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2-DE protein expression in endometrial carcinoma.

https://arctichealth.org/en/permalink/ahliterature80911
Source
Acta Oncol. 2006;45(6):685-94
Publication Type
Article
Date
2006
Author
Caroline, L
Johanna, L
Susanne, B
Uwe, R
Kjell, S
Karolina, B
Bo, F
Britta, N
Gert, A
Author Affiliation
Department of Gynaecologic Oncology, Radiumhemmet, Institute of Oncology and Pathology, Karolinska University Hospital and Institute, Stockholm, Sweden. caroline.lundgren@karolinska.se
Source
Acta Oncol. 2006;45(6):685-94
Date
2006
Language
English
Publication Type
Article
Keywords
Carcinoma - metabolism
Cluster analysis
Electrophoresis, Gel, Two-Dimensional
Endometrial Neoplasms - metabolism - pathology
Female
Gene Expression
Histocytochemistry
Humans
Neoplasm Proteins - metabolism
Ploidies
Statistics, nonparametric
Sweden
Abstract
The objective of this study was to explore the protein expression pattern in normal endometrial mucosa (n = 5) and endometrial carcinoma (n = 15) of low (diploid) and high (aneuploid) malignancy potential by two-dimensional gel electrophoresis (2-DE). The specimens were evaluated for histopathologic subtype, stage and grade in relation to DNA ploidy. A match-set consisting of five samples from normal endometrium, eight diploid and seven aneuploid tumours was created. All the diploid and three of the aneuploid tumours were of endometrioid subtype, while the remaining four were of uterine seropapillary type. There were 192 protein spots differentiating diploid tumours from normal endometrium and 238 protein spots were separating aneuploid tumours from normal endometrium (p
PubMed ID
16938811 View in PubMed
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Acception of cholesterol from cells in men of the Russian population correlates with concentration of pre-beta1 high-density lipoproteins.

https://arctichealth.org/en/permalink/ahliterature182095
Source
Bull Exp Biol Med. 2003 Oct;136(4):366-8
Publication Type
Article
Date
Oct-2003
Author
A P Serdyuk
K. Lasselin
G. Castro
O A Litinskaya
G. Frushar
V A Metel'skaya
Author Affiliation
Department of Metabolic Disorders, State Research Center for Preventive Medicine, Russian Ministry of Health, Moscow. vicamet@orc.ru
Source
Bull Exp Biol Med. 2003 Oct;136(4):366-8
Date
Oct-2003
Language
English
Publication Type
Article
Keywords
Animals
Apolipoprotein A-I - blood
Carcinoma, Hepatocellular - chemistry
Cell Line, Tumor
Chemical Fractionation
Cholesterol - blood - chemistry - metabolism
Cholesterol, HDL - blood - chemistry - isolation & purification
Electrophoresis, Gel, Two-Dimensional
Humans
Male
Middle Aged
Patient Selection
Phosphatidylcholine-Sterol O-Acyltransferase - blood
Rats
Russia - epidemiology
Triglycerides - blood
Abstract
We analyzed subfraction composition of HDL and cholesterol-acceptor properties of the plasma in Russian men with high and low HDL cholesterol. HDL were subfractionated by two-dimensional electrophoresis in agarose-polyacrylamide gel. The content of pre-beta1 HDL increased in individuals with high concentration of HDL cholesterol and strictly correlated with acception of cellular cholesterol in both groups.
PubMed ID
14714084 View in PubMed
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Airway irritation among indoor swimming pool personnel: trichloramine exposure, exhaled NO and protein profiling of nasal lavage fluids.

https://arctichealth.org/en/permalink/ahliterature123142
Source
Int Arch Occup Environ Health. 2013 Jul;86(5):571-80
Publication Type
Article
Date
Jul-2013
Author
Louise Fornander
Bijar Ghafouri
Mats Lindahl
Pål Graff
Author Affiliation
Occupational and Environmental Medicine, Department of Clinical and Experimental Medicine, Faculty of Health Sciences, Linköping University, Linköping, Sweden.
