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101 records – page 1 of 11.

Aldehyde-protein adducts in the liver as a result of ethanol-induced oxidative stress.

https://arctichealth.org/en/permalink/ahliterature10666
Source
Front Biosci. 1999 Jun 1;4:D506-13
Publication Type
Article
Date
Jun-1-1999
Author
O. Niemelä
Author Affiliation
Department of Clinical Chemistry, University of Oulu, FIN-90220 Oulu, and EP Central Hospital Laboratory, Seinäjoki, Finland. onni.niemela@epshp.fi
Source
Front Biosci. 1999 Jun 1;4:D506-13
Date
Jun-1-1999
Language
English
Publication Type
Article
Keywords
Aldehydes - immunology - metabolism
Animals
Biological Markers - analysis - blood
Disease Models, Animal
Ethanol - metabolism
Extracellular Matrix Proteins - metabolism
Humans
Liver - chemistry - metabolism
Liver Diseases - immunology - metabolism
Oxidative Stress
Protein Binding
Proteins - immunology - metabolism
Rats
Research Support, Non-U.S. Gov't
Swine
Abstract
A number of systems that generate oxygen free radicals and reactive aldehydic species are activated by excessive ethanol consumption. Recent studies from human alcoholics and from experimental animals have indicated that acetaldehyde and aldehydic products of lipid peroxidation, which are generated in such processes, can bind to proteins forming stable adducts. Adduct formation may lead to several adverse consequences, such as interference with protein function, stimulation of fibrogenesis, and induction of immune responses. The presence of protein adducts in the centrilobular region of the liver in alcohol abusers with an early phase of histological liver damage indicates that adduct formation is one of the key events in the pathogenesis of alcoholic liver disease. Dietary supplementation with fat and/or iron strikingly increases the amount of aldehyde-derived epitopes in the liver together with promotion of fibrogenesis.
PubMed ID
10352137 View in PubMed
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An intrinsically disordered domain in Polaribacter irgensii KOPRI 22228 CspB confers extraordinary freeze-tolerance.

https://arctichealth.org/en/permalink/ahliterature289779
Source
Biochem Biophys Res Commun. 2018 02 05; 496(2):374-380
Publication Type
Journal Article
Research Support, Non-U.S. Gov't
Date
02-05-2018
Author
Youn Hong Jung
Ji-Hyun Uh
Kyunghee Lee
Hana Im
Author Affiliation
Department of Molecular Biology, Sejong University, 209 Neungdong-ro, Gunja-dong, Gwangjin-gu, Seoul 05006, Republic of Korea.
Source
Biochem Biophys Res Commun. 2018 02 05; 496(2):374-380
Date
02-05-2018
Language
English
Publication Type
Journal Article
Research Support, Non-U.S. Gov't
Keywords
Adaptation, Physiological - genetics
Bacterial Proteins - chemistry - genetics - metabolism
Cloning, Molecular
Cold Temperature
DNA-Binding Proteins - chemistry - genetics - metabolism
Escherichia coli - genetics - metabolism
Flavobacteriaceae - genetics - metabolism
Gene Expression
Intrinsically Disordered Proteins - chemistry - genetics - metabolism
Liposomes - chemistry - metabolism
Mutation
Protein Binding
Protein Domains
Recombinant Proteins - chemistry - genetics - metabolism
Stress, Physiological
Abstract
Organisms living in extremely cold environments possess mechanisms to survive low temperatures. Among the known cold-induced genes, cold-shock proteins (Csps) are the most prominent. A csp-homologous gene, cspBPi, has been cloned from the Arctic bacterium Polaribacter irgensii KOPRI 22228, and overexpression of this gene greatly increased the freezing tolerance of its host. This protein consists of a unique N-terminal domain and a well conserved C-terminal cold shock domain. To elucidate the detailed mechanisms involved in the extraordinary freeze-tolerance conferred by CspBPi, we identified the responsible domain by mutational analysis. Changes of residues in the cold shock domain that are crucial for binding RNA or single-stranded DNA did not impair the ability of the host to survive freezing stress. All domain-shuffled CspBPi variants containing the N-terminal domain retained the ability to confer superior freeze-tolerance. Slow electrophoretic mobility and far-UV circular dichroism spectra of the N-terminal domain suggested an intrinsically disordered structure for this region. The N-terminal domain also bound to lipid vesicles in vitro. This lipid vesicle binding characteristic is shared with other intrinsically disordered proteins, such as a-synuclein and plant dehydrins, known to confer cold-tolerance when overexpressed, suggesting a mechanism for cold-survival through membrane binding.
PubMed ID
29330047 View in PubMed
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ARC15105 is a potent antagonist of von Willebrand factor mediated platelet activation and adhesion.

