Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • News & Views
  • Published:

Hemoglobin as a chariot for NO bioactivity

Nature Medicine volume 8, pages 657–658 (2002)Cite this article

Nitric oxide (NO) is a potent vasodilator that is produced in endothelial cells and has been assumed to act exclusively at its site of synthesis. New evidence suggests that red blood cells distribute NO bioactivity, matching blood flow to tissue oxygen demands and endowing NO with features of a hormone (pages 711–717).

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Figure 1: McMahon et al.

References

  1. Muirhead, H. & Perutz, M.F. Structure of hemoglobin. A three-dimensional Fourier synthesis of reduced haemoglobin at 5.5 A resolution. Nature 199, 633–639 (1963).

    Article  CAS  Google Scholar 

  2. McMahon, T.J. et al. Nitric oxide in the human respiratory cycle. Nature Med. 8, 711–717 (2002).

    Article  CAS  Google Scholar 

  3. Perutz, M.F. Stereochemistry of cooperative effects in haemoglobin. Nature 228, 726–739 (1970).

    Article  CAS  Google Scholar 

  4. Jia, L. et al. S-nitrosohemoglobin: A dynamic activity of blood involved in vascular control. Nature 380, 221–226 (1996).

    Article  CAS  Google Scholar 

  5. Gow, A.J. et al. The oxyhemoglobin reaction of nitric oxide. Proc. Natl. Acad. Sci. USA 96, 9027–9032 (1999).

    Article  CAS  Google Scholar 

  6. Pawlowski, J.R. et al. Export by red blood cells of nitric oxide bioactivity. Nature 409, 622–626 (2001).

    Article  Google Scholar 

  7. Chan, N.L. et al. Crystal structure of the S-nitroso form of liganded human hemoglobin. Biochemistry 37, 16459–16464 (1998).

    Article  CAS  Google Scholar 

  8. Liao, J. et al. Intravascular flow decreases erythrocyte consumption of nitric oxide. Proc. Natl. Acad. Sci. USA 96, 8757–8761 (1999).

    Article  CAS  Google Scholar 

  9. Vaughn, M.W. et al. Erythrocytes possess an intrinsic barrier to nitric oxide consumption. J. Biol. Chem. 275, 2342–2348 (2000).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Weill Medical College of Cornell University Department of Pharmacology, New York, New York, USA

    Paul Lane & Steven Gross

Authors
  1. Paul Lane
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Steven Gross
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Lane, P., Gross, S. Hemoglobin as a chariot for NO bioactivity. Nat Med 8, 657–658 (2002). https://doi.org/10.1038/nm0702-657

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1038/nm0702-657

This article is cited by

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing