Temat: uncoupling protein - Katalog OPAC zbiorów

Skocz do pozycji: 1.

Tytuł:: Polymorphisms in the gene of UCP3 in dairy cattle
Polimorfizm w genie UCP3 u bydła mlecznego
Autorzy:: Glosinska, J.
Kowalewska-Luczak, I.
Kulig, H.
Wojdak-Maksymiec, K.
Powiązania:: https://bibliotekanauki.pl/articles/82812.pdf
Data publikacji:: 2015
Wydawca:: Zachodniopomorski Uniwersytet Technologiczny w Szczecinie. Wydawnictwo Uczelniane ZUT w Szczecinie
Tematy:: dairy cattle
gene polymorphism
milk production trait
uncoupling protein
milk productivity
Źródło:: Folia Pomeranae Universitatis Technologiae Stetinensis. Agricultura, Alimentaria, Piscaria et Zootechnica; 2015, 36
2081-1284
Pojawia się w:: Folia Pomeranae Universitatis Technologiae Stetinensis. Agricultura, Alimentaria, Piscaria et Zootechnica
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 2.

Tytuł:: The contribution of uncoupling protein and ATP synthase to state 3 respiration in Acanthamoeba castellanii mitochondria.
Autorzy:: Jarmuszkiewicz, Wiesława
Czarna, Małgorzata
Sluse-Goffart, Claudine
Sluse, Francis
Powiązania:: https://bibliotekanauki.pl/articles/1043287.pdf
Data publikacji:: 2004
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: Acanthamoeba castellanii
uncoupling protein
energy-dissipating
mitochondria
Opis:: Mitochondria of the amoeba Acanthamoeba castellanii possess a free fatty acid-activated uncoupling protein (AcUCP) that mediates proton re-uptake driven by the mitochondrial proton electrochemical gradient. We show that AcUCP activity diverts energy from ATP synthesis during state 3 mitochondrial respiration in a fatty acid-dependent way. The efficiency of AcUCP in mitochondrial uncoupling increases when the state 3 respiratory rate decreases as the AcUCP contribution is constant at a given linoleic acid concentration while the ATP synthase contribution decreases with respiratory rate. Respiration sustained by this energy-dissipating process remains constant at a given linoleic acid concentration until more than 60% inhibition of state 3 respiration by n-butyl malonate is achieved. The present study supports the validity of the ADP/O method to determine the actual contributions of AcUCP (activated with various linoleic acid concentrations) and ATP synthase in state 3 respiration of A. castellanii mitochondria fully depleted of free fatty acid-activated and describes how the two contributions vary when the rate of succinate dehydrogenase is decreased by succinate uptake limitation.
Źródło:: Acta Biochimica Polonica; 2004, 51, 2; 533-538
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 3.

Tytuł:: Uncoupling proteins in mitochondria of plants and some microorganisms.
Autorzy:: Jarmuszkiewicz, Wiesława
Powiązania:: https://bibliotekanauki.pl/articles/1044176.pdf
Data publikacji:: 2001
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: uncoupling protein
alternative oxidase
mitochondria
fatty acid
Opis:: Uncoupling proteins, members of the mitochondrial carrier family, are present in mitochondrial inner membrane and mediate free fatty acid-activated, purine-nucleotide-inhibited H+ re-uptake. Since 1995, it has been shown that the uncoupling protein is present in many higher plants and some microorganisms like non-photosynthetic amoeboid protozoon, Acanthamoeba castellanii and non-fermentative yeast Candida parapsilosis. In mitochondria of these organisms, uncoupling protein activity is revealed not only by stimulation of state 4 respiration by free fatty acids accompanied by decrease in membrane potential (these effects being partially released by ATP and GTP) but mainly by lowering ADP/O ratio during state 3 respiration. Plant and microorganism uncoupling proteins are able to divert very efficiently energy from oxidative phosphorylation, competing for ΔμH+ with ATP synthase. Functional connection and physiological role of uncoupling protein and alternative oxidase, two main energy-dissipating systems in plant-type mitochondria, are discussed.
Źródło:: Acta Biochimica Polonica; 2001, 48, 1; 145-155
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 4.

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
Powiązania:: https://bibliotekanauki.pl/articles/1040301.pdf
Data publikacji:: 2010
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: adenine nucleotide translocase (ANT)
uncoupling protein-3 (UCP3)
fatty acid-induced uncoupling
skeletal muscle mitochondria
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.
Źródło:: Acta Biochimica Polonica; 2010, 57, 4; 413-419
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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