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Your search keyword '"Pelto‐Huikko, Markku"' showing total 7 results
Start Over Author "Pelto‐Huikko, Markku" Journal journal of biological chemistry
7 results on '"Pelto‐Huikko, Markku"'

3. Human Mitochondrial Thioredoxin

Author

Damdimopoulos, Anastasios E., primary, Miranda-Vizuete, Antonio, additional, Pelto-Huikko, Markku, additional, Gustafsson, Jan-Åke, additional, and Spyrou, Giannis, additional

Published
2002
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6. Competition between Thyroid Hormone Receptor-associated Protein (TRAP) 220 and Transcriptional Intermediary Factor (TIF) 2 for Binding to Nuclear Receptors

Author

Treuter, Eckardt, primary, Johansson, Lotta, additional, Thomsen, Jane S., additional, Wärnmark, Anette, additional, Leers, Jörg, additional, Pelto-Huikko, Markku, additional, Sjöberg, Maria, additional, Wright, Anthony P.H., additional, Spyrou, Giannis, additional, and Gustafsson, Jan-Åke, additional

Published
1999
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7. Human mitochondrial thioredoxin. Involvement in mitochondrial membrane potential and cell death.

Author

Damdimopoulos AE, Miranda-Vizuete A, Pelto-Huikko M, Gustafsson JA, and Spyrou G

Subjects
Amino Acid Sequence, Blotting, Western, Cell Death, Cell Line, Cloning, Molecular, DNA, Complementary metabolism, Dose-Response Relationship, Drug, Enzyme Inhibitors pharmacology, Etoposide pharmacology, Humans, Immunohistochemistry, Membrane Potentials, Microscopy, Fluorescence, Mitochondrial Proteins genetics, Mitochondrial Proton-Translocating ATPases metabolism, Molecular Sequence Data, Oligomycins pharmacology, Protein Binding, RNA, Messenger metabolism, Rotenone pharmacology, Sequence Homology, Amino Acid, Thioredoxins genetics, Time Factors, Tissue Distribution, Transfection, Mitochondria physiology, Mitochondrial Proteins physiology, Thioredoxins metabolism
Abstract

Thioredoxins (Trx) are a class of small multifunctional redox-active proteins found in all organisms. Recently, we reported the cloning of a mitochondrial thioredoxin, Trx2, from rat heart. To investigate the biological role of Trx2 we have isolated the human homologue, hTrx2, and generated HEK-293 cells overexpressing Trx2 (HEK-Trx2). Here, we show that HEK-Trx2 cells are more resistant toward etoposide. In addition, HEK-Trx2 are more sensitive toward rotenone, an inhibitor of complex I of the respiratory chain. Finally, overexpression of Trx2 confers an increase in mitochondrial membrane potential, DeltaPsi(m). Treatment with oligomycin could both reverse the effect of rotenone and decrease the membrane potential suggesting that Trx2 interferes with the activity of ATP synthase. Taken together, these results suggest that Trx2 interacts with specific components of the mitochondrial respiratory chain and plays an important role in the regulation of the mitochondrial membrane potential.

Published
2002
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