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100 records – page 1 of 10.

ACE gene polymorphism explains 30-40% of variability in serum ACE activity in both women and men in the population at large: the Copenhagen City Heart Study.

https://arctichealth.org/en/permalink/ahliterature199818
Source
Atherosclerosis. 1999 Dec;147(2):425-7
Publication Type
Article
Date
Dec-1999

Acetaminophen prevents aging-associated hyperglycemia in aged rats: effect of aging-associated hyperactivation of p38-MAPK and ERK1/2.

https://arctichealth.org/en/permalink/ahliterature90253
Source
Diabetes Metab Res Rev. 2009 Mar;25(3):279-86
Publication Type
Article
Date
Mar-2009
Author
Wu Miaozong
Desai Devashish H
Kakarla Sunil K
Katta Anjaiah
Paturi Satyanarayana
Gutta Anil K
Rice Kevin M
Walker Ernest M
Blough Eric R
Author Affiliation
Department of Biological Sciences, Marshall University, Huntington, WV 25755-1090, USA.
Source
Diabetes Metab Res Rev. 2009 Mar;25(3):279-86
Date
Mar-2009
Language
English
Publication Type
Article
Keywords
Acetaminophen - pharmacology
Aging - drug effects - physiology
Animals
Blood Glucose - drug effects
Enzyme Activation - drug effects
Glucose Transporter Type 4 - metabolism
Hyperglycemia - prevention & control
Liver - drug effects
Mitogen-Activated Protein Kinase 1 - metabolism
Mitogen-Activated Protein Kinase 3 - metabolism
Muscle, Skeletal - drug effects - physiology
Rats
Rats, Inbred BN
Rats, Inbred F344
Superoxides - metabolism
p38 Mitogen-Activated Protein Kinases - metabolism
Abstract
BACKGROUND: Aging-related hyperglycemia is associated with increased oxidative stress and diminished muscle glucose transporter-4 (Glut4) that may be regulated, at least in part, by the mitogen-activated protein kinases (MAPK). METHODS: To test the possibility that aging-related hyperglycemia can be prevented by pharmacological manipulation of MAPK hyperactivation, aged (27-month old) Fischer 344/NNiaHSD x Brown Norway/BiNia F1 (F344BN) rats were administered acetaminophen (30 mg/kg body weight/day) for 6 months in drinking water. RESULTS: Hepatic histopathology, serum aspartate aminotransferase and alanine aminotransferase analyses suggested that chronic acetaminophen did not cause hepatotoxicity. Compared with adult (6-month) and aged (27-month) rats, very aged rats (33-month) had higher levels of blood glucose, phosphorylation of soleus p38-MAPK and extracellular-regulated kinase 1/2 (ERK1/2), superoxide and oxidatively modified proteins (p
PubMed ID
19177471 View in PubMed
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[Action of electrical stimulation of the structures of the posterior hypothalamus on the acetylcholinesterase activity of the motor portion of the cortex normally and under pharmacological influences]

https://arctichealth.org/en/permalink/ahliterature13137
Source
Fiziol Zh. 1977 Sep-Oct;23(5):591-8
Publication Type
Article

[Activated protein C resistance as a cause of thrombophilia]

https://arctichealth.org/en/permalink/ahliterature64478
Source
Rev Invest Clin. 1996 May-Jun;48(3):223-9
Publication Type
Article
Author
G J Ruiz-Argüelles
Author Affiliation
Laboratorios Clínicos de Puebla, México.
Source
Rev Invest Clin. 1996 May-Jun;48(3):223-9
Language
Spanish
Publication Type
Article
Keywords
Antithrombin III - analysis
Blood Coagulation Factors - analysis - physiology
DNA Mutational Analysis
English Abstract
Enzyme Activation
Factor V - genetics
Factor V Deficiency - complications - epidemiology
Female
Humans
Male
Mexico - epidemiology
Partial Thromboplastin Time
Phenotype
Pregnancy
Pregnancy Complications, Hematologic - epidemiology - etiology
Prevalence
Protein C - physiology
Protein S - analysis
Thrombosis - blood - genetics
Abstract
The proportion of identifiable causes of familial thrombophilia has increased from 5-10% to 60-70% since the identification of activated protein C resistance (aPCR) in February 1993 by Dahlbäck et al. A mutation in the factor V gene (G-->A, 1691) leads to the so called Leiden mutation (R 506 Q) that produces a mutated factor V resistant to the catalytic action of activated protein C (aPC), yet normal in its procoagulant properties. This recently identified aPCR is in Nordic populations the most prevalent and well defined genetic defect associated with disease so far described. Its prevalence in the general population ranges from 0% to up to 15% and suggests that a positive genetic selection pressure has been involved. The aPCR phenotype can be assessed in vitro by measurement of the prolongation of the activated partial thromboplastin time in the presence of aPC, whereas the aPCR genotype is studied using polymerase chain reaction searching for the Arg to Gln mutation in the coagulation factor V gene. Some acquired conditions such as the presence of lupus anticoagulants, antiphospholipid antibodies, pregnancy, liver disease and contraceptives may lead into the aPCR phenotype. The aPCR search must be the initial step in the study of a patient with thrombophilia, either inherited or acquired aPCR together with protein C, protein S and antithrombin III explain 60 to 70% of cases of familial thrombophilia.
PubMed ID
8966383 View in PubMed
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Activating glucokinase (GCK) mutations as a cause of medically responsive congenital hyperinsulinism: prevalence in children and characterisation of a novel GCK mutation.