Source
Int Arch Occup Environ Health. 2013 Jul;86(5):571-80
Date
Jul-2013
Language
English
Publication Type
Article
Keywords
Adult
Air Pollutants, Occupational - adverse effects - analysis
Biological Markers - metabolism
Chlorides - adverse effects - analysis
Cross-Sectional Studies
Electrophoresis, Gel, Two-Dimensional
Female
Humans
Immunoblotting
Male
Middle Aged
Nasal Lavage Fluid - chemistry
Nitric Oxide - metabolism
Nitrogen Compounds - adverse effects - analysis
Occupational Diseases - diagnosis - epidemiology - etiology - metabolism
Occupational Exposure - adverse effects - analysis
Prevalence
Proteome - metabolism
Respiratory Tract Diseases - diagnosis - epidemiology - etiology - metabolism
Risk factors
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Sweden - epidemiology
Swimming Pools
Abstract
Occurrence of airway irritation among indoor swimming pool personnel was investigated. The aims of this study were to assess trichloramine exposure levels and exhaled nitric oxide in relation to the prevalence of airway symptoms in swimming pool facilities and to determine protein effects in the upper respiratory tract.
The presence of airway symptoms related to work was examined in 146 individuals working at 46 indoor swimming pool facilities. Levels of trichloramine, as well as exhaled nitric oxide, were measured in five facilities with high prevalence of airway irritation and four facilities with no airway irritation among the personnel. Nasal lavage fluid was collected, and protein profiles were determined by a proteomic approach.
17 % of the swimming pool personnel reported airway symptoms related to work. The levels of trichloramine in the swimming pool facilities ranged from 0.04 to 0.36 mg/m(3). There was no covariance between trichloramine levels, exhaled nitric oxide and prevalence of airway symptoms. Protein profiling of the nasal lavage fluid showed that the levels alpha-1-antitrypsin and lactoferrin were significantly higher, and S100-A8 was significantly lower in swimming pool personnel.
This study confirms the occurrence of airway irritation among indoor swimming pool personnel. Our results indicate altered levels of innate immunity proteins in the upper airways that may pose as potential biomarkers. However, swimming pool facilities with high prevalence of airway irritation could not be explained by higher trichloramine exposure levels. Further studies are needed to clarify the environmental factors in indoor swimming pools that cause airway problems and affect the immune system.
PubMed ID
22729567 View in PubMed
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Antiserum to pregnancy-associated plasma protein A (PAPP-A) recognizes human haptoglobin.

https://arctichealth.org/en/permalink/ahliterature65300
Source
Br J Obstet Gynaecol. 1989 Jul;96(7):867-9
Publication Type
Article
Date
Jul-1989
Author
M R Bueler
N A Bersinger
Author Affiliation
Department of Clinical Chemistry, University Hospital, Zurich, Switzerland.
Source
Br J Obstet Gynaecol. 1989 Jul;96(7):867-9
Date
Jul-1989
Language
English
Publication Type
Article
Keywords
Antibodies, Monoclonal - diagnostic use
Blotting, Western
Electrophoresis, Gel, Two-Dimensional
Female
Haptoglobins - immunology
Humans
Immune Sera
Pregnancy
Pregnancy Proteins - immunology
Pregnancy-Associated Plasma Protein-A - analysis - immunology
Reagent kits, diagnostic
Research Support, Non-U.S. Gov't
Abstract
The presence of pregnancy-associated plasma protein A (PAPP-A) in non-pregnancy serum has been questioned with reference to insufficient specificity of the antibodies raised against this glycoprotein in some departments and used in immunoassay. For convenience, but also because of this unclear situation, many laboratories now use the only commercially available anti-PAPP-A preparations in their assays. By analysing pregnancy and non-pregnancy serum with two-dimensional electrophoresis (2-DE) and Western blotting, we could demonstrate that this antiserum marketed by Dakopatts (Denmark) was capable of binding haptoglobin whereas our own (Dr P. Bischof) antibody preparation did not recognize haptoglobin.
