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Prepublished online as a Blood First Edition Paper on January 30, 2003; DOI 10.1182/blood-2002-12-3825.
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Blood, 1 June 2003, Vol. 101, No. 11, pp. 4408-4415
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Vasoactivity of S-nitrosohemoglobin: role of oxygen, heme, and NO oxidation states
Jack H. Crawford,
C. Roger White, and
Rakesh P. Patel
From the Department of Pathology, the Center for Free Radical Biology, and the Department of Medicine, University of Alabama at Birmingham, Birmingham, AL.
The mechanisms by which S-nitrosohemoglobin (SNOHb) stimulates vasodilation are unclear and underlie the controversies surrounding the proposal that this S-nitrosothiol modulates blood flow in vivo. Among the mechanistic complexities are the nature of vasoactive species released from SNOHb and the role heme and oxygen play in this process. This is important to address since hemoglobin inhibits NO-dependent vasodilation. We compared the vasodilatory properties of distinct oxidation and ligation states of SNOHb at different oxygen tensions. The results show that SNOHb in the oxygenated state (SNOoxyHb) is significantly less efficient than SNOHb in the ferric or met oxidation state (SNOmetHb) at stimulating relaxation of isolated rat aortic rings. Using pharmacologic approaches to modulate nitrogen monoxide radical (·NO)–dependent relaxation, our data suggest that SNOoxyHb promotes vasodilation in a ·NO-independent manner. In contrast, both SNOmetHb and S-nitrosoglutathione (GSNO), a putative intermediate in SNOHb reactivity, elicit vasodilation in a ·NO-dependent process. Consistent with previous observations, an increase in sensitivity of SNOHb vasodilation at low oxygen tensions also was observed. However, this was not exclusive for this protein but applied to a range of nitrosovasodilators (including a ·NO donor [DeaNonoate], an S-nitrosothiol [GSNO], and the nitroxyl anion donor, Angelis salt). This suggests that oxygen-dependent modulation of SNOHb vasoactivity does not occur by controlling the allosteric state of Hb but is a property of vessel responsiveness to nitrosovasodilators at low oxygen tensions.
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S-nitrosohemoglobin is distinguished from other nitrosovasodilators by unique oxygen-dependent responses that support an allosteric mechanism of action
- Timothy J. McMahon, John R. Pawloski, Douglas T. Hess, Claude A. Piantadosi, Benjamin P. Luchsinger, David J. Singel, Jonathan S. Stamler, Jack H. Crawford, C. Roger White, and Rakesh P. Patel
Blood 2003 102: 410-411.
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