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677 records – page 1 of 68.

6-PGD polymorphism: a fast 'Elcho' variant found in Finland.

https://arctichealth.org/en/permalink/ahliterature246786
Source
Hum Genet. 1979 Oct 1;51(2):225-6
Publication Type
Article
Date
Oct-1-1979

A 50?bp deletion in the SOD1 promoter lowers enzyme expression but is not associated with ALS in Sweden.

https://arctichealth.org/en/permalink/ahliterature286592
Source
Amyotroph Lateral Scler Frontotemporal Degener. 2016 Jul-Aug;17(5-6):452-7
Publication Type
Article
Author
Caroline Ingre
Anna Wuolikainen
Stefan L Marklund
Anna Birve
Rayomand Press
Peter M Andersen
Source
Amyotroph Lateral Scler Frontotemporal Degener. 2016 Jul-Aug;17(5-6):452-7
Language
English
Publication Type
Article
Keywords
Adult
Aged
Amyotrophic Lateral Sclerosis - enzymology - epidemiology - genetics
Analysis of Variance
Cohort Studies
Erythrocytes - enzymology
Female
Genotype
Humans
Male
Middle Aged
Polymorphism, Genetic - genetics
Sequence Deletion - genetics
Superoxide Dismutase-1 - genetics - metabolism
Sweden - epidemiology
Abstract
Mutations in the superoxide dismutase (SOD1) gene have been linked to amyotrophic lateral sclerosis (ALS). A 50 base pair (bp) deletion of SOD1 has been suggested to reduce transcription and to be associated with later disease onset in ALS. This study was aimed to reveal if the 50?bp deletion influenced SOD1 enzymatic activity, occurrence and phenotype of the disease in a Swedish ALS/control cohort. Blood samples from 512 Swedish ALS patients and 354 Swedish controls without coding SOD1 mutations were analysed for the 50?bp deletion allele. The enzymatic activity of SOD1 in erythrocytes was analysed and genotype-phenotype correlations were assessed. Results demonstrated that the genotype frequencies of the 50?bp deletion were all found to be in Hardy-Weinberg equilibrium. No significant differences were found for age of onset, disease duration or site of onset. SOD1 enzymatic activity showed a statistically significant decreasing trend in the control group, in which the allele was associated with a 5% reduction in SOD1 activity. The results suggest that the 50?bp deletion has a moderate reducing effect on SOD1 synthesis. No modulating effects, however, were found on ALS onset, phenotype and survival in the Swedish population.
PubMed ID
27002425 View in PubMed
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[A blood transfusion in Sweden--the societal cost].

https://arctichealth.org/en/permalink/ahliterature166918
Source
Lakartidningen. 2006 Sep 20-26;103(38):2752-6
Publication Type
Article

Abnormal hematologic profiles in elite cross-country skiers: blood doping or?

https://arctichealth.org/en/permalink/ahliterature71327
Source
Clin J Sport Med. 2003 May;13(3):132-7
Publication Type
Article
Date
May-2003
Author
James Stray-Gundersen
Tapio Videman
Ilkka Penttilä
Inggard Lereim
Author Affiliation
jimsg@singlepoint.net
Source
Clin J Sport Med. 2003 May;13(3):132-7
Date
May-2003
Language
English
Publication Type
Article
Keywords
Doping in Sports - statistics & numerical data
Erythrocyte Indices - drug effects
Erythropoiesis - drug effects - physiology
Female
Hemoglobins - analysis
Humans
Male
Prevalence
Research Support, Non-U.S. Gov't
Reticulocyte Count
Skiing - physiology - statistics & numerical data
Abstract
OBJECTIVE: There is widespread public concern about fairness in sports. Blood doping undermines fairness and places athletes' health at risk. The purpose of this study was to examine the prevalence of abnormal hematologic profiles in elite cross-country skiers, which may indicate a high probability of blood doping. SETTING AND PARTICIPANTS: Samples were obtained as part of routine International Ski Federation blood testing procedures from participants at the World Ski Championships. Sixty-eight percent of all skiers and 92% of those finishing in the top 10 places were tested. MAIN OUTCOME MEASURES: Using flow cytometry, we analyzed erythrocyte and reticulocyte indices. Reference values were from the 1989 Nordic Ski World Championships data set and the International Olympic Committee Erythropoietin 2000 project. RESULTS: Of the skiers tested and finishing within the top 50 places in the competitions, 17% had "highly abnormal" hematologic profiles, 19% had "abnormal" values, and 64% were normal. Fifty percent of medal winners and 33% of those finishing from 4th to 10th place had highly abnormal hematologic profiles. In contrast, only 3% of skiers finishing from 41st to 50th place had highly abnormal values. CONCLUSIONS: These data suggest that blood doping is both prevalent and effective in cross-country ski racing, and current testing programs for blood doping are ineffective. It is unlikely that blood doping is less common in other endurance sports. Ramifications of doping affect not only elite athletes who may feel compelled to risk their health but also the general population, particularly young people.
PubMed ID
12792206 View in PubMed
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Acetaldehyde adducts of proteins: diagnostic and pathogenic implications in diseases caused by excessive alcohol consumption.