https://arctichealth.org/en/permalink/ahliterature127558
Source
Arterioscler Thromb Vasc Biol. 2012 Apr;32(4):902-9
Publication Type
Article
Date
Apr-2012
Author
Jolanta M Siller-Matula
Yahye Merhi
Jean-François Tanguay
Daniel Duerschmied
Denisa D Wagner
Kathleen E McGinness
P Shannon Pendergrast
Jou-Ku Chung
Xianbin Tian
Robert G Schaub
Bernd Jilma
Author Affiliation
Department of Cardiology, Medical University of Vienna, Austria.
Source
Arterioscler Thromb Vasc Biol. 2012 Apr;32(4):902-9
Date
Apr-2012
Language
English
Publication Type
Article
Keywords
Aged
Animals
Aptamers, Nucleotide - administration & dosage - pharmacokinetics - therapeutic use
Aptamers, Peptide - administration & dosage - pharmacokinetics - pharmacology
Austria
Biological Availability
Blood Platelets - drug effects - metabolism
Boston
Case-Control Studies
Collagen - metabolism
Cross-Sectional Studies
Dose-Response Relationship, Drug
Drug Stability
Female
Half-Life
Humans
Injections, Intravenous
Injections, Subcutaneous
Macaca fascicularis
Male
Middle Aged
Myocardial Infarction - blood
Platelet Activation - drug effects
Platelet Adhesiveness - drug effects
Platelet Aggregation Inhibitors - administration & dosage - pharmacokinetics - pharmacology
Platelet Function Tests
Protein Binding
Quebec
Rats
Swine
von Willebrand Factor - antagonists & inhibitors - metabolism
Abstract
We investigated the stability, pharmacokinetic, and pharmacodynamic profile of the 2(nd) generation anti-von Willeband factor aptamer ARC15105.
Platelet plug formation was measured by collagen/adenosine diphosphate-induced closure time with the platelet function analyzer-100 and platelet aggregation by multiple electrode aggregometry. Platelet adhesion was measured on denuded porcine aortas and in a flow chamber. Aptamer stability was assessed by incubation in nuclease rich human, monkey, and rat serum for up to 72 hours. Pharmacokinetic and pharmacodynamic profiles were tested in cynomolgus monkeys after IV and SC administration. The median IC(100) and IC(50) to prolong collagen/adenosine diphosphate-induced closure timewere 27 nmol/L and 12 nmol/L, respectively. ARC15105 (1.3 µmol/L) completely inhibited ristocetin-induced platelet aggregation in whole blood (P90% on denuded porcine aortas (P90% (P90% in blood samples taken 300 hours after a 20 mg/kg IV or SC dose in monkeys.
The potency, pharmacokinetic profile, and SC bioavailability of ARC15105 support its clinical investigation for chronic inhibition of von Willeband factor -mediated platelet activation.
PubMed ID
22282355 View in PubMed
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The Arctic Alzheimer mutation facilitates early intraneuronal Abeta aggregation and senile plaque formation in transgenic mice.

https://arctichealth.org/en/permalink/ahliterature6604
Source
Neurobiol Aging. 2006 Jan;27(1):67-77
Publication Type
Article
Date
Jan-2006
Author
Anna Lord
Hannu Kalimo
Chris Eckman
Xiao-Qun Zhang
Lars Lannfelt
Lars N G Nilsson
Author Affiliation
Department of Public Health and Caring Sciences, Geriatrics, Uppsala University, Dag Hammarskjölds Väg 20, SE-751 85 Uppsala, Sweden.
Source
Neurobiol Aging. 2006 Jan;27(1):67-77
Date
Jan-2006
Language
English
Publication Type
Article
Keywords
Aging - metabolism
Alzheimer Disease - genetics - metabolism
Amyloid beta-Protein - metabolism
Animals
Brain - metabolism
Disease Models, Animal
Genetic Predisposition to Disease - genetics
Mice
Mice, Inbred C57BL
Mice, Transgenic
Mutagenesis, Site-Directed
Mutation
Neurons - metabolism
Protein Binding
Research Support, Non-U.S. Gov't
Senile Plaques - metabolism
Abstract
The Arctic mutation (APP E693G) is unique, since it is located within the amyloid-beta (Abeta) sequence and leads to Alzheimer's disease (AD). Arctic Abeta peptides more easily form Abeta protofibrils in vitro, but little is known about the pathogenic mechanism of the Arctic mutation in vivo. Here, we analyzed APP transgenic mice with both the Swedish and Arctic mutations (tg-APPArcSwe) and transgenic mice with the Swedish mutation alone (tg-APPSwe). Intense intraneuronal Abeta-immunoreactive staining was present in young tg-APPArcSwe mice, but not in tg-APPSwe mice. Intracellular Abeta aggregates in tg-APPArcSwe were strongly stained by antibodies recognizing the N-terminus of Abeta, while those recognizing the C-terminus of Abeta stained weakly. The Abeta aggregates inside neurons increased with age and predated extracellular Abeta deposition in both tg-APPArcSwe and tg-APPSwe mice. Senile plaque deposition was markedly accelerated in tg-APPArcSwe mice, as compared to tg-APPSwe mice. We conclude that the Arctic mutation causes AD by facilitating amyloidosis through early accumulation of intracellular Abeta aggregates in association with a rapid onset of senile plaque deposition.
PubMed ID
16298242 View in PubMed
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Arctic mutant Aß40 aggregates on a7 nicotinic acetylcholine receptors and inhibits their functions.

