The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Erythrocytes Possess an Intrinsic Barrier to Nitric Oxide Consumption
Open accessAbstract
It has been reported that free hemoglobin (Hb) reacts with NO at an extremely high rate (K(Hb) approximately 10(7) M(-1) s(-1)) and that the red blood cell (RBC) membrane is highly permeable to NO. RBCs, however, react with NO 500-1000 times slower. This reduction of NO reaction rate by RBCs has been attributed to the extracellular diffusion limitation. To test whether additional limitations are also important, we designed a competition test, which allows the extracellular diffusion limitation to be distinguished from transmembrane or intracellular resistance. This test exploited the competition between free Hb and RBCs for NO generated in a homogenous phase by an NO donor. If the extracellular diffusion resistance is negligible, then the results would follow a kinetic model that assumes homogenous reaction without extracellular diffusion limitation. In this case, the measured effective reaction rate constant, K(RBC), would remain invariant of the hematocrit, extracellular-free Hb concentration, and NO donor concentration. Results show that the K(RBC) approaches a constant only when the hematocrit is greater than 10%, suggesting that at higher hematocrit, the extracellular diffusion resistance is negligible. Under such a condition, the NO consumption by RBCs is still 500-1000 times slower than that by free Hb. This result suggests that intrinsic RBC factors, such as transmembrane diffusion limitation or intracellular mechanisms, exist to reduce the NO consumption by RBCs.
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Cites
Mechanism of NO-induced oxidation of myoglobin and hemoglobin
Eich, R. F., Li, T., Lemon, D. D., Doherty, D. H., Curry, S. R., Aitken, J. F., Mathews, A. J., Johnson, K. A., Smith, R. D., Phillips, et al. (1996) · Biochemistry · doi:10.1021/bi960442g · Cited by 613
Diffusion-limited reaction of free nitric oxide with erythrocytes
Liu, X., Miller, M. J. S., Joshi, M. S., Sadowska-Krowicka, H., Clark, D. A., & Lancaster, J. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.30.18709 · Cited by 512
Cited by
Cell-free hemoglobin limits nitric oxide bioavailability in sickle-cell disease
Reiter, C. D., Wang, X., Tanus-Santos, J. E., Hogg, N., Cannon, R. O., Schechter, A. N., & Gladwin, M. T. (2002) · Nature Medicine · doi:10.1038/nm1202-799 · Cited by 1,330
Export by red blood cells of nitric oxide bioactivity
Pawloski, J. R., Hess, D. T., & Stamler, J. S. (2001) · Nature · doi:10.1038/35054560 · Cited by 579
Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia
Kuhn, V., Diederich, L., Keller, T. C. S., Kramer, C. M., Lückstädt, W., Panknin, C., Suvorava, T., Isakson, B. E., Kelm, M., & Cortese-Krott, M. M. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6954 · Cited by 469
Maia, L. B., & Moura, J. J. G. (2014) · Chemical Reviews · doi:10.1021/cr400518y · Cited by 401
Kinetic and Mechanistic Studies of the NO•-Mediated Oxidation of Oxymyoglobin and Oxyhemoglobin
Herold, S., Exner, M., & Nauser, T. (2001) · Biochemistry · doi:10.1021/bi002407m · Cited by 324
Metadata
- Authors
- Vaughn, M. W., Huang, K.-T., Kuo, L., & Liao, J. C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-01
- Volume
- 275
- Issue
- 4
- Pages
- 2342-2348
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1993924886
- Cited by
- 225
- References
- 2
- FWCI
- 5.05
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Vaughn, M. W., Huang, K.-T., Kuo, L., & Liao, J. C. (2000). Erythrocytes Possess an Intrinsic Barrier to Nitric Oxide Consumption. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.275.4.2342
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