https://arctichealth.org/en/permalink/ahliterature85895
Source
Eur J Endocrinol. 2008 Jul;159(1):27-34
Publication Type
Article
Date
Jul-2008
Author
Christesen Henrik B T
Tribble Nicholas D
Molven Anders
Siddiqui Juveria
Sandal Tone
Brusgaard Klaus
Ellard Sian
Njølstad Pål R
Alm Jan
Brock Jacobsen Bendt
Hussain Khalid
Gloyn Anna L
Author Affiliation
HC Andersen Children's Hospital, Odense University Hospital, DK-5000 Odense C, Denmark.
Source
Eur J Endocrinol. 2008 Jul;159(1):27-34
Date
Jul-2008
Language
English
Publication Type
Article
Keywords
Cohort Studies
Denmark - epidemiology
Enzyme Activation - drug effects
Gene Frequency
Genotype
Glucokinase - genetics - metabolism
Glucose - metabolism
Great Britain - epidemiology
Heterozygote
Mutation
Norway - epidemiology
Persistent Hyperinsulinemia Hypoglycemia of Infancy - drug therapy - epidemiology - genetics
Prevalence
Substrate Specificity
Abstract
OBJECTIVE: Activating glucokinase (GCK) mutations are a rarely reported cause of congenital hyperinsulinism (CHI), but the prevalence of GCK mutations is not known. METHODS: From a pooled cohort of 201 non-syndromic children with CHI from three European referral centres (Denmark, n=141; Norway, n=26; UK, n=34), 108 children had no K(ATP)-channel (ABCC8/KCNJ11) gene abnormalities and were screened for GCK mutations. Novel GCK mutations were kinetically characterised. RESULTS: In five patients, four heterozygous GCK mutations (S64Y, T65I, W99R and A456V) were identified, out of which S64Y was novel. Two of the mutations arose de novo, three were dominantly inherited. All the five patients were medically responsive. In the combined Danish and Norwegian cohort, the prevalence of GCK-CHI was estimated to be 1.2% (2/167, 95% confidence interval (CI) 0-2.8%) of all the CHI patients. In the three centre combined cohort of 72 medically responsive children without K(ATP)-channel mutations, the prevalence estimate was 6.9% (5/72, 95% CI 1.1-12.8%). All activating GCK mutations mapped to the allosteric activator site. The novel S64Y mutation resulted in an increased affinity for the substrate glucose (S(0.5) 1.49+/-0.08 and 7.39+/-0.05 mmol/l in mutant and wild-type proteins respectively), extrapolating to a relative activity index of approximately 22 compared with the wild type. CONCLUSION: In the largest study performed to date on GCK in children with CHI, GCK mutations were found only in medically responsive children who were negative for ABCC8 and KCNJ11 mutations. The estimated prevalence (approximately 7%) suggests that screening for activating GCK mutations is warranted in those patients.
PubMed ID
18450771 View in PubMed
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Activation and relocalization of caspase 3 during the apoptotic cascade of human mesothelioma cells.