PubMed ID
2475160 View in PubMed
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Association between sequence variations in genes encoding human zona pellucida glycoproteins and fertilization failure in IVF.

https://arctichealth.org/en/permalink/ahliterature63226
Source
Hum Reprod. 2005 Jun;20(6):1578-85
Publication Type
Article
Date
Jun-2005
Author
M. Männikkö
R-M Törmälä
T. Tuuri
A. Haltia
H. Martikainen
L. Ala-Kokko
J S Tapanainen
J T Lakkakorpi
Author Affiliation
Collagen Research Unit, Biocenter and Department of Medical Biochemistry and Molecular Biology, University of Oulu, FIN-90014 Oulu, Finland.
Source
Hum Reprod. 2005 Jun;20(6):1578-85
Date
Jun-2005
Language
English
Publication Type
Article
Keywords
Adult
Case-Control Studies
Egg Proteins - genetics
Electrophoresis, Gel, Two-Dimensional - methods
Exons
Female
Fertilization in Vitro - methods
Humans
Infertility, Female - genetics
Introns
Membrane Glycoproteins - genetics
Pregnancy
Receptors, Cell Surface - genetics
Research Support, Non-U.S. Gov't
Sequence Analysis
Sperm Injections, Intracytoplasmic
Treatment Failure
Variation (Genetics)
Abstract
BACKGROUND: The zona pellucida (ZP) has multiple roles in reproductive processes, including oocyte maturation, fertilization and implantation. We used, for the first time, a genetic approach to study whether human ZP genes possess structural alterations in women with unsuccessful IVF trials. In theory, this may result in gradual reduction of sperm-zona interaction and eventually in total fertilization failure (TFF). METHODS: Eighteen infertile women (TFFs) whose IVF did not result in any fertilized oocytes, whereas fertilization by ICSI was successful, were screened for mutations in ZP genes by means of conformation-sensitive gel electrophoresis. Twenty-three fertilizers in IVF (FIVFs) and 68 women with proven fertility (WPFs) constituted the two control groups. RESULTS: Altogether, 20 sequence variations were found in the ZP genes. Two variations in ZP3, one in the regulatory region (c. 1-87 T --> G) and one in exon 6 [c. 894 G --> A (p. K298)] existed more frequently in TFFs than in FIVF and WPF groups (P-values 0.027 and 0.008, respectively). CONCLUSIONS: Our study on ZP genes of infertile women revealed a high degree of sequence variations. This may reflect gradual reduction of fertility among TFFs, but the putative roles and influences of single variations can only be hypothesized.
PubMed ID
15860499 View in PubMed
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Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry.

https://arctichealth.org/en/permalink/ahliterature64465
Source
Eur J Biochem. 1996 Jul 1;239(1):144-9
Publication Type
Article
Date
Jul-1-1996
Author
S N Vladimirov
A V Ivanov
G G Karpova
A K Musolyamov
T A Egorov
B. Thiede
B. Wittmann-Liebold
A. Otto
Author Affiliation
Novosibirsk Institute of Bioorganic Chemistry, Siberian Division, Russian Academy of Sciences, Russian Federation.
