in NEIL2 repair activity, while CDK5 does not directly alter the enzymatic activity of NEIL2 in vitro, suggesting distinct modes of regulating NEIL2 function by the two kinases. Interestingly, we show a rapid dephosphorylation of NEIL2 in response to oxidative stress in SH-SY5Y cells. This points to phosphorylation as an important modulator of NEIL2 function in this cellular model, not least during oxidative stress.
Keywords	DNA damage ; DNA glycosylases ; DNA repair ; cyclin-dependent kinase ; dephosphorylation ; enzyme activity ; genome ; humans ; models ; oxidation ; oxidative stress ; phosphorylation ; protein kinase C
Language	English
Dates of publication	2023-0202
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article ; Online
ZDB-ID	2704216-9
ISSN	2076-3921
ISSN	2076-3921
DOI	10.3390/antiox12020355
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Article ; Online: Bowhead NEIL1: molecular cloning, characterization, and enzymatic properties.

Holm, Signe / Larsen, Rikke Møller / Holst, Camilla Myrup / Heide-Jørgensen, Mads Peter / Steffensen, John Fleng / Stevnsner, Tinna / Larsen, Knud

Biochimie

2022 Volume 206, Page(s) 136–149

Abstract: Nei Like DNA Glycosylase 1 (NEIL1) is a DNA glycosylase, which specifically processes oxidative DNA damage by initiating base excision repair. NEIL1 recognizes and removes bases, primarily oxidized pyrimidines, which have been damaged by endogenous ... ...

Abstract	Nei Like DNA Glycosylase 1 (NEIL1) is a DNA glycosylase, which specifically processes oxidative DNA damage by initiating base excision repair. NEIL1 recognizes and removes bases, primarily oxidized pyrimidines, which have been damaged by endogenous oxidation or exogenous mutagenic agents. NEIL1 functions through a combined glycosylase/AP (apurinic/apyrimidinic)-lyase activity, whereby it cleaves the N-glycosylic bond between the DNA backbone and the damaged base via its glycosylase activity and hydrolysis of the DNA backbone through beta-delta elimination due to its AP-lyase activity. In our study we investigated our hypothesis proposing that the cancer resistance of the bowhead whale can be associated with a better DNA repair with NEIL1 being upregulated or more active. Here, we report the molecular cloning and characterization of three transcript variants of bowhead whale NEIL1 of which two were homologous to human transcripts. In addition, a novel NEIL1 transcript variant was found. A differential expression of NEIL mRNA was detected in bowhead eye, liver, kidney, and muscle. The A-to-I editing of NEIL1 mRNA was shown to be conserved in the bowhead and two adenosines in the 242Lys codon were subjected to editing. A mass spectroscopy analysis of liver and eye tissue failed to demonstrate the existence of a NEIL1 isoform originating from RNA editing. Recombinant bowhead and human NEIL1 were expressed in E. coli and assayed for enzymatic activity. Both bowhead and human recombinant NEIL1 catalyzed, with similar efficiency, the removal of a 5-hydroxyuracil lesion in a DNA bubble structure. Hence, these results do not support our hypothesis but do not refute the hypothesis either.
MeSH term(s)	Animals ; Humans ; Bowhead Whale/genetics ; Bowhead Whale/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; DNA Repair ; DNA Glycosylases/genetics ; DNA Glycosylases/chemistry ; DNA Glycosylases/metabolism ; Cloning, Molecular ; DNA ; RNA, Messenger ; Lyases/metabolism ; Escherichia coli Proteins/genetics ; Deoxyribonuclease (Pyrimidine Dimer)/genetics ; Deoxyribonuclease (Pyrimidine Dimer)/metabolism
Chemical Substances	DNA Glycosylases (EC 3.2.2.-) ; DNA (9007-49-2) ; RNA, Messenger ; Lyases (EC 4.-) ; NEIL1 protein, human (EC 3.2.2.-) ; Nei protein, E coli (EC 3.1.25.1) ; Escherichia coli Proteins ; Deoxyribonuclease (Pyrimidine Dimer) (EC 3.1.25.1)
Language	English
Publishing date	2022-11-02
Publishing country	France
Document type	Journal Article
ZDB-ID	120345-9
ISSN	1638-6183 ; 0300-9084
ISSN (online)	1638-6183
ISSN	0300-9084
DOI	10.1016/j.biochi.2022.10.014
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Article ; Online: The role of aging and brain-derived neurotrophic factor signaling in expression of base excision repair genes in the human brain.