https://arctichealth.org/en/permalink/ahliterature16909
Source
APMIS. 2005 Jun;113(6):426-35
Publication Type
Article
Date
Jun-2005
Author
Y. Soini
K. Kahlos
R. Sormunen
M. Säily
P. Mäntymaa
P. Koistinen
P. Pääkkö
V. Kinnula
Author Affiliation
Department of Pathology, University of Oulu, Finland. msoini@cc.oulu.fi
Source
APMIS. 2005 Jun;113(6):426-35
Date
Jun-2005
Language
English
Publication Type
Article
Keywords
Antibiotics, Antineoplastic - pharmacology
Antigens, CD95 - genetics - metabolism
Apoptosis
Caspases - analysis - metabolism
Enzyme Activation
Epirubicin - pharmacology
Humans
Membrane Glycoproteins - genetics - metabolism
Mesothelioma - enzymology
Research Support, Non-U.S. Gov't
Tumor Cells, Cultured
Abstract
Apoptosis plays an important role in cancer biology. We investigated the expression of caspases 3 and 8 in malignant mesothelioma and malignant mesothelioma cell lines and putative changes in their ultrastructural expression prior and after exposure to epirubicin. Further studies were conducted to compare these changes to the localization and expression of the bcl-2 group of proteins bcl-X, bax and mcl-1, and Fas-Fas ligand in the same cells. In the histological samples, caspase 3 and 8 immunoreactivity was seen in 27/37 (73%) and 16/37 (43%) of the mesotheliomas. The immunostaining was cytoplasmic diffuse, granular, and occasionally nuclear. All six mesothelioma cell lines expressed caspases 3 and 8 by immunoblotting. After exposure to epirubicin the extent of apoptosis was increased in all cell lines investigated, being weakest in the most resistant M38K cell line. Immunoelectron microscopy revealed immunogold labeling for caspases 3 and 8 in the mitochondria with the accumulation of caspase 3 in the apoptotic bodies, while the mitochondrial localization of the bcl-2 proteins appeared to be very stable. Fas receptor could be detected by flow cytometry, whereas the most resistant cell line (M38K) lacked Fas ligand when assessed by RT-PCR. These results suggest the importance of caspase 3 during the apoptotic process of mesothelioma cells and indicate that epirubicin-induced apoptosis is independent of the mitochondrial pathway.
PubMed ID
15996160 View in PubMed
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[Activation of plasminogen with immobilized trypsin]

https://arctichealth.org/en/permalink/ahliterature65930
Source
Ukr Biokhim Zh. 1979 Jul-Aug;51(4):335-9
Publication Type
Article
Author
E V Eretskaia
S A Kudinov
Source
Ukr Biokhim Zh. 1979 Jul-Aug;51(4):335-9
Language
Ukrainian
Publication Type
Article
Keywords
English Abstract
Enzyme Activation
Enzymes, Immobilized - metabolism
Female
Fetal Blood - metabolism
Humans
Hydrogen-Ion Concentration
Kinetics
Placenta
Plasminogen - metabolism
Pregnancy
Temperature
Trypsin - metabolism
Abstract
Human plasminogen isolated from the placenta serum fraction by means of affinity chromatography was activated by trypsin being in covalent bond with sepharose. The activation is studied as dependent on pH, temperature and the proenzyme-activator ratio in the presence of 25% glycerol as a stabilizing agent and without it. Utilization of the immobilized trypsin as a plasminogen activator makes it possible to transform completely the proenzyme to plasmin varying the plasminogen-trypsin ratio and time of activation when it is conducted under optimal conditions: in the presence of 25% glycerol at pH 7.0-7.1 and the temperature of 30 degrees C.
PubMed ID
38546 View in PubMed
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[Activity of serum enzymes in workers in the enzyme production industry]

https://arctichealth.org/en/permalink/ahliterature73828
Source
Gig Sanit. 1989 Dec;(12):21-3
Publication Type
Article
Date
Dec-1989
Author
A A Kuchuk
F A Onikienko
Source
Gig Sanit. 1989 Dec;(12):21-3
Date
Dec-1989
Language
Russian
Publication Type
Article
Keywords
Acid Phosphatase - blood
Adult
Cholinesterases - blood - deficiency
English Abstract
Enzyme Activation
Enzymes - biosynthesis
Female
Humans
Industrial Microbiology
L-Lactate Dehydrogenase - blood
Male
Monoamine Oxidase - blood
Occupational Medicine
Ukraine
Abstract
Unfavorable industrial factors in the production of enzyme preparations (enzyme dusts, microorganisms-producers) cause changes in the activity of a number of enzymes in workers' blood serum. Degree frequency and direction of enzyme shifts depend on the purity of enzyme preparations, degree of contact with them, workers' length of service and health status. The analysis of the obtained results enables us to recommend a determination of cholinesterase activity, acid phosphatase and lactate-dehydrogenase as indicators for a hygienic assessment of the effect of enzyme preparations and diagnosis of body pathogenic changes.
PubMed ID
2628194 View in PubMed
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100 records – page 1 of 10.