Intracellular oxygen transport

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R-HSA-8981607
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Homo sapiens
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Globins are heme-containing proteins that reversibly bind molecular oxygen. Humans contain at least 5 types of globins: hemoglobins, myoglobin, cytoglobin, neuroglobin, and androglobin (reviewed in Burmester et al. 2014). Myoglobin, neuroglobin, and cytoglobin are cytosolic globins with similar affinities for oxygen (reviewed in Hankeln et al. 2005). Androglobin is a more distantly related globin of uncertain function that is expressed in testes (Hoogewijs et al. 2012). Myoglobin is predominantly expressed in muscle tissue (reviewed in Helbo et al. 2013), neuroglobin is expressed in neurons, and cytoglobin is expressed in connective tissue fibroblasts and smooth muscle cells (reviewed in Pesce et al. 2002, Hankeln et al. 2004, Ascenzi et al. 2016). Whereas myoglobin contains pentacoordinated heme iron, neuroglobin and cytoglobin contain hexacoordinated heme iron: the iron atom is bound by 4 nitrogen atoms of heme and 2 histidine residues of the globin. Binding by one of the histidines is reversible, which allows the iron atom to bind various ligands such as molecular oxygen, carbon monoxide, and nitric oxide (reviewed in Kakar et al. 2010). Neuroglobin may function in oxygen homeostasis, however the importance of its oxygen-binding activity is unclear (reviewed in Pesce et al. 2002, Hankeln et al. 2005). Cytoglobin may function in nitric oxide metabolism (Thuy et al. 2016, Liu et al. 2017). Globins can also regulate oxygen homeostasis via reactions with nitric oxide (NO), a vasodilator. Oxygenated globins scavenge NO by oxidation while deoxygenated globins can act as a nitrite reductase to produce NO (reviewed in Hendgen-Cotta et al. 2014, Tejero and Gladwin 2014).

Literature References
PubMed ID Title Journal Year
27146058 Absence of cytoglobin promotes multiple organ abnormalities in aged mice

Thuy, le TT, Van Thuy, TT, Matsumoto, Y, Hai, H, Ikura, Y, Yoshizato, K, Kawada, N

Sci Rep 2016
15804831 The cellular and subcellular localization of neuroglobin and cytoglobin -- a clue to their function?

Hankeln, T, Wystub, S, Laufs, T, Schmidt, M, Gerlach, F, Saaler-Reinhardt, S, Reuss, S, Burmester, T

IUBMB Life 2004
15598495 Neuroglobin and cytoglobin in search of their role in the vertebrate globin family

Hankeln, T, Ebner, B, Fuchs, C, Gerlach, F, Haberkamp, M, Laufs, TL, Roesner, A, Schmidt, M, Weich, B, Wystub, S, Saaler-Reinhardt, S, Reuss, