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Article ; Online: Autobiographical sketch: A life in DNA repair—and beyond.

Krokan, Hans E

2012 Volume 11, Issue 3, Page(s) 224–235

MeSH term(s)	AlkB Homolog 2, Alpha-Ketoglutarate-Dependent Dioxygenase ; Animals ; Biochemistry/history ; Biomedical Research ; Cloning, Molecular ; DNA Repair/genetics ; DNA Repair/physiology ; DNA Repair Enzymes/genetics ; DNA Repair Enzymes/physiology ; DNA Replication/physiology ; Dioxygenases/genetics ; Dioxygenases/physiology ; Education, Medical ; History, 20th Century ; History, 21st Century ; Humans ; Industry ; Mice ; Norway ; Uracil-DNA Glycosidase/genetics ; Uracil-DNA Glycosidase/physiology
Chemical Substances	Dioxygenases (EC 1.13.11.-) ; ALKBH2 protein, human (EC 1.14.11.33) ; AlkB Homolog 2, Alpha-Ketoglutarate-Dependent Dioxygenase (EC 1.14.11.33) ; Uracil-DNA Glycosidase (EC 3.2.2.-) ; DNA Repair Enzymes (EC 6.5.1.-)
Language	English
Publishing date	2012-11-27
Publishing country	Netherlands
Document type	Autobiography ; Biography ; Historical Article ; Journal Article
ZDB-ID	2071608-4
ISSN	1568-7856 ; 1568-7864
ISSN (online)	1568-7856
ISSN	1568-7864
DOI	10.1016/j.dnarep.2011.04.014
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Article ; Online: Base excision repair.

Krokan, Hans E / Bjørås, Magnar

Cold Spring Harbor perspectives in biology

2013 Volume 5, Issue 4, Page(s) a012583

Abstract: Base excision repair (BER) corrects DNA damage from oxidation, deamination and alkylation. Such base lesions cause little distortion to the DNA helix structure. BER is initiated by a DNA glycosylase that recognizes and removes the damaged base, leaving ... ...

Abstract	Base excision repair (BER) corrects DNA damage from oxidation, deamination and alkylation. Such base lesions cause little distortion to the DNA helix structure. BER is initiated by a DNA glycosylase that recognizes and removes the damaged base, leaving an abasic site that is further processed by short-patch repair or long-patch repair that largely uses different proteins to complete BER. At least 11 distinct mammalian DNA glycosylases are known, each recognizing a few related lesions, frequently with some overlap in specificities. Impressively, the damaged bases are rapidly identified in a vast excess of normal bases, without a supply of energy. BER protects against cancer, aging, and neurodegeneration and takes place both in nuclei and mitochondria. More recently, an important role of uracil-DNA glycosylase UNG2 in adaptive immunity was revealed. Furthermore, other DNA glycosylases may have important roles in epigenetics, thus expanding the repertoire of BER proteins.
MeSH term(s)	Animals ; Cell Nucleus/metabolism ; DNA/genetics ; DNA Damage ; DNA Glycosylases/genetics ; DNA Polymerase beta/metabolism ; DNA Repair ; Epigenesis, Genetic ; Escherichia coli/enzymology ; Humans ; Mice ; Mice, Knockout ; Mitochondria/metabolism ; Models, Molecular ; Mutagenesis ; Neoplasms/enzymology ; Oxygen/chemistry ; Poly(ADP-ribose) Polymerases/metabolism ; Protein Conformation
Chemical Substances	DNA (9007-49-2) ; Poly(ADP-ribose) Polymerases (EC 2.4.2.30) ; DNA Polymerase beta (EC 2.7.7.7) ; CCNO protein, human (EC 3.2.2.-) ; DNA Glycosylases (EC 3.2.2.-) ; Oxygen (S88TT14065)
Language	English
Publishing date	2013-04-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	1943-0264
ISSN (online)	1943-0264
DOI	10.1101/cshperspect.a012583
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Article: Base excision repair efficiency and mechanism in nuclear extracts are influenced by the ratio between volume of nuclear extraction buffer and nuclei-implications for comparative studies.

