Results 61 to 70 of about 98,042 (158)

Quantifying variability associated with high-resolution respirometry in human permeabilized skeletal muscle fibers

Advanced Exercise and Health Science
Rates of skeletal muscle mitochondrial respiration are often measured using an Oroboros Oxygraph-2K (O2K) high-resolution respirometer. The purpose of this investigation was to determine the coefficients of variation (CV) and technical error of ...
Emily J. Ferguson, Justin Bureau, Tanner Stokes, Danielle Nyman, Joel Seigel, Shivam Gandhi, Luca J. Delfinis, Brendon J. Gurd, Christopher G.R. Perry, Chris McGlory   +9 more
doaj   +1 more source

Rate-limiting Step Preceding Cytochrome c Release in Cells Primed for Fas-mediated Apoptosis Revealed by Analysis of Cellular Mosaicism of Respiratory Changes [PDF]

, 2001
In the present work, Jurkat cells undergoing anti-Fas antibody (anti-Fas)-triggered apoptosis exhibited in increasing proportion a massive release of cytochrome c from mitochondria, as revealed by double-labeling confocal immunofluorescence microscopy ...
Attardi, Giuseppe, Hájek, Petr, Villani, Gaetano   +2 more
core  

Correlation of mitochondrial respiration in platelets, peripheral blood mononuclear cells and muscle fibers

Heliyon
There is a growing interest for the possibility of using peripheral blood cells (including platelets) as markers for mitochondrial function in less accessible tissues.
Emil Westerlund, Sigurður E. Marelsson, Michael Karlsson, Fredrik Sjövall, Imen Chamkha, Eleonor Åsander Frostner, Johan Lundgren, Vineta Fellman, Erik A. Eklund, Katarina Steding-Ehrenborg, Niklas Darin, Gesine Paul, Magnus J. Hansson, Johannes K. Ehinger, Eskil Elmér   +14 more
doaj   +1 more source

Mitochondrial ATP fuels ABC transporter-mediated drug efflux in cancer chemoresistance

Nature Communications, 2021
Drug efflux through ABC transporters is a common mechanism leading to chemoresistance in cancer. Here, the authors show that mitochondrial respiration provides ATP to allow ABC transporters activity so mitochondrial respiration inhibition overcomes ...
Emily L. Giddings, Devin P. Champagne, Meng-Han Wu, Joshua M. Laffin, Tina M. Thornton, Felipe Valenca-Pereira, Rachel Culp-Hill, Karen A. Fortner, Natalia Romero, James East, Phoebe Cao, Hugo Arias-Pulido, Karatatiwant S. Sidhu, Brian Silverstrim, Yoonseok Kam, Shana Kelley, Mark Pereira, Susan E. Bates, Janice Y. Bunn, Steven N. Fiering, Dwight E. Matthews, Robert W. Robey, Domink Stich, Angelo D’Alessandro, Mercedes Rincon   +24 more
doaj   +1 more source

In silico simulation of reversible and irreversible swelling of mitochondria: The role of membrane rigidity [PDF]

, 2020
Mitochondria have been widely accepted as the main source of ATP in the cell. The inner mitochondrial membrane (IMM) is important for the maintenance of ATP production and other functions of mitochondria.
Arieli, Baranov, Bazil, Bazil, Beavis, Bernardi, Bernardi, Bernardi, Brenner, Carraro, Carroll, Chapa-Dubocq, Crockett, Giorgi, Griffiths, Halestrap, Halestrap, Halestrap, Halestrap, Hollander, Holmuhamedov, Hoppe, Ichas, Ichas, Igor Khmelinskii, Javadov, Javadov, Javadov, Kirichok, Kuznetsov, Kwong, Ladbrooke, Lehninger, Lopez-Crisosto, Makarov, Massari, O'Rourke, Palmer, Petronilli, Pokhilko, Sabzali Javadov, Scalettar, Selivanov, Shinitzky, Song, Szabo, Vladimir I. Makarov, Wodtke, Zaza Khuchua   +48 more
core   +1 more source

The methyl donor S-adenosylmethionine prevents liver hypoxia and dysregulation of mitochondrial bioenergetic function in a rat model of alcohol-induced fatty liver disease

Redox Biology, 2016
Background: Mitochondrial dysfunction and bioenergetic stress play an important role in the etiology of alcoholic liver disease. Previous studies from our laboratory show that the primary methyl donor S-Adenosylmethionine (SAM) minimizes alcohol-induced ...
Adrienne L. King, Sudheer K. Mantena, Kelly K. Andringa, Telisha Millender-Swain, Kimberly J. Dunham-Snary, Claudia R. Oliva, Corinne E. Griguer, Shannon M. Bailey   +7 more
doaj   +1 more source

Synergistic interaction of fatty acids and oxysterols impairs mitochondrial function and limits liver adaptation during nafld progression [PDF]

, 2018
The complete mechanism accounting for the progression from simple steatosis to steatohepatitis in nonalcoholic fatty liver disease (NAFLD) has not been elucidated.
Avolio, Carlo, Bellanti, Francesco, Blonda, Maria, di Bello, Giorgia, Facciorusso, Antonio, Iannelli, Giuseppina, Iuliano, Luigi, Poli, Giuseppe, Serviddio, Gaetano, Tamborra, Rosanna, Vendemiale, Gianluigi, Villani, Rosanna   +11 more
core   +2 more sources

Metformin induces distinct bioenergetic and metabolic profiles in sensitive versus resistant high grade serous ovarian cancer and normal fallopian tube secretory epithelial cells. [PDF]

, 2017
Metformin is a widely used agent for the treatment of diabetes and infertility, however, it has been found to have anti-cancer effects in a variety of malignancies including high grade serous ovarian cancer (HGSC).
Aspuria, Paul-Joseph P, Hodeib, Melissa, Karlan, Beth Y, Lunt, Sophia Y, Ogrodzinski, Martin P, Reue, Karen, Vergnes, Laurent   +6 more
core   +1 more source

Extra-matrix Mg\u3csup\u3e2+\u3c/sup\u3e Limits Ca\u3csup\u3e2+\u3c/sup\u3e Uptake and Modulates Ca\u3csup\u3e2+\u3c/sup\u3e Uptake-independent Respiration and Redox State in Cardiac Isolated Mitochondria [PDF]

, 2013
Cardiac mitochondrial matrix (m) free Ca2+ ([Ca2+]m) increases primarily by Ca2+ uptake through the Ca2+ uniporter (CU). Ca2+ uptake via the CU is attenuated by extra-matrix (e) Mg2+ ([Mg2+]e).
Blomeyer, Christoph A., Boelens, Age D., Camara, Amadou K.S., Dash, Ranjan K., Pradhan, Ranjan K., Stowe, David F.   +5 more
core   +1 more source

The Human SLC25A33 and SLC25A36 Genes of Solute Carrier Family 25 Encode Two Mitochondrial Pyrimidine Nucleotide Transporters [PDF]

, 2014
The human genome encodes 53 members of the solute carrier family 25 (SLC25), also called the mitochondrial carrier family, many of which have been shown to transport inorganic anions, amino acids, carboxylates, nucleotides, and coenzymes across the inner
Agrimi, G., Cirigliano, A., Di Noia, M. A., Iacobazzi, V., Palmieri, Ferdinando, Rinaldi, T., Todisco, S.   +6 more
core   +2 more sources