Lautrup, Sofie / Myrup Holst, Camilla / Yde, Anne / Asmussen, Stine / Thinggaard, Vibeke / Larsen, Knud / Laursen, Lisbeth Schmidt / Richner, Mette / Vaegter, Christian B / Prieto, G Aleph / Berchtold, Nicole / Cotman, Carl W / Stevnsner, Tinna

Aging cell

2023 Volume 22, Issue 9, Page(s) e13905

Abstract: DNA damage is a central contributor to the aging process. In the brain, a major threat to the DNA is the considerable amount of reactive oxygen species produced, which can inflict oxidative DNA damage. This type of damage is removed by the base excision ... ...

Abstract	DNA damage is a central contributor to the aging process. In the brain, a major threat to the DNA is the considerable amount of reactive oxygen species produced, which can inflict oxidative DNA damage. This type of damage is removed by the base excision repair (BER) pathway, an essential DNA repair mechanism, which contributes to genome stability in the brain. Despite the crucial role of the BER pathway, insights into how this pathway is affected by aging in the human brain and the underlying regulatory mechanisms are very limited. By microarray analysis of four cortical brain regions from humans aged 20-99 years (n = 57), we show that the expression of core BER genes is largely downregulated during aging across brain regions. Moreover, we find that expression of many BER genes correlates positively with the expression of the neurotrophin brain-derived neurotrophic factor (BDNF) in the human brain. In line with this, we identify binding sites for the BDNF-activated transcription factor, cyclic-AMP response element-binding protein (CREB), in the promoter of most BER genes and confirm the ability of BDNF to regulate several BER genes by BDNF treatment of mouse primary hippocampal neurons. Together, these findings uncover the transcriptional landscape of BER genes during aging of the brain and suggest BDNF as an important regulator of BER in the human brain.
MeSH term(s)	Animals ; Humans ; Mice ; Aging/genetics ; Aging/metabolism ; Brain/metabolism ; Brain-Derived Neurotrophic Factor/genetics ; Brain-Derived Neurotrophic Factor/metabolism ; DNA Repair/genetics ; Signal Transduction/genetics
Chemical Substances	Brain-Derived Neurotrophic Factor ; BDNF protein, human (7171WSG8A2)
Language	English
Publishing date	2023-06-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2113083-8
ISSN	1474-9726 ; 1474-9718
ISSN (online)	1474-9726
ISSN	1474-9718
DOI	10.1111/acel.13905
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Article: Role of Estrogen and Other Sex Hormones in Brain Aging. Neuroprotection and DNA Repair.

Zárate, Sandra / Stevnsner, Tinna / Gredilla, Ricardo

Frontiers in aging neuroscience

2017 Volume 9, Page(s) 430

Abstract: Aging is an inevitable biological process characterized by a progressive decline in physiological function and increased susceptibility to disease. The detrimental effects of aging are observed in all tissues, the brain being the most important one due ... ...