Akbari, Mansour / Krokan, Hans E

Mutation research

2012 Volume 736, Issue 1-2, Page(s) 33–38

Abstract: The base excision repair (BER) pathway corrects many different DNA base lesions and is important for genomic stability. The mechanism of BER cannot easily be investigated in intact cells and therefore in vitro methods that reflect the in vivo processes ... ...

Abstract	The base excision repair (BER) pathway corrects many different DNA base lesions and is important for genomic stability. The mechanism of BER cannot easily be investigated in intact cells and therefore in vitro methods that reflect the in vivo processes are in high demand. Reconstitution of BER using purified proteins essentially mirror properties of the proteins used, and does not necessarily reflect the mechanism as it occurs in the cell. Nuclear extracts from cultured cells have the capacity to carry out complete BER and can give important information on the mechanism. Furthermore, candidate proteins in extracts can be inhibited or depleted in a controlled way, making defined extracts an important source for mechanistic studies. The major drawback is that there is no standardized method of preparing nuclear extract for BER studies, and it does not appear to be a topic given much attention. Here we have examined BER activity of nuclear cell extracts from HeLa cells, using as substrate a circular DNA molecule with either uracil or an AP-site in a defined position. We show that BER activity of nuclear extracts from the same batch of cells varies inversely with the volume of nuclear extraction buffer relative to nuclei volume, in spite of identical protein concentrations in the BER assay mixture. Surprisingly, the uracil-DNA glycosylase activity (mainly UNG2), but not amount of UNG2, also correlated negatively with the volume of extraction buffer. These studies demonstrate that the method for preparation of nuclear extract is an important factor to consider for in vitro BER analysis and conditions used in comparative studies must be carefully worked out.
MeSH term(s)	Buffers ; Cell Nucleus/chemistry ; Cell Nucleus/metabolism ; Cells, Cultured ; DNA Repair ; HeLa Cells ; Humans
Chemical Substances	Buffers
Language	English
Publishing date	2012-08-01
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	206607-5
ISSN	1873-135X ; 0027-5107 ; 1383-5718 ; 0165-1110 ; 0165-1161 ; 0165-7992 ; 0921-8777 ; 0165-1218 ; 1383-5726 ; 0167-8817 ; 0921-8734 ; 1383-5742
ISSN (online)	1873-135X
ISSN	0027-5107 ; 1383-5718 ; 0165-1110 ; 0165-1161 ; 0165-7992 ; 0921-8777 ; 0165-1218 ; 1383-5726 ; 0167-8817 ; 0921-8734 ; 1383-5742
DOI	10.1016/j.mrfmmm.2011.06.006
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Article: Cytotoxicity and mutagenicity of endogenous DNA base lesions as potential cause of human aging.

Akbari, Mansour / Krokan, Hans E

Mechanisms of ageing and development

2008 Volume 129, Issue 7-8, Page(s) 353–365

Abstract: Endogenous factors constitute a substantial source of damage to the genomic DNA. The type of damage includes a number of different base lesions and single- and double-strand breaks. Unrepaired DNA damage can give rise to mutations and may cause cell ... ...

Abstract	Endogenous factors constitute a substantial source of damage to the genomic DNA. The type of damage includes a number of different base lesions and single- and double-strand breaks. Unrepaired DNA damage can give rise to mutations and may cause cell death. A number of studies have demonstrated an association between aging and the accumulation of DNA damage. This may be attributed to reduced DNA repair with age, although this is apparently not a general feature for all types of damage and repair mechanisms. Therefore, detailed studies that improve our knowledge of DNA repair systems as well as mutagenic and toxic effects of DNA lesions will help us to gain a better insight into the mechanisms of aging. The aim of this review is to provide a brief description of cytotoxic and mutagenic endogenous DNA lesions that are mainly repaired by base excision repair and single-strand break repair pathways and to discuss the potential role of DNA lesions and DNA repair dysfunction in the onset of human aging.
MeSH term(s)	Aging/genetics ; Cell Nucleus/genetics ; DNA/chemistry ; DNA Damage ; DNA Repair ; Humans ; Mitochondria/genetics ; Mutation
Chemical Substances	DNA (9007-49-2)
Language	English
Publishing date	2008-07
Publishing country	Ireland
Document type	Journal Article ; Review
ZDB-ID	183915-9
ISSN	1872-6216 ; 0047-6374
ISSN (online)	1872-6216
ISSN	0047-6374
DOI	10.1016/j.mad.2008.01.007
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Article ; Online: Methylation damage to RNA induced in vivo in Escherichia coli is repaired by endogenous AlkB as part of the adaptive response.

