The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Mitochondrial Thioredoxin-Responding Off–On Fluorescent Probe
Abstract
We synthesized a new probe, Mito-Naph, to visualize mitochondrial thioredoxin (Trx) activity in cells. A fluorescence off-on change is induced by disulfide cleavage of the probe, resulting from a reaction with Trx and subsequent intramolecular cyclization by the released thiolate to give a fluorescent product. By measuring the fluorescence at 540 nm, Trx activity can be detected at nanomolar concentrations (down to 50 nM) well below its physiological levels. The in vitro and in vivo Trx preference of Mito-Naph was demonstrated by fluorometric and confocal microscopic experiments. In vitro kinetic analysis of the disulfide bond cleavage revealed that the second-order rate constant for Trx is (4.04 ± 0.26) × 10(3) (M s)(-1), approximately 5000 times faster than that for GSH. The inhibition experiments involving PX-12, a selective inhibitor of Trx, also revealed that the emission from Mito-Naph significantly decreased in PX-12 dose-dependent manners, both in living cells and in cellular protein extracts. The Trx preference was further supported by an observation that the fluorescence intensity of rat liver extract was decreased according to the Trx depletion by immunoprecipitation. On the basis of these results, it is concluded that Mito-Naph preferentially reacts with Trx, compared with other biological thiols containing amino acids in vitro and in vivo.
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Citations
Cites
Thioredoxin-interacting protein links oxidative stress to inflammasome activation
Zhou, R., Tardivel, A., Thorens, B., Choi, I., & Tschopp, J. (2010) · Nature Immunology · doi:10.1038/ni.1831 · Cited by 2,708
Mammalian thioredoxin is a direct inhibitor of apoptosis signal‐regulating kinase (ASK) 1
Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., Kawabata, M., Miyazono, K., & Ichijo, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.9.2596 · Cited by 2,377
Hydrogen peroxide mediates amyloid β protein toxicity
Behl, C. (1994) · Cell · doi:10.1016/0092-8674(94)90131-7 · Cited by 2,074
Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
Hwang, C., Sinskey, A. J., & Lodish, H. F. (1992) · Science · doi:10.1126/science.1523409 · Cited by 1,968
Fluorescent and colorimetric probes for detection of thiols
Chen, X., Zhou, Y., Peng, X., & Yoon, J. (2010) · Chemical Society Reviews · doi:10.1039/b925092a · Cited by 1,580
Selective fluorescent imaging of superoxide in vivo using ethidium-based probes
Robinson, K. M., Janes, M. S., Pehar, M., Monette, J. S., Ross, M. F., Hagen, T. M., Murphy, M. P., & Beckman, J. S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601945103 · Cited by 777
Nonn, L., Williams, R. R., Erickson, R. P., & Powis, G. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.3.916-922.2003 · Cited by 438
Thioredoxin‐2 (TRX‐2) is an essential gene regulating mitochondria‐dependent apoptosis
Tanaka, T., Hosoi, F., Yamaguchi‐Iwai, Y., Nakamura, H., Masutani, H., Ueda, S., Nishiyama, A., Takeda, S., Wada, H., Spyrou, G., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/21.7.1695 · Cited by 322
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Li, Y., Jarvis, R., Zhu, K., Glass, Z., Ogurlu, R., Gao, P., Li, P., Chen, J., Yu, Y., Yang, Y., et al. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202004994 · Cited by 75
Metadata
- Authors
- Lee, M. H., Han, J. H., Lee, J.-H., Choi, H. G., Kang, C., & Kim, J. S.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2012-10-05
- Volume
- 134
- Issue
- 41
- Pages
- 17314-17319
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2319499784
- Cited by
- 161
- References
- 8
- FWCI
- 6.39
- Type
- journal article
- Language
- en
- Open access
- closed
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