Source
Eur J Biochem. 1996 Jul 1;239(1):144-9
Date
Jul-1-1996
Language
English
Publication Type
Article
Keywords
Amino Acid Sequence
Chromatography, High Pressure Liquid
Electrophoresis, Gel, Two-Dimensional
Female
Humans
Molecular Sequence Data
Molecular Weight
Placenta - chemistry
Pregnancy
Research Support, Non-U.S. Gov't
Ribosomal Proteins - chemistry
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Abstract
Reverse-phase HPLC was used to fractionate 40S ribosomal proteins from human placenta. Application of a C4 reverse-phase column allowed us to obtain 27 well-resolved peaks. The protein composition of each chromatographic fraction was established by two-dimensional polyacrylamide gel electrophoresis and N-terminal sequencing. N-terminally blocked proteins were cleaved with endoproteinase Lys-C, and suitable peptides were sequenced. All sequences were compared with those of ribosomal proteins available from data bases. This allowed us to identify all proteins from the 40S human ribosomal subunit in the HPLC elution profile. By matrix-assisted laser-desorption ionization mass spectrometry the masses of the 40S proteins were determined and checked for the presence of post-translational modifications. For several proteins differences to the deduced sequences and the calculated masses were found to be due to post-translational modifications.
PubMed ID
8706699 View in PubMed
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Colorectal cancer risks in relatives of young-onset cases: is risk the same across all first-degree relatives?

https://arctichealth.org/en/permalink/ahliterature161866
Source
Clin Gastroenterol Hepatol. 2007 Oct;5(10):1195-8
Publication Type
Article
Date
Oct-2007
Author
Lisa A Boardman
Bruce W Morlan
Kari G Rabe
Gloria M Petersen
Noralane M Lindor
Sandra K Nigon
Julia Goldberg
Steven Gallinger
Author Affiliation
Division of Gastroenterology, Department of Internal Medicine, Mayo Clinic College of Medicine, Rochester, Minnesota, USA.
Source
Clin Gastroenterol Hepatol. 2007 Oct;5(10):1195-8
Date
Oct-2007
Language
English
Publication Type
Article
Keywords
Adult
Age of Onset
Colorectal Neoplasms - diagnosis - epidemiology - genetics
DNA Mismatch Repair
DNA, Neoplasm - analysis
Electrophoresis, Gel, Two-Dimensional
Family
Female
Genetic Predisposition to Disease
Humans
Inheritance Patterns - genetics
Male
Middle Aged
Minnesota - epidemiology
Mutation
Ontario - epidemiology
Polymerase Chain Reaction
Prognosis
Retrospective Studies
Risk factors
SEER Program
Siblings
Abstract
During the last 15 years, several single-gene mendelian disorders have been discovered that might account for some of the familial aggregation detected in large population studies of colorectal cancer (CRC). Mutations in DNA mismatch repair (MMR) genes cause hereditary nonpolyposis colorectal cancer-Lynch syndrome, the most common of the recognized CRC-predisposition syndromes, in which one major feature is a young age for cancer onset. However, for young-onset microsatellite stable (MSS) CRC, the familial risk for CRC is unknown.
Patients with CRC who were
Notes
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Cites: Cancer Res. 1997 Nov 1;57(21):4787-949354440
Cites: Cancer Res. 1998 Apr 15;58(8):1713-89563488
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PubMed ID
17702662 View in PubMed
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Comparison of ethanol-soluble proteins from different rye (Secale cereale) varieties by two-dimensional electrophoresis.

https://arctichealth.org/en/permalink/ahliterature9844
Source
Electrophoresis. 2002 Dec;23(24):4157-66
Publication Type
Article
Date
Dec-2002
Author
Louise Radzikowski
Ljiljana Nesic
Hanne Boskov Hansen
Susanne Jacobsen
Ib Søndergaard
Author Affiliation
BioCentrum--DTU, Biochemistry and Nutrition, Søltofts Plads, The Technical University of Denmark, Lyngby, Denmark.