Vågbø, Cathrine Broberg / Svaasand, Eva K / Aas, Per A / Krokan, Hans E

DNA repair

2013 Volume 12, Issue 3, Page(s) 188–195

Abstract: ... in vitro and in pre-damaged DNA and RNA bacteriophages in vivo are repaired by the Escherichia coli (E ... deficient E. coli strains during exposure to methyl methanesulfonate (MMS). Repair was observed both in AlkB ... by AlkB takes place in endogenous RNA as part of an adaptive response in wild-type E. coli cells. ...

Abstract	Cytotoxic 1-methyladenine (1-meA) and 3-methylcytosine (3-meC) lesions induced in DNA and RNA in vitro and in pre-damaged DNA and RNA bacteriophages in vivo are repaired by the Escherichia coli (E. coli) protein AlkB and a human homolog, ALKBH3. However, it is not known whether endogenous RNA is repaired in vivo by repair proteins present at physiological concentrations. The concept of RNA repair as a biologically relevant process has therefore remained elusive. Here, we demonstrate AlkB-mediated repair of endogenous RNA in vivo by measuring differences in lesion-accumulation in two independent AlkB-proficient and deficient E. coli strains during exposure to methyl methanesulfonate (MMS). Repair was observed both in AlkB-overproducing strains and in the wild-type strains after AlkB induction. RNA repair appeared to be highest in RNA species below 200 nucleotides in size, mainly comprising tRNAs. Strikingly, at least 10-fold more lesions were repaired in RNA than in DNA. This may be a consequence of some 30-fold higher levels of aberrant methylation in RNA than in DNA after exposure to MMS. A high primary kinetic isotope effect (>10) was measured using a deuterated methylated RNA substrate, D3-1me(rA), demonstrating that it is the catalytic step, and not the search step that is rate-limiting. Our results demonstrate that RNA repair by AlkB takes place in endogenous RNA as part of an adaptive response in wild-type E. coli cells.
MeSH term(s)	Adaptation, Physiological/genetics ; Alkylating Agents/pharmacology ; DNA Repair ; DNA, Bacterial/genetics ; Enzyme Induction ; Escherichia coli/enzymology ; Escherichia coli/genetics ; Escherichia coli Proteins/physiology ; Kinetics ; Methyl Methanesulfonate/pharmacology ; Methylation ; Mixed Function Oxygenases/physiology ; RNA, Bacterial/genetics ; RNA, Bacterial/metabolism
Chemical Substances	Alkylating Agents ; DNA, Bacterial ; Escherichia coli Proteins ; RNA, Bacterial ; Methyl Methanesulfonate (AT5C31J09G) ; Mixed Function Oxygenases (EC 1.-) ; AlkB protein, E coli (EC 1.14.11.-)
Language	English
Publishing date	2013-03-01
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2071608-4
ISSN	1568-7856 ; 1568-7864
ISSN (online)	1568-7856
ISSN	1568-7864
DOI	10.1016/j.dnarep.2012.11.010
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Article: DNA base modifications in honey bee and fruit fly genomes suggest an active demethylation machinery with species- and tissue-specific turnover rates.

Rasmussen, Erik M K / Vågbø, Cathrine B / Münch, Daniel / Krokan, Hans E / Klungland, Arne / Amdam, Gro V / Dahl, John Arne

Biochemistry and biophysics reports

2016 Volume 6, Page(s) 9–15

Abstract: Well-known epigenetic DNA modifications in mammals include the addition of a methyl group and a hydroxyl group to cytosine, resulting in 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC) respectively. In contrast, the abundance and the functional ...

Abstract	Well-known epigenetic DNA modifications in mammals include the addition of a methyl group and a hydroxyl group to cytosine, resulting in 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC) respectively. In contrast, the abundance and the functional implications of these modifications in invertebrate model organisms such as the honey bee (
Language	English
Publishing date	2016-02-22
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2831046-9
ISSN	2405-5808
ISSN	2405-5808
DOI	10.1016/j.bbrep.2016.02.011
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Article ; Online: Red versus blue light illumination in hexyl 5-aminolevulinate photodynamic therapy: the influence of light color and irradiance on the treatment outcome in vitro.