https://arctichealth.org/en/permalink/ahliterature11788
Source
Scand J Clin Lab Invest Suppl. 1993;213:45-54
Publication Type
Article
Date
1993
Author
O. Niemelä
Author Affiliation
Department of Clinical Chemistry, University of Oulu, Finland.
Source
Scand J Clin Lab Invest Suppl. 1993;213:45-54
Date
1993
Language
English
Publication Type
Article
Keywords
Acetaldehyde - blood - metabolism
Alcoholism - diagnosis - metabolism
Blood Proteins - metabolism
Erythrocytes - metabolism
Ethanol - metabolism
Fibrinogen - metabolism
Humans
Liver - metabolism
Proteins - metabolism
Research Support, Non-U.S. Gov't
Abstract
Alcohol abuse and alcoholism continue to be a major threat to human health. Given their increasing incidence and the detrimental impact on society, it is actually surprising that no objective, specific indicators for the early detection of alcohol-related health problems are available. A diagnostic test for a disease involving excessive alcohol consumption should be extremely specific in order to achieve positive predictive power, and: ideally it should also be very sensitive in order to identify problem drinkers in broad screening programs. The present research indicates that such a test for alcohol abuse may be provided by measurements of covalent chemical addition products (adducts) of acetaldehyde with biologically stable macromolecules. It was recently demonstrated that proteins modified with acetaldehyde are formed in vivo and can induce an antibody response as a result of alcohol consumption. Monoclonal and polyclonal antibodies raised by immunizations against acetaldehyde-modified proteins recognize acetaldehyde adducts irrespective of the nature of the carrier protein. Use of such antibodies in sensitive two-site immunoenzymatic or immunofluorometric assays has indicated that high acetaldehyde adduct concentrations exist in the erythrocytes of alcohol abusers, in healthy volunteers after a bout of drinking, and also in alcohol consuming mothers who subsequently give birth to children with foetal alcohol effects. We have developed the first immunohistochemical techniques for the detection of acetaldehyde adducts in human tissues. The centrilobular region of the liver of alcohol abusers with an early stage of histological tissue damage was found to contain acetaldehyde-modified epitopes, whereas the adducts were more widespread in advanced liver disease. The diagnostic superiority of acetaldehyde adducts as markers of ethanol consumption is due to the fact that they represent true metabolites of ethanol and allow estimations of past alcohol consumption after the ethanol has been eliminated from the body. Investigations into the formation of acetaldehyde adducts in alcohol consumers do not only have diagnostic applications but also help to explain the pathogenesis of alcohol-induced organ damage. Many types of hypersensitivity and immune responses are brought about by acetaldehyde-modified proteins. In addition, such metabolites of ethanol also aggravate liver disease through disturbed protein function and stimulation of fibrogenesis.
PubMed ID
8322018 View in PubMed
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ACID PHOSPHATASE ACTIVITY OF SERUM, THROMBOCYTES AND ERYTHROCYTES IN A JUVENILE FORM OF GAUCHER'S DISEASE.

https://arctichealth.org/en/permalink/ahliterature45243
Source
Acta Paediatr. 1964 Nov;53:558-69
Publication Type
Article
Date
Nov-1964

[Acid stability of erythrocytes in children with bronchial asthma]

https://arctichealth.org/en/permalink/ahliterature16301
Source
Pediatr Akus Ginekol. 1975;(5):13-5
Publication Type
Article
Date
1975

Activation of potassium channels in erythrocytes of marine teleost Scorpaena porcus.

https://arctichealth.org/en/permalink/ahliterature10059
Source
Membr Cell Biol. 2001;14(6):773-82
Publication Type
Article
Date
2001
Author
Y A Silkin
E N Silkina
A O Sherstobitov
G P Gusev
Author Affiliation
Karadag Natural Reserve, Ukrainian Academy of Sciences, Feodosia, Crimean Region.
Source
Membr Cell Biol. 2001;14(6):773-82
Date
2001
Language
English
Publication Type
Article
Keywords
Animals
Calcimycin - pharmacology
Erythrocytes - metabolism
Fishes - blood
Humans
In Vitro
Ion Transport - drug effects
Ionophores - pharmacology
Lead - pharmacology
Potassium - metabolism
Potassium Channels - blood
Propranolol - pharmacology
Sodium - metabolism
Vanadates - pharmacology
Abstract
To assess the possibility of stimulating Ca2+-activated K+ channels, marine fish erythrocytes were incubated at 20-22 degrees C in saline containing a Ca2+-ATPase inhibitor (orthovanadate), a Ca2+ ionophore (A23187), propranolol or Pb2+. Incubation of the cells for up to 2 h under control conditions or in the presence of 5 mM NH4VO3 and 1 mM Ca2+ did not affect the intracellular K+ and Na+ concentrations. About 50% cellular K+ was lost from erythrocytes incubated in the presence of 0.01 mM A23187, 1 mM EGTA and 0.4-1.0 mM Ca2+. There was a significant loss of cellular K+ after the addition of 0.05-0.2 mM propranolol to the incubation medium. The stimulatory effect of propranolol on the K+ efflux was independent of external Ca2+. Blockers of Ca2+ transport, verapamil and Co2+, caused only a small decrease in the K+ loss induced by propranolol. The treatment of erythrocytes with 1-2 microM Pb2+ led to a minor K+ loss, but at a Pb2+ concentration of 20-50 microM, about 70% cellular K+ was lost. The K+ efflux induced by propranolol or Pb2+ was completely blocked by 1 mM quinine. The induced K+ loss from the erythrocytes was accompanied by a slight increase in the intracellular Na+ concentration. These data indicate the possibility of inducing Ca2+- and Pb2+-activated potassium channels in erythrocytes of S. porcus. A distinctive feature of the cells is a high sensitivity to propranolol, which activates K+ channels in the absence of external Ca2+.
PubMed ID
11817573 View in PubMed
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677 records – page 1 of 68.