Source
Electrophoresis. 2002 Dec;23(24):4157-66
Date
Dec-2002
Language
English
Publication Type
Article
Keywords
Comparative Study
Electrophoresis, Gel, Two-Dimensional - methods
Ethanol
Indicators and Reagents
Multivariate Analysis
Plant Proteins - isolation & purification
Research Support, Non-U.S. Gov't
Secale cereale - chemistry - classification
Software
Solubility
Abstract
The major storage proteins from six rye varieties, grown under the same conditions in 1997 and 1998 in Rønhave, Denmark, were analyzed by two-dimensional (2-D) polyacrylamide gel electrophoresis. The proteins were extracted from ground rye kernels with 70% ethanol and separated by 2-D electrophoresis. The gels were scanned, compared using ImageMaster software and the data sets were analyzed by principal component analysis (PCA) using THE UNSCRAMBLER software. Afterwards MATLAB was used to make a cluster analysis of the varieties based on PCA. The analysis of the gels showed, that the protein patterns (number of different proteins and their isoelectric points and molecular weights) from the six rye varieties were different. Based on the presence of unique cultivar-specific spots it was possible to differentiate between all six varieties if the two harvest years were investigated separately. When the results were combined from the two years five varieties could be differentiated. The results from the PCA confirmed the finding of the unique spots and cluster analysis was made in order to illustrate the results. The combination of the results from 2-D electrophoresis and other grain characteristics showed that one protein spot was located close to the parameters bread volume and bread height.
PubMed ID
12481272 View in PubMed
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Comparison of myosin isoenzymes present in skeletal and cardiac muscles of the Arctic charr Salvelinus alpinus (L.). Sequential expression of different myosin heavy chains during development of the fast white skeletal muscle.

https://arctichealth.org/en/permalink/ahliterature6901
Source
Eur J Biochem. 1991 Feb 14;195(3):743-53
Publication Type
Article
Date
Feb-14-1991
Author
I. Martinez
J S Christiansen
R. Ofstad
R L Olsen
Author Affiliation
Institute of Fisheries Technology Research, Tromsø, Norway.
Source
Eur J Biochem. 1991 Feb 14;195(3):743-53
Date
Feb-14-1991
Language
English
Publication Type
Article
Keywords
Aging
Animals
Arctic Regions
Comparative Study
Electrophoresis, Gel, Two-Dimensional
Electrophoresis, Polyacrylamide Gel
Fishes - growth & development
Heart - growth & development
Muscle Development
Muscles - enzymology
Myocardium - enzymology
Myosins - isolation & purification
Peptide Mapping
Rabbits
Research Support, Non-U.S. Gov't
Abstract
The expression of myosin isoforms and their subunit composition in the white skeletal body musculature of Arctic charr (Salvelinus alpinus) of different ages (from 77-day embryos until about 5 years old) was studied at the protein level by means of electrophoretic techniques. Myosin from the white muscle displayed three types of light chain during all the developmental stages examined: two myosin light chains type 1 (LC1F) differing in both apparent molecular mass and pI, one myosin light chain type 2 (LC2F) and one myosin light chain type 3 (LC3F). The fastest-migrating form of LC1F seemed to be predominant during the embryonic and eleutheroembryonic periods. The slowest-migrating form of LC1F was predominant in the 5-year-old fish. Between 1 year and 4 years, both types of LC1F were present in similar amounts. Cardiac as well as red muscle myosin from 3-year-old fish had two types of light chain. The myosin light chains from atria and ventriculi were indistinguishable by two-dimensional electrophoresis, but were different from the myosin light chains from red muscle. Neither the light chains from cardiac nor red muscle were coexpressed with the myosin light chains of white muscle at any of the developmental stages examined. Two myosin heavy chain bands were resolved by SDS/glycerol/polyacrylamide gel electrophoresis of the extract from embryos. One of the bands was present in minor amounts. The other, and most abundant, band comigrated with the only band found in the extracts of white muscle myosin from older fish. One-dimensional Staphylococcus aureus V8 protease peptide mapping of these bands revealed some differences during development of the white muscle tentatively interpreted as follows. The myosin heavy chain band present in minor amounts in the embryos may represent an early embryonic form that is replaced by a late embryonic or foetal form in the eleutheroembryos. The foetal myosin heavy chain appears to be present until the resorption of the yolk sack and beginning of the free-swimming stage. A new form of myosin heavy chain, termed neonatal and probably expressed around hatching, is present until about 1 year of age.(ABSTRACT TRUNCATED AT 400 WORDS)
PubMed ID
1825632 View in PubMed
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Contribution of methylmercury, polychlorinated biphenyls and organochlorine pesticides to the toxicity of a contaminant mixture based on Canadian Arctic population blood profiles.