https://arctichealth.org/en/permalink/ahliterature259619
Source
J Neurochem. 2014 Dec;131(5):667-74
Publication Type
Article
Date
Dec-2014
Author
Ye Ju
Toru Asahi
Naoya Sawamura
Source
J Neurochem. 2014 Dec;131(5):667-74
Date
Dec-2014
Language
English
Publication Type
Article
Keywords
Amyloid beta-Peptides - genetics
Animals
CHO Cells
Calcium - metabolism
Cricetulus
Humans
Microscopy, Electron, Transmission
Mutation - genetics
Peptide Fragments - genetics
Protein Aggregates - genetics
Protein Binding - genetics
Transfection
alpha7 Nicotinic Acetylcholine Receptor - metabolism - ultrastructure
Abstract
Amyloid ß protein (Aß) plays a central role in the pathogenesis of Alzheimer's disease (AD). Point mutations within the Aß sequence associated with familial AD (FAD) are clustered around the central hydrophobic core of Aß. Several types of mutations within the Aß sequence have been identified, and the 'Arctic' mutation (E22G) has a purely cognitive phenotype typical of AD. Previous studies have shown that the primary result of the 'Arctic' mutation is increased formation of Aß protofibrils. However, the molecular mechanism underlying this effect remains unknown. Aß42 binds to a neuronal nicotinic acetylcholine receptor subunit, neuronal acetylcholine receptor subunit alpha-7 (CHRNA7), with high affinity and, thus, may be involved in the pathogenesis of AD. Therefore, to clarify the molecular mechanism of Arctic mutation-mediated FAD, we focused on CHRNA7 as a target molecule of Arctic Aß. We performed an in vitro binding assay using purified CHRNA7 and synthetic Arctic Aß40, and demonstrated that Arctic Aß40 specifically bound to CHRNA7. The aggregation of Arctic Aß40 was enhanced with the addition of CHRNA7. Furthermore, the function of CHRNA7 was detected by measuring Ca(2+) flux and phospho-p44/42 MAPK (ERK1/2) activation. Our results indicated that Arctic Aß40 aggregation was enhanced by the addition of CHRNA7, which destabilized the function of CHRNA7 via inhibition of Ca(2+) responses and activation of ERK1/2. These findings indicate that Arctic Aß mutation may be involved in the mechanism underlying FAD. This mechanism may involve binding and aggregation, leading to the inhibition of CHRNA7 functions.
PubMed ID
25059095 View in PubMed
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The basis of prostaglandin synthesis in coral: molecular cloning and expression of a cyclooxygenase from the Arctic soft coral Gersemia fruticosa.