Helander, Linda / Krokan, Hans E / Johnsson, Anders / Gederaas, Odrun A / Plaetzer, Kristjan

Journal of biomedical optics

2014 Volume 19, Issue 8, Page(s) 88002

Abstract: Hexyl 5-aminolevulinate (HAL) is a lipophilic derivative of 5-aminolevulinate, a key intermediate in biosynthesis of the photosensitizer protoporphyrin IX (PpIX). The photodynamic efficacy and cell death mode after red versus blue light illumination of ... ...

Abstract	Hexyl 5-aminolevulinate (HAL) is a lipophilic derivative of 5-aminolevulinate, a key intermediate in biosynthesis of the photosensitizer protoporphyrin IX (PpIX). The photodynamic efficacy and cell death mode after red versus blue light illumination of HAL-induced PpIX have been examined and compared using five different cancer cell lines. LED arrays emitting at 410 and 624 nm served as homogenous and adjustable light sources. Our results show that the response after HAL-PDT is cell line specific, both regarding the shape of the dose-survival curve, the overall dose required for efficient cell killing, and the relative amount of apoptosis. The ratio between 410 and 624 nm in absorption coefficient correlates well with the difference in cell killing at the same wavelengths. In general, the PDT efficacy was several folds higher for blue light as compared with red light, as expected. However, HAL-PDT₆₂₄ induced more apoptosis than HAL-PDT₄₁₀ and illumination with low irradiance resulted in more apoptosis than high irradiance at the same lethal dose. This indicates differences in death modes after low and high irradiance after similar total light doses. From a treatment perspective, these differences may be important.
MeSH term(s)	Aminolevulinic Acid/therapeutic use ; Apoptosis/drug effects ; Apoptosis/radiation effects ; Cell Line, Tumor ; Cell Survival/drug effects ; Cell Survival/radiation effects ; Color ; Dose-Response Relationship, Radiation ; Humans ; Lighting/methods ; Neoplasms, Experimental/drug therapy ; Neoplasms, Experimental/pathology ; Photochemotherapy/methods ; Radiation Dosage ; Treatment Outcome
Chemical Substances	Aminolevulinic Acid (88755TAZ87)
Language	English
Publishing date	2014-08-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1309154-2
ISSN	1560-2281 ; 1083-3668
ISSN (online)	1560-2281
ISSN	1083-3668
DOI	10.1117/1.JBO.19.8.088002
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Article ; Online: Activation-induced cytidine deaminase (AID) is localized to subnuclear domains enriched in splicing factors.

Hu, Yi / Ericsson, Ida / Doseth, Berit / Liabakk, Nina B / Krokan, Hans E / Kavli, Bodil

Experimental cell research

2014 Volume 322, Issue 1, Page(s) 178–192

Abstract: Activation-induced cytidine deaminase (AID) is the mutator enzyme in adaptive immunity. AID initiates the antibody diversification processes in activated B cells by deaminating cytosine to uracil in immunoglobulin genes. To some extent other genes are ... ...

Abstract	Activation-induced cytidine deaminase (AID) is the mutator enzyme in adaptive immunity. AID initiates the antibody diversification processes in activated B cells by deaminating cytosine to uracil in immunoglobulin genes. To some extent other genes are also targeted, which may lead to genome instability and B cell malignancy. Thus, it is crucial to understand its targeting and regulation mechanisms. AID is regulated at several levels including subcellular compartmentalization. However, the complex nuclear distribution and trafficking of AID has not been studied in detail previously. In this work, we examined the subnuclear localization of AID and its interaction partner CTNNBL1 and found that they associate with spliceosome-associated structures including Cajal bodies and nuclear speckles. Moreover, protein kinase A (PKA), which activates AID by phosphorylation at Ser38, is present together with AID in nuclear speckles. Importantly, we demonstrate that AID physically associates with the major spliceosome subunits (small nuclear ribonucleoproteins, snRNPs), as well as other essential splicing components, in addition to the transcription machinery. Based on our findings and the literature, we suggest a transcription-coupled splicing-associated model for AID targeting and activation.
MeSH term(s)	Apoptosis Regulatory Proteins/metabolism ; Cells, Cultured ; Coiled Bodies/metabolism ; Cytidine Deaminase/metabolism ; HEK293 Cells ; HeLa Cells ; Humans ; Nuclear Proteins/metabolism ; Protein Binding ; Protein Transport ; RNA Splicing ; Ribonucleoproteins, Small Nuclear/metabolism ; Spliceosomes/metabolism ; Tissue Distribution
Chemical Substances	Apoptosis Regulatory Proteins ; CTNNBL1 protein, human ; Nuclear Proteins ; Ribonucleoproteins, Small Nuclear ; AICDA (activation-induced cytidine deaminase) (EC 3.5.4.-) ; Cytidine Deaminase (EC 3.5.4.5)
Language	English
Publishing date	2014-03-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1493-x
ISSN	1090-2422 ; 0014-4827
ISSN (online)	1090-2422
ISSN	0014-4827
DOI	10.1016/j.yexcr.2014.01.004
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Article ; Online: Error-free versus mutagenic processing of genomic uracil--relevance to cancer.

