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Wyszukujesz frazę "UCP3" wg kryterium: Temat


Wyświetlanie 1-3 z 3
Tytuł:
Genetic variants of uncoupling proteins-2 and -3 in relation to maximal oxygen uptake in different sports
Autorzy:
Holdys, Joanna
Gronek, Piotr
Kryściak, Jakub
Stanisławski, Daniel
Tematy:
UCP2
athletic performance
genetic polymorphism
UCP3
energy efficiency
Pokaż więcej
Wydawca:
Polskie Towarzystwo Biochemiczne
Powiązania:
https://bibliotekanauki.pl/articles/1039610.pdf  Link otwiera się w nowym oknie
Opis:
Uncoupling proteins 2 and 3 (UCP2 and UCP3) as mitochondrial electron transporters are involved in regulation of ATP production and energy dissipation as heat. Energy efficiency plays an important role in physical performance, especially in aerobic fitness. The aim of this study was to examine the association between maximal oxygen uptake and genetic variants of the UCP2 and UCP3 genes. The studies were carried out in a group of 154 men and 85 women, professional athletes representing various sports and fitness levels and students of the University of Physical Education in Poznań. Physiological and molecular procedures were used, i.e. direct measurement of maximum oxygen uptake (VO2max) and analysis of an insertion/deletion (I/D) polymorphism in the 3'untranslated region of exon 8 of the UCP2 gene and a C>T substitution in exon 5 (Y210Y) of the UCP3 gene. No statistically significant associations were found, only certain trends. Insertion allele (I) of the I/D UCP2 and the T allele of the UCP3 gene were favourable in obtaining higher VO2max level and might be considered as endurance-related alleles.
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
A comparative study of the inhibitory effects of purine nucleotides and carboxyatractylate on the uncoupling protein-3 and adenine nucleotide translocase
Autorzy:
Komelina, Natalia
Amerkhanov, Zarif
Tematy:
adenine nucleotide translocase (ANT)
uncoupling protein-3 (UCP3)
fatty acid-induced uncoupling
skeletal muscle mitochondria
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Wydawca:
Polskie Towarzystwo Biochemiczne
Powiązania:
https://bibliotekanauki.pl/articles/1040301.pdf  Link otwiera się w nowym oknie
Opis:
Uncoupling proteins (UCPs) mediate fatty acid-induced proton cycling in mitochondria, which is stimulated by superoxide and inhibited by GDP. Fatty acid anions can also be transported by adenine nucleotide translocase (ANT), thus resulting in the uncoupling of oxidative phosphorylation. In the present work, an attempt was made to distinguish between the protonophoric activity of UCP3 and that of ANT using inhibition analysis. This study was carried out using mitochondria from skeletal muscles of hibernating Yakut ground squirrel, which have a significant level of UCP3 mRNA. We found that millimolar concentrations of GDP, which is considered to be a specific inhibitor of UCPs, slightly recoupled the mitochondrial respiration and restored the membrane potential. Addition of the specific ANT inhibitor CAT (carboxyatractylate), in micromolar concentration, prior to GDP prevented its recoupling effect. Moreover, GDP and ADP exhibited a competitive kinetic behavior with respect to ANT. In brown adipose tissue, CAT did not prevent the UCP1-iduced increase in chloride permeability and the inhibitory effect of GDP, thus confirming the inability of CAT to affect UCP1. These results allow us to conclude that the recoupling effect of purine nucleotides on skeletal muscle mitochondria of hibernating ground squirrels can be explained by interaction of the nucleotides with ANT, whereas UCP3 is not involved in the process.
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Cross-species hybridizations in situ of genes associated with meat production traits in the wild pig genome
Międzygatunkowe hybrydyzacje in situ genów związanych z cechami użytkowości mięsnej w genomie dzika
Autorzy:
Kozubska-Sobocinska, A.
Danielak-Czech, B.
Babicz, M.
Tematy:
wild pig
fluorescence in situ hybridization
cross-species hybridization
in situ hybridization
gene
meat production trait
genome
ghrelin
UCP2 gene
UCP3 gene
Pokaż więcej
Wydawca:
Uniwersytet Przyrodniczy w Lublinie. Wydawnictwo Uniwersytetu Przyrodniczego w Lublinie
Powiązania:
https://bibliotekanauki.pl/articles/2196829.pdf  Link otwiera się w nowym oknie
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

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