https://arctichealth.org/en/permalink/ahliterature3964
Source
J Biol Chem. 2001 Mar 9;276(10):7033-40
Publication Type
Article
Date
Mar-9-2001
Author
R. Koljak
I. Järving
R. Kurg
W E Boeglin
K. Varvas
K. Valmsen
M. Ustav
A R Brash
N. Samel
Author Affiliation
Department of Bioorganic Chemistry, Institute of Chemistry, Tallinn Technical University, Akadeemia tee 15, Tallinn 12618, Estonia.
Source
J Biol Chem. 2001 Mar 9;276(10):7033-40
Date
Mar-9-2001
Language
English
Publication Type
Article
Keywords
Alanine - chemistry
Amino Acid Sequence
Animals
Arginine - chemistry
Blotting, Northern
COS Cells
Chromatography, Thin Layer
Cloning, Molecular
Cnidaria - metabolism
Cyclooxygenase 1
Cyclooxygenase 2
DNA, Complementary - metabolism
Hela Cells
Histidine - chemistry
Humans
Isoenzymes - chemistry
Isoleucine - chemistry
Membrane Proteins
Microscopy, Fluorescence
Models, Genetic
Molecular Sequence Data
Phylogeny
Plasmids - metabolism
Polymerase Chain Reaction
Prostaglandin-Endoperoxide Synthases - biosynthesis - chemistry - genetics
Prostaglandins - biosynthesis
Protein Binding
RNA, Messenger - metabolism
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Serine - chemistry
Tyrosine - chemistry
Abstract
In vertebrates, the synthesis of prostaglandin hormones is catalyzed by cyclooxygenase (COX)-1, a constitutively expressed enzyme with physiological functions, and COX-2, induced in inflammation and cancer. Prostaglandins have been detected in high concentrations in certain corals, and previous evidence suggested their biosynthesis through a lipoxygenase-allene oxide pathway. Here we describe the discovery of an ancestor of cyclooxygenases that is responsible for prostaglandin biosynthesis in coral. Using a homology-based polymerase chain reaction cloning strategy, the cDNA encoding a polypeptide with approximately 50% amino acid identity to both mammalian COX-1 and COX-2 was cloned and sequenced from the Arctic soft coral Gersemia fruticosa. Nearly all the amino acids essential for substrate binding and catalysis as determined in the mammalian enzymes are represented in coral COX: the arachidonate-binding Arg(120) and Tyr(355) are present, as are the heme-coordinating His(207) and His(388); the catalytic Tyr(385); and the target of aspirin attack, Ser(530). A key amino acid that determines the sensitivity to selective COX-2 inhibitors (Ile(523) in COX-1 and Val(523) in COX-2) is present in coral COX as isoleucine. The conserved Glu(524), implicated in the binding of certain COX inhibitors, is represented as alanine. Expression of the G. fruticosa cDNA afforded a functional cyclooxygenase that converted exogenous arachidonic acid to prostaglandins. The biosynthesis was inhibited by indomethacin, whereas the selective COX-2 inhibitor nimesulide was ineffective. We conclude that the cyclooxygenase occurs widely in the animal kingdom and that vertebrate COX-1 and COX-2 are evolutionary derivatives of the invertebrate precursor.
PubMed ID
11085996 View in PubMed
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Binding of xenoestrogens to the sex steroid-binding protein in plasma from Arctic charr (Salvelinus alpinus L.).

https://arctichealth.org/en/permalink/ahliterature5527
Source
Comp Biochem Physiol C Toxicol Pharmacol. 2004 Oct;139(1-3):127-33
Publication Type
Article
Date
Oct-2004
Author
K-E Tollefsen
J. Ovrevik
J. Stenersen
Author Affiliation
Department of Biology, University of Oslo, P.O. Box. 1050 Blindern, N-0316 Oslo, Norway. knut.erik.tollefsen@niva.no
Source
Comp Biochem Physiol C Toxicol Pharmacol. 2004 Oct;139(1-3):127-33
Date
Oct-2004
Language
English
Publication Type
Article
Keywords
Animals
Binding Sites
Binding, Competitive
Biological Assay
Comparative Study
Dose-Response Relationship, Drug
Estradiol - metabolism
Estradiol Congeners - metabolism
Estrogens - blood - metabolism
Female
Ligands
Male
Protein Binding
Sex Hormone-Binding Globulin - metabolism
Tritium
Trout - blood - metabolism
Xenobiotics - blood - metabolism - pharmacology
Abstract
A specific sex steroid-binding protein (SBP) is believed to be involved in regulation of circulating sex steroids, steroid delivery to target cells and intracellular signalling in sex steroid-sensitive tissues. In the present work, interactions between xenoestrogens and the plasma SBP in Arctic charr (Salvelinus alpinus L.) were determined using ligand-protein binding studies. The test compounds were all able to displace tritiated 17 beta-estradiol (E2) from the Arctic charr SBP (acSBP) in a competitive and dose-dependent manner. The acSBP affinities for the xenoestrogens ranged over several orders of magnitude (17 beta-estradiol>>ethynylestradiol (EE2)>zearalenone (ZEA)>diethylstilbestrol (DES)>genistein (GEN)>bisphenol A (BPA), 4-t-octylphenol (OP)>>o,p'-DDT, and dieldrin (DIN)), but were consistently lower than that of 17 beta-estradiol (about 4 x 10(2) -10(6)-fold less potent). The relative binding affinity (RBA) for selected chemicals were independent of both gender, age and maturation status, as well as variations of acSBP binding affinity. The affinity of endogenous steroids and estrogen mimics for the acSBP shows a high correlation to the affinity for the rainbow trout SBP, thus suggesting a phylogenetically conserved ligand-binding site between closely related species. Furthermore, it is argued that interaction with the acSBP- and SBP-mediated processes may introduce novel pathways for endocrine disruption, which may work in concert with the classical receptor-mediated effects.
PubMed ID
15556074 View in PubMed
Less detail

