Format

Send to:

Choose Destination
See comment in PubMed Commons below
Blood. 2003 Jun 1;101(11):4408-15. Epub 2003 Jan 30.

Vasoactivity of S-nitrosohemoglobin: role of oxygen, heme, and NO oxidation states.

Author information

  • 1Department of Pathology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.

Abstract

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.

PMID:
12560216
[PubMed - indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire
    Loading ...
    Write to the Help Desk