Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2013 Aug 16;1(1):405-10.
doi: 10.1016/j.redox.2013.08.001.

The emerging roles of somatic globins in cardiovascular redox biology and beyond

Affiliations
Review

The emerging roles of somatic globins in cardiovascular redox biology and beyond

Mizanur M Rahaman et al. Redox Biol. .

Abstract

The vertebrate globins are a group of hemoproteins with the intrinsic capacity to regulate gaseous ligands and redox signaling required for cardiovascular biology. This graphical review will provide a comprehensive synopsis of somatic cardiovascular globins focusing on expression, function and redox signaling - an emerging area in both physiology and disease.

Keywords: Cariovascular; Cytochrome b5 reductase; Cytoglobin; Globin; Hemoglobin; Myoglobin; Neuroglobi; Nitric oxide.

PubMed Disclaimer

Figures

Fig. 1
Fig. 1
Schematic outline of the vertebrate globins in the cardiovascular system highlighting cell-type specific expression, biochemical functions and phylogenetic features.
Fig. 2
Fig. 2
Cell type-specific expression of hemoglobin, myoglobin, cytoglobin and neuroglobin along the vascular tree.
Fig. 3
Fig. 3
Mechanism of Hb α-regulated NO signaling in endothelial cells. Hb α is expressed in small artery and arteriolar endothelial cells and enriched at the myoendothelial junction (lower left hand corner). Nitric oxide, released from eNOS, reacts with oxy-Hb αFe2+ resulting in NO scavenging (dioxygenation reaction) or reacts with Hb αFe3+ resulting in a slow and weak binding NO allowing for diffusion. The cycling of Hb αFe3+ to Hb αFe2+ is controlled by a CytB5 and CytB5R3 dependent mechanism.
Fig. 4
Fig. 4
Known somatic cell types that express hemoglobin, the identified chains, and functions.

References

    1. Bolognesi M., Bordo D., Rizzi M., Tarricone C., Ascenzi P. Nonvertebrate hemoglobins: structural bases for reactivity. Progress in Biophysics and Molecular Biology. 1997;68(1):29–68. - PubMed
    1. Kendrew J.C. Myoglobin and the structure of proteins. Science. 1963;139(3561):1259–1266. - PubMed
    1. Perutz M.F. Regulation of oxygen affinity of hemoglobin: influence of structure of the globin on the heme iron. Annual Review of Biochemistry. 1979;48:327–386. - PubMed
    1. Hardison R.C. A brief history of hemoglobins: plant, animal, protist, and bacteria. Proceedings of the National Academy of Sciences of the United States of America. 1996;93(12):5675–5679. - PMC - PubMed
    1. Reeder B.J. The redox activity of hemoglobins: from physiologic functions to pathologic mechanisms. Antioxidants & Redox Signaling. 2010;13(7):1087–1123. - PubMed

LinkOut - more resources