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Science 27 June 1997:
Vol. 276. no. 5321, pp. 2034 - 2037
DOI: 10.1126/science.276.5321.2034
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Reports

Blood Flow Regulation by S-Nitrosohemoglobin in the Physiological Oxygen Gradient

Jonathan S. Stamler, * Li Jia, Jerry P. Eu, Timothy J. McMahon, Ivan T. Demchenko, Joseph Bonaventura, Kim Gernert, Claude A. Piantadosi

The binding of oxygen to heme irons in hemoglobin promotes the binding of nitric oxide (NO) to cysteinebeta 93, forming S-nitrosohemoglobin. Deoxygenation is accompanied by an allosteric transition in S-nitrosohemoglobin [from the R (oxygenated) to the T (deoxygenated) structure] that releases the NO group. S-nitrosohemoglobin contracts blood vessels and decreases cerebral perfusion in the R structure and relaxes vessels to improve blood flow in the T structure. By thus sensing the physiological oxygen gradient in tissues, hemoglobin exploits conformation-associated changes in the position of cysteinebeta 93 SNO to bring local blood flow into line with oxygen requirements.

J. S. Stamler, Department of Medicine, Divisions of Respiratory and Cardiovascular Medicine and Department of Cell Biology, Duke University Medical Center, Room 321 MSRB, Box 2612, Durham, NC 27710, USA.
L. Jia, J. P. Eu, T. J. McMahon, I. T. Demchenko, C. A. Piantadosi, Department of Medicine, Division of Respiratory Medicine, Duke University Medical Center, Durham, NC 27710, USA.
J. Bonaventura, Department of Cell Biology and Nicholas School of the Environment, Duke University Medical Center, Durham, NC 27710, USA.
K. Gernert, Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
*   To whom correspondence should be addressed.

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Effects of S-Nitrosation and Cross-Linking of Hemoglobin on Hypoxic Pulmonary Vasoconstriction in Isolated Rat Lungs.
S. Deem, J.-U. Kim, B. N. Manjula, A. S. Acharya, M. E. Kerr, R. P. Patel, M. T. Gladwin, and E. R. Swenson (2002)
Circ. Res. 91, 626-632
   Abstract »    Full Text »    PDF »
Nitric oxide is consumed, rather than conserved, by reaction with oxyhemoglobin under physiological conditions.
M. S. Joshi, T. B. Ferguson Jr., T. H. Han, D. R. Hyduke, J. C. Liao, T. Rassaf, N. Bryan, M. Feelisch, and J. R. Lancaster Jr. (2002)
PNAS 99, 10341-10346
   Abstract »    Full Text »    PDF »
S-Nitrosohemoglobin Is Unstable in the Reductive Erythrocyte Environment and Lacks O2/NO-linked Allosteric Function.
M. T. Gladwin, X. Wang, C. D. Reiter, B. K. Yang, E. X. Vivas, C. Bonaventura, and A. N. Schechter (2002)
J. Biol. Chem. 277, 27818-27828
   Abstract »    Full Text »    PDF »
Heme Nitrosylation of Deoxyhemoglobin by S-Nitrosoglutathione Requires Copper.
A. A. Romeo, J. A. Capobianco, and A. M. English (2002)
J. Biol. Chem. 277, 24135-24141
   Abstract »    Full Text »    PDF »
Cardiopulmonary Responses to Exercise in Women with Sickle Cell Anemia.
L. A. Callahan, K. F. Woods, G. A. Mensah, L. T. Ramsey, P. Barbeau, and B. Gutin (2002)
Am. J. Respir. Crit. Care Med. 165, 1309-1316
   Abstract »    Full Text »    PDF »
Heme Redox Properties of S-Nitrosated Hemoglobin A0 and Hemoglobin S. IMPLICATIONS FOR INTERACTIONS OF NITRIC OXIDE WITH NORMAL AND SICKLE RED BLOOD CELLS.
C. Bonaventura, C. H. Taboy, P. S. Low, R. D. Stevens, C. Lafon, and A. L. Crumbliss (2002)
J. Biol. Chem. 277, 14557-14563
   Abstract »    Full Text »    PDF »
Basal and Stimulated Protein S-Nitrosylation in Multiple Cell Types and Tissues.
A. J. Gow, Q. Chen, D. T. Hess, B. J. Day, H. Ischiropoulos, and J. S. Stamler (2002)
J. Biol. Chem. 277, 9637-9640
   Abstract »    Full Text »    PDF »
Complex Regulation of iNOS in Lung.
B. R. Pitt and C. M. St. Croix (2002)
Am. J. Respir. Cell Mol. Biol. 26, 6-9
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