Purification, Molecular Cloning, and Characterization of TRP32, a Novel Thioredoxin-related Mammalian Protein of 32 kDa

Lee, Kyung-Kwon; Murakawa, Masao; Takahashi, Shuntaro; Tsubuki, Satoshi; Kawashima, Seiichi; Sakamaki, Kazuhiro; Yonehara, Shin

doi:10.1074/jbc.273.30.19160

Cited by 81 publications

(77 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…8) Trx supports six peroxiredoxins (PDRX) that have heterogeneous subcellular distributions but a common activity to eliminate peroxides (146). Redox functions can be provided by Trx-related proteins (TRP14, TRP32, nucleeoredoxin and Trx-related transmembrane protein), which contain a Trx motif and may have evolved to recognize distinctive groups of proteins from those recognized by Trx-1 (105,107,122,198). A large number of Trx-like proteins are known (below dotted line), and many of these are likely to be redox active, either in pathways dependent on Trx or in parallel pathways, which evolved to provide additional specificity beyond that provided by the Trx proteins.…”

Section: Gsh and Trxs As Common Control Nodes For Protein Thiol Redoxmentioning

confidence: 99%

Radical-free biology of oxidative stress

Jones¹

2008

American Journal of Physiology-Cell Physiology

997

839

View full text Add to dashboard Cite

Free radical-induced macromolecular damage has been studied extensively as a mechanism of oxidative stress, but large-scale intervention trials with free radical scavenging antioxidant supplements show little benefit in humans. The present review summarizes data supporting a complementary hypothesis for oxidative stress in disease that can occur without free radicals. This hypothesis, which is termed the "redox hypothesis," is that oxidative stress occurs as a consequence of disruption of thiol redox circuits, which normally function in cell signaling and physiological regulation. The redox states of thiol systems are sensitive to twoelectron oxidants and controlled by the thioredoxins (Trx), glutathione (GSH), and cysteine (Cys). Trx and GSH systems are maintained under stable, but nonequilibrium conditions, due to a continuous oxidation of cell thiols at a rate of about 0.5% of the total thiol pool per minute. Redox-sensitive thiols are critical for signal transduction (e.g., H-Ras, PTP-1B), transcription factor binding to DNA (e.g., Nrf-2, nuclear factor-B), receptor activation (e.g., ␣IIb␤3 integrin in platelet activation), and other processes. Nonradical oxidants, including peroxides, aldehydes, quinones, and epoxides, are generated enzymatically from both endogenous and exogenous precursors and do not require free radicals as intermediates to oxidize or modify these thiols. Because of the nonequilibrium conditions in the thiol pathways, aberrant generation of nonradical oxidants at rates comparable to normal oxidation may be sufficient to disrupt function. Considerable opportunity exists to elucidate specific thiol control pathways and develop interventional strategies to restore normal redox control and protect against oxidative stress in aging and age-related disease.thioredoxin; glutathione; cysteine; hydrogen peroxide; redox signaling; protein thiol ONE OF THE GREAT REDOX BIOLOGISTS of the past century, Howard S. Mason, professed that to advance science, a scientist must interpret observations at the limit of their meaning. The present review of the redox biology of thiol systems addresses the possibility that disruption of the function and homeostasis of thiol systems is the most central feature of oxidative stress that contributes to mechanisms of aging and age-related disease. I have termed this the "redox hypothesis" to facilitate distinction from free radical hypotheses.Many proteins contain redox-sensitive thiols, and reactions of thiol systems occur largely by nonradical two-electron transfers. Accumulating data show that central thiol-disulfide couples are maintained under nonequilibrium conditions in biological systems. This presents a condition wherein changes in abundance and distribution of redox catalysts and changes in rates of generation of relevant oxidants (e.g., peroxides) and precursors for NADPH supply can account for pathological effects of oxidative stress through altered functions of enzymes, receptors, transporters, transcription factors, and structural elements, without free ra...

show abstract

Section: Gsh and Trxs As Common Control Nodes For Protein Thiol Redoxmentioning

confidence: 99%

Radical-free biology of oxidative stress

Jones¹

2008

American Journal of Physiology-Cell Physiology

997

839

View full text Add to dashboard Cite

show abstract

“…Cleavage products were indicated with arrows the sequence, Cys-Gly-Pro-Cys, are necessary for the redox function of thioredoxin (Arner and Holmgren, 2000). Several thioredoxins or thioredoxin-like proteins exist in mammalian cells (Kurooka et al, 1997;Lee et al, 1998b;Spyrou et al, 1997), whose individual physiologic roles have not been clearly understood. The most-well characterized member of these thioredoxins, Trx1, is critical for mammalian development because a homozygous deletion of this gene causes embryonic lethality in mice (Matsui et al, 1996).…”

Section: Discussionmentioning

confidence: 99%

Thioredoxin participates in a cell death pathway induced by interferon and retinoid combination

Karra

Lindner

et al. 2001

Oncogene

View full text Add to dashboard Cite

“…Although several thioredoxin or thioredoxin-like proteins have been described in mammalian cells (Kurooka et al, 1997;Lee et al, 1998;Spyrou et al, 1997), their physiologic roles have not been clearly understood. The well characterized of these, Trx1, is critical for mammalian development (Matsui et al, 1996).…”

Section: Discussionmentioning

confidence: 99%

Modulation of p53 dependent gene expression and cell death through thioredoxin-thioredoxin reductase by the Interferon-Retinoid combination

Lindner

et al. 2001

Oncogene

View full text Add to dashboard Cite

Purification, Molecular Cloning, and Characterization of TRP32, a Novel Thioredoxin-related Mammalian Protein of 32 kDa

Abstract: We purified a protein of 32 kDa from human thymoma HPB-ALL cells that was co-purified with a catalytic fragment of MST (mammalian STE-20-like), a kinase of the STE20 family, which is proteolytically activated by caspase in apoptosis (

Cited by 81 publications

References 45 publications

Radical-free biology of oxidative stress

Radical-free biology of oxidative stress

Thioredoxin participates in a cell death pathway induced by interferon and retinoid combination

Modulation of p53 dependent gene expression and cell death through thioredoxin-thioredoxin reductase by the Interferon-Retinoid combination

Contact Info

Product

Resources

About