Krokan, Hans E / Sætrom, Pål / Aas, Per Arne / Pettersen, Henrik Sahlin / Kavli, Bodil / Slupphaug, Geir

DNA repair

2014 Volume 19, Page(s) 38–47

Abstract: Genomic uracil is normally processed essentially error-free by base excision repair (BER), with mismatch repair (MMR) as an apparent backup for U:G mismatches. Nuclear uracil-DNA glycosylase UNG2 is the major enzyme initiating BER of uracil of U:A pairs ... ...

Abstract	Genomic uracil is normally processed essentially error-free by base excision repair (BER), with mismatch repair (MMR) as an apparent backup for U:G mismatches. Nuclear uracil-DNA glycosylase UNG2 is the major enzyme initiating BER of uracil of U:A pairs as well as U:G mismatches. Deficiency in UNG2 results in several-fold increases in genomic uracil in mammalian cells. Thus, the alternative uracil-removing glycosylases, SMUG1, TDG and MBD4 cannot efficiently complement UNG2-deficiency. A major function of SMUG1 is probably to remove 5-hydroxymethyluracil from DNA with general back-up for UNG2 as a minor function. TDG and MBD4 remove deamination products U or T mismatched to G in CpG/mCpG contexts, but may have equally or more important functions in development, epigenetics and gene regulation. Genomic uracil was previously thought to arise only from spontaneous cytosine deamination and incorporation of dUMP, generating U:G mismatches and U:A pairs, respectively. However, the identification of activation-induced cytidine deaminase (AID) and other APOBEC family members as DNA-cytosine deaminases has spurred renewed interest in the processing of genomic uracil. Importantly, AID triggers the adaptive immune response involving error-prone processing of U:G mismatches, but also contributes to B-cell lymphomagenesis. Furthermore, mutational signatures in a substantial fraction of other human cancers are consistent with APOBEC-induced mutagenesis, with U:G mismatches as prime suspects. Mutations can be caused by replicative polymerases copying uracil in U:G mismatches, or by translesion polymerases that insert incorrect bases opposite abasic sites after uracil-removal. In addition, kataegis, localized hypermutations in one strand in the vicinity of genomic rearrangements, requires APOBEC protein, UNG2 and translesion polymerase REV1. What mechanisms govern error-free versus error prone processing of uracil in DNA remains unclear. In conclusion, genomic uracil is an essential intermediate in adaptive immunity and innate antiviral responses, but may also be a fundamental cause of a wide range of malignancies.
MeSH term(s)	APOBEC-1 Deaminase ; Adaptive Immunity/genetics ; Animals ; Cytidine Deaminase/genetics ; Cytidine Deaminase/metabolism ; Cytosine/metabolism ; DNA Glycosylases/genetics ; DNA Glycosylases/metabolism ; DNA Repair/genetics ; Humans ; Lymphoma, B-Cell/genetics ; Lymphoma, B-Cell/metabolism ; Lymphoma, B-Cell/pathology ; Mutagenesis ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Nucleotidyltransferases/genetics ; Nucleotidyltransferases/metabolism ; Uracil/metabolism
Chemical Substances	Nuclear Proteins ; Uracil (56HH86ZVCT) ; Cytosine (8J337D1HZY) ; Nucleotidyltransferases (EC 2.7.7.-) ; REV1 protein, human (EC 2.7.7.-) ; CCNO protein, human (EC 3.2.2.-) ; DNA Glycosylases (EC 3.2.2.-) ; AICDA (activation-induced cytidine deaminase) (EC 3.5.4.-) ; APOBEC-1 Deaminase (EC 3.5.4.36) ; APOBEC1 protein, human (EC 3.5.4.36) ; Cytidine Deaminase (EC 3.5.4.5)
Language	English
Publishing date	2014-07
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2071608-4
ISSN	1568-7856 ; 1568-7864
ISSN (online)	1568-7856
ISSN	1568-7864
DOI	10.1016/j.dnarep.2014.03.028
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Article ; Online: Photodynamic treatment with hexyl-aminolevulinate mediates reversible thiol oxidation in core oxidative stress signaling proteins.