https://arctichealth.org/en/permalink/ahliterature90943
Source
Toxicol Lett. 2009 Feb 10;184(3):176-85
Publication Type
Article
Date
Feb-10-2009
Author
Pelletier Guillaume
Masson Sheila
Wade Mike J
Nakai Jamie
Alwis Ramona
Mohottalage Susantha
Kumarathasan Premkumari
Black Paleah
Bowers Wayne J
Chu Ih
Vincent Renaud
Author Affiliation
Hazard Identification Division, Environmental Health, Science and Research Bureau, Chemicals Management Directorate, Health Canada, Canada. guillaume_pelletier@hc-sc.gc.ca
Source
Toxicol Lett. 2009 Feb 10;184(3):176-85
Date
Feb-10-2009
Language
English
Publication Type
Article
Keywords
Age Factors
Animals
Arctic Regions
Body Weight - drug effects
Brain - drug effects - metabolism
Canada
Cerebellum - drug effects - metabolism
Complex Mixtures - toxicity
Disease Models, Animal
Electrophoresis, Gel, Two-Dimensional
Female
Gestational Age
Hippocampus - drug effects - metabolism
Hydrocarbons, Chlorinated - blood - toxicity
Hypothyroidism - blood - chemically induced
Male
Methylmercury Compounds - blood - toxicity
Mitochondrial Proteins - metabolism
Nerve Tissue Proteins - metabolism
Pesticides - blood - toxicity
Polychlorinated Biphenyls - blood - toxicity
Propylthiouracil
Rats
Rats, Sprague-Dawley
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Taurine - metabolism
Thyroid Gland - drug effects - metabolism
Thyroid Hormones - blood
Water Pollutants, Chemical - blood - toxicity
Abstract
Human populations are simultaneously exposed to a variety of anthropogenic contaminants. However, despite extensive literature on animal exposure to single compounds, data on the toxicity of complex mixtures are scarce. The Northern Contaminant Mixture (NCM) was formulated to contain the 27 most abundant contaminants in the same relative proportions found in the blood of Canadian Arctic populations. Sprague-Dawley rat dams were dosed from the first day of gestation until weaning with methylmercury (MeHg), polychlorinated biphenyls (PCBs) or organochlorines pesticides (OCs) administered either separately or together in the NCM. An additional control group for hypothyroxinemia was included by dosing dams with the goitrogen 6-propyl-2-thiouracil (PTU). Offspring growth, survival, serum thyroxine and Thyroid Stimulating Hormone (TSH) levels, thyroid gland morphology, brain taurine content and cerebellum and hippocampus protein expression patterns resulting from such exposures were monitored. Pups' increased mortality rate and impaired growth observed in the NCM treatment group were attributed to MeHg, while decreased circulating thyroxine levels and perturbations of thyroid gland morphology were mostly attributable to PCBs. Interestingly, despite comparable reduction in serum thyroxine levels, PCBs and PTU exposures produced markedly different effects on pup's growth, serum TSH level and brain taurine content. Analysis of cerebellum and hippocampus protein expression patterns corroborated previous cerebellum gene expression data, as contaminant co-exposure in the NCM significantly masked the effects of individual components on protein two-dimensional electrophoresis patterns. Identification by MALDI-TOF/TOF MS of differentially expressed proteins involved notably in neuronal and mitochondrial functions provided clues on the cellular and molecular processes affected by these contaminant mixtures.
PubMed ID
19059321 View in PubMed
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29 records – page 1 of 3.