Abstract	Aging is an inevitable biological process characterized by a progressive decline in physiological function and increased susceptibility to disease. The detrimental effects of aging are observed in all tissues, the brain being the most important one due to its main role in the homeostasis of the organism. As our knowledge about the underlying mechanisms of brain aging increases, potential approaches to preserve brain function rise significantly. Accumulating evidence suggests that loss of genomic maintenance may contribute to aging, especially in the central nervous system (CNS) owing to its low DNA repair capacity. Sex hormones, particularly estrogens, possess potent antioxidant properties and play important roles in maintaining normal reproductive and non-reproductive functions. They exert neuroprotective actions and their loss during aging and natural or surgical menopause is associated with mitochondrial dysfunction, neuroinflammation, synaptic decline, cognitive impairment and increased risk of age-related disorders. Moreover, loss of sex hormones has been suggested to promote an accelerated aging phenotype eventually leading to the development of brain hypometabolism, a feature often observed in menopausal women and prodromal Alzheimer's disease (AD). Although data on the relation between sex hormones and DNA repair mechanisms in the brain is still limited, various investigations have linked sex hormone levels with different DNA repair enzymes. Here, we review estrogen anti-aging and neuroprotective mechanisms, which are currently an area of intense study, together with the effect they may have on the DNA repair capacity in the brain.
Language	English
Publishing date	2017-12-22
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2558898-9
ISSN	1663-4365
ISSN	1663-4365
DOI	10.3389/fnagi.2017.00430
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Article ; Online: Endothelin-1 induces a strong pressor effect in ball pythons (Python regius).

Jensen, Maja Fuhlendorff / Nedergaard, Signe / Nielsen, Hang Nguyen / Skovgaard, Nini / Stevnsner, Tinna V / Wang, Tobias

Comparative biochemistry and physiology. Part A, Molecular & integrative physiology

2019 Volume 241, Page(s) 110620

Abstract: Endothelin-1 (ET-1) is a very potent vasoactive peptide released from endothelial cells, and ET-1 plays an important role in the maintenance and regulation of blood pressure in mammals. ET-1 signaling is mediated by two receptors: ... ...

Abstract	Endothelin-1 (ET-1) is a very potent vasoactive peptide released from endothelial cells, and ET-1 plays an important role in the maintenance and regulation of blood pressure in mammals. ET-1 signaling is mediated by two receptors: ET
MeSH term(s)	Animals ; Blood Pressure/drug effects ; Boidae/physiology ; Endothelin Receptor Antagonists/pharmacology ; Endothelin-1/pharmacology ; Mesenteric Arteries/drug effects ; Nitric Oxide/metabolism ; Pulmonary Artery/drug effects ; Receptors, Endothelin/chemistry ; Receptors, Endothelin/genetics ; Receptors, Endothelin/metabolism ; Vasoconstriction/drug effects ; Vasodilation/drug effects
Chemical Substances	Endothelin Receptor Antagonists ; Endothelin-1 ; Receptors, Endothelin ; Nitric Oxide (31C4KY9ESH)
Language	English
Publishing date	2019-11-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	121246-1
ISSN	1531-4332 ; 0300-9629 ; 1095-6433
ISSN (online)	1531-4332
ISSN	0300-9629 ; 1095-6433
DOI	10.1016/j.cbpa.2019.110620
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Article ; Online: The Caenorhabditis elegans Werner syndrome protein participates in DNA damage checkpoint and DNA repair in response to CPT-induced double-strand breaks.

Hyun, Moonjung / Choi, Seoyun / Stevnsner, Tinna / Ahn, Byungchan

Cellular signalling

2016 Volume 28, Issue 3, Page(s) 214–223

Abstract: The RecQ helicases play roles in maintenance of genomic stability in species ranging from Escherichia coli to humans and interact with proteins involved in DNA metabolic pathways such as DNA repair, recombination, and replication. Our previous studies ... ...