Helander, Linda / Sharma, Animesh / Krokan, Hans E / Plaetzer, Kristjan / Krammer, Barbara / Tortik, Nicole / Gederaas, Odrun A / Slupphaug, Geir / Hagen, Lars

Molecular bioSystems

2016 Volume 12, Issue 3, Page(s) 796–805

Abstract: Photodynamic therapy (PDT) is a highly selective two-step cancer treatment involving a photosensitizer and illumination with visible light in the presence of molecular oxygen. PDT is clinically approved worldwide for treating several premalignant ... ...

Abstract	Photodynamic therapy (PDT) is a highly selective two-step cancer treatment involving a photosensitizer and illumination with visible light in the presence of molecular oxygen. PDT is clinically approved worldwide for treating several premalignant conditions and cancer forms, especially endoscopically accessible tumors and dermatological malignancies. PDT-mediated cytotoxicity takes place via autophagy, apoptosis and necrosis, but the exact trigger mechanisms for various death-pathways are still unknown. PDT induces reactive oxygen species (ROS) through photochemical reactions. ROS can react with different macromolecules resulting in cellular damage, including oxidation of proteins. One of the known protein modifications is reversible oxidation of cysteine thiols (-SH), which in many cases constitute a redox switch to modulate protein activity and cellular signaling. Here we have examined the role of reversible oxidation of protein thiols as a potential mediator of cytotoxicity after hexylaminolevulinate-mediated photodynamic treatment (HAL-PDT) in the human epidermoid carcinoma cell line A431. Nearly 2300 proteins were found to be reversibly oxidized after HAL-PDT, of which 374 high-confidence proteins were further allocated to cellular compartments and functional networks. 115 of the high confidence proteins were associated with apoptosis and 257 have previously not been reported to be reversibly oxidized on cysteines. We find an enrichment of DNA damage checkpoint and oxidative stress response proteins. Many of these constitute potential signaling hubs in apoptosis, including ATM, p63, RSK1 p38, APE1/Ref-1 and three 14-3-3 family members. Our study represents the first comprehensive mapping of reversibly oxidized proteins subsequent to HAL-PDT. Several of the proteins constitute potentially novel redox-regulated apoptotic triggers as well as potential targets for adjuvants that may improve the efficacy of HAL-PDT and PDT using other photosensitizers.
MeSH term(s)	Aminolevulinic Acid/analogs & derivatives ; Aminolevulinic Acid/pharmacology ; Apoptosis/drug effects ; Cell Compartmentation/drug effects ; Cell Line, Tumor ; Cysteine/metabolism ; DNA Damage ; Humans ; Oxidation-Reduction/drug effects ; Oxidative Stress/drug effects ; Photochemotherapy ; Proteins/metabolism ; Reactive Oxygen Species/metabolism ; Signal Transduction/drug effects ; Sulfhydryl Compounds/metabolism
Chemical Substances	Proteins ; Reactive Oxygen Species ; Sulfhydryl Compounds ; Aminolevulinic Acid (88755TAZ87) ; 5-aminolevulinic acid hexyl ester (G7H20TKI67) ; Cysteine (K848JZ4886)
Language	English
Publishing date	2016-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2188635-0
ISSN	1742-2051 ; 1742-206X
ISSN (online)	1742-2051
ISSN	1742-206X
DOI	10.1039/c5mb00744e
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