Bioinformatics-driven identification and examination of candidate genes for non-alcoholic fatty liver disease.

https://arctichealth.org/en/permalink/ahliterature136831
Source
PLoS One. 2011;6(1):e16542
Publication Type
Article
Date
2011
Author
Karina Banasik
Johanne M Justesen
Malene Hornbak
Nikolaj T Krarup
Anette P Gjesing
Camilla H Sandholt
Thomas S Jensen
Niels Grarup
Asa Andersson
Torben Jørgensen
Daniel R Witte
Annelli Sandbæk
Torsten Lauritzen
Bernard Thorens
Søren Brunak
Thorkild I A Sørensen
Oluf Pedersen
Torben Hansen
Author Affiliation
Hagedorn Research Institute, Gentofte, Denmark. kabs@hagedorn.dk
Source
PLoS One. 2011;6(1):e16542
Date
2011
Language
English
Publication Type
Article
Keywords
Case-Control Studies
Computational Biology - methods
Data Mining
Denmark
Diabetes Mellitus, Type 2 - genetics
Fatty Liver - genetics
Humans
Metabolic Syndrome X - genetics
Middle Aged
Obesity - genetics
Phenotype
Polymorphism, Single Nucleotide
Protein Binding
Quantitative Trait Loci
Abstract
Candidate genes for non-alcoholic fatty liver disease (NAFLD) identified by a bioinformatics approach were examined for variant associations to quantitative traits of NAFLD-related phenotypes.
By integrating public database text mining, trans-organism protein-protein interaction transferal, and information on liver protein expression a protein-protein interaction network was constructed and from this a smaller isolated interactome was identified. Five genes from this interactome were selected for genetic analysis. Twenty-one tag single-nucleotide polymorphisms (SNPs) which captured all common variation in these genes were genotyped in 10,196 Danes, and analyzed for association with NAFLD-related quantitative traits, type 2 diabetes (T2D), central obesity, and WHO-defined metabolic syndrome (MetS).
273 genes were included in the protein-protein interaction analysis and EHHADH, ECHS1, HADHA, HADHB, and ACADL were selected for further examination. A total of 10 nominal statistical significant associations (P
Notes
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PubMed ID
21339799 View in PubMed
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Body iron stores, dietary iron intake and coronary heart disease mortality.

https://arctichealth.org/en/permalink/ahliterature214445
Source
J Intern Med. 1995 Sep;238(3):223-30
Publication Type
Article
Date
Sep-1995
Author
A. Reunanen
H. Takkunen
P. Knekt
R. Seppänen
A. Aromaa
Author Affiliation
Research and Development Centre, Social Insurance Institution, Helsinki, Finland.
Source
J Intern Med. 1995 Sep;238(3):223-30
Date
Sep-1995
Language
English
Publication Type
Article
Keywords
Coronary Disease - blood - chemically induced - mortality
Diet
Female
Finland - epidemiology
Follow-Up Studies
Hematologic Tests
Humans
Iron - administration & dosage - adverse effects - blood
Male
Middle Aged
Population Surveillance
Prospective Studies
Protein Binding
Risk factors
Abstract
To assess whether increased body iron stores and dietary iron intake are associated with an increased risk of coronary heart disease mortality.
A prospective population study with a mean mortality follow-up time of 14 years.
Participants attending a health screening examination carried out in several localities in Finland.
All 6086 men and 6102 women aged from 45 to 64 years at the baseline examination without known heart disease, who had had serum iron and total iron binding capacity (TIBC) assessed. In a random fifth of these people, dietary iron intake was assessed by a dietary history.
The study was observational without any interventions.
Mortality from coronary heart disease.
Altogether, 739 of the men and 245 of the women died from coronary heart disease. No relationship between TIBC and coronary mortality was observed in the men; in the women, an inverse although not significant association was found. Transferrin saturation was inversely but not significantly associated with coronary mortality in men; in women, the relationship was U-formed with a higher mortality at both the lower and higher ends of the distribution. Adjustment for other risk factors did not alter the results. No association was found with dietary iron intake and coronary mortality.
The results do not corroborate earlier findings that excess body iron stores and increased iron intake are associated with an elevated risk of coronary heart disease.
PubMed ID
7673851 View in PubMed
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101 records – page 1 of 11.