Abstract	The RecQ helicases play roles in maintenance of genomic stability in species ranging from Escherichia coli to humans and interact with proteins involved in DNA metabolic pathways such as DNA repair, recombination, and replication. Our previous studies found that the Caenorhabditis elegans WRN-1 RecQ protein (a human WRN ortholog) exhibits ATP-dependent 3'-5' helicase activity and that the WRN-1 helicase is stimulated by RPA-1 on a long forked DNA duplex. However, the role of WRN-1 in response to S-phase associated with DSBs is unclear. We found that WRN-1 is involved in the checkpoint response to DSBs after CPT, inducing cell cycle arrest, is recruited to DSBs by RPA-1 and functions upstream of ATL-1 and ATM-1 for CHK-1 phosphorylation in the S-phase checkpoint. In addition, WRN-1 and RPA-1 recruitments to the DSBs require MRE-11, suggesting that DSB processing controlled by MRE-11 is important for WRN-1 at DSBs. The repair of CPT-induced DSBs is greatly reduced in the absence of WRN-1. These observations suggest that WRN-1 functions downstream of RPA-1 and upstream of CHK-1 in the DSB checkpoint pathway and is also required for the repair of DSB.
MeSH term(s)	Animals ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/antagonists & inhibitors ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Camptothecin/toxicity ; Checkpoint Kinase 1 ; Comet Assay ; DNA Breaks, Double-Stranded/drug effects ; DNA Helicases/genetics ; DNA Helicases/metabolism ; DNA Repair ; Mutagenesis ; Protein Kinases/chemistry ; Protein Kinases/genetics ; Protein Kinases/metabolism ; RNA Interference ; Replication Protein A/antagonists & inhibitors ; Replication Protein A/genetics ; Replication Protein A/metabolism ; S Phase Cell Cycle Checkpoints/drug effects
Chemical Substances	Caenorhabditis elegans Proteins ; Replication Protein A ; mre-11 protein, C elegans ; Protein Kinases (EC 2.7.-) ; Checkpoint Kinase 1 (EC 2.7.11.1) ; chk-1 protein, C elegans (EC 2.7.11.1) ; DNA Helicases (EC 3.6.4.-) ; WRN-1 protein, C elegans (EC 5.99.-) ; Camptothecin (XT3Z54Z28A)
Language	English
Publishing date	2016-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1002702-6
ISSN	1873-3913 ; 0898-6568
ISSN (online)	1873-3913
ISSN	0898-6568
DOI	10.1016/j.cellsig.2015.12.006
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Article ; Online: Mitochondrial base excision repair assays.

Gredilla, Ricardo / Stevnsner, Tinna

Methods in molecular biology (Clifton, N.J.)

2012 Volume 920, Page(s) 289–304

Abstract: Mitochondrial DNA (mtDNA) is constantly exposed to oxidative injury. Due to its location close to the main site of reactive oxygen species, the inner mitochondrial membrane, mtDNA is more susceptible than nuclear DNA to oxidative damage. The accumulation ...

Abstract	Mitochondrial DNA (mtDNA) is constantly exposed to oxidative injury. Due to its location close to the main site of reactive oxygen species, the inner mitochondrial membrane, mtDNA is more susceptible than nuclear DNA to oxidative damage. The accumulation of DNA damage is thought to be particularly deleterious in post-mitotic cells, including neurons, and to play a critical role in the aging process and in a variety of diseases. Thus, efficient mtDNA repair is important for the maintenance of genomic integrity and a healthy life. The base excision repair (BER) mechanism was the first to be described in mitochondria, and consequently it is the best known. This chapter outlines protocols for isolating mitochondria from mammalian cells in culture and from rodent tissues including liver and brain. It also covers the isolation of synaptic mitochondria. BER takes place in four distinct steps, and protocols describing in vitro assays for measuring these enzymatic steps in lysates of isolated mitochondria are included.
MeSH term(s)	Animals ; Brain/cytology ; Cell Fractionation/methods ; Cells, Cultured ; DNA Glycosylases/metabolism ; DNA Polymerase gamma ; DNA Repair ; DNA-(Apurinic or Apyrimidinic Site) Lyase/metabolism ; DNA-Directed DNA Polymerase/metabolism ; Denaturing Gradient Gel Electrophoresis ; Liver/cytology ; Mice ; Mitochondria/genetics ; Mitochondrial Proteins/metabolism ; Nuclear Proteins/metabolism ; Synapses/metabolism
Chemical Substances	Mitochondrial Proteins ; Nuclear Proteins ; DNA Polymerase gamma (EC 2.7.7.7) ; DNA-Directed DNA Polymerase (EC 2.7.7.7) ; DNA Glycosylases (EC 3.2.2.-) ; DNA-(Apurinic or Apyrimidinic Site) Lyase (EC 4.2.99.18)
Language	English
Publishing date	2012
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-61779-998-3_20
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