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Role of metallothionein in nitric oxide signaling as revealed by a green fluorescent fusion protein
Open accessAbstract
Although the function of metallothionein (MT), a 6- to 7-kDa cysteine-rich metal binding protein, remains unclear, it has been suggested from in vitro studies that MT is an important component of intracellular redox signaling, including being a target for nitric oxide (NO). To directly study the interaction between MT and NO in live cells, we generated a fusion protein consisting of MT sandwiched between two mutant green fluorescent proteins (GFPs). In vitro studies with this chimera (FRET-MT) demonstrate that fluorescent resonance energy transfer (FRET) can be used to follow conformational changes indicative of metal release from MT. Imaging experiments with live endothelial cells show that agents that increase cytoplasmic Ca 2+ act via endogenously generated NO to rapidly and persistently release metal from MT. A role for this interaction in intact tissue is supported by the finding that the myogenic reflex of mesenteric arteries is absent in MT knockout mice (MT −/− ) unless endogenous NO synthesis is blocked. These results are the first application of intramolecular green fluorescent protein (GFP)-based FRET in a native protein and demonstrate the utility of FRET-MT as an intracellular surrogate indicator of NO production. In addition, an important role of metal thiolate clusters of MT in NO signaling in vascular tissue is revealed.
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Cited by
Protein S-nitrosylation: Purview and parameters
Hess, D. T., Matsumoto, A., Kim, S.-O., Marshall, H. E., & Stamler, J. S. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1569 · Cited by 2,153
Metals in Neurobiology: Probing Their Chemistry and Biology with Molecular Imaging
Que, E. L., Domaille, D. W., & Chang, C. J. (2008) · Chemical Reviews · doi:10.1021/cr078203u · Cited by 2,061
Metallothionein: the multipurpose protein
Coyle, P., Philcox, J. C., Carey, L. C., & Rofe, A. M. (2002) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s00018-002-8454-2 · Cited by 1,304
Reducing the Environmental Sensitivity of Yellow Fluorescent Protein
Griesbeck, O., Baird, G. S., Campbell, R. E., Zacharias, D. A., & Tsien, R. Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102815200 · Cited by 1,023
Jiang, P., & Guo, Z. (2004) · Coordination Chemistry Reviews · doi:10.1016/j.cct.2003.10.013 · Cited by 989
Metadata
- Authors
- Pearce, L. L., Gandley, R. E., Han, W., Wasserloos, K., Stitt, M., Kanai, A. J., McLaughlin, M. K., Pitt, B. R., & Levitan, E. S.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-01-04
- Volume
- 97
- Issue
- 1
- Pages
- 477-482
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2023882972
- Cited by
- 230
- References
- 0
- FWCI
- 12.47
- Type
- journal article
- Language
- en
- Open access
- green
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- Pearce, L. L., Gandley, R. E., Han, W., Wasserloos, K., Stitt, M., Kanai, A. J., McLaughlin, M. K., Pitt, B. R., & Levitan, E. S. (2000). Role of metallothionein in nitric oxide signaling as revealed by a green fluorescent fusion protein. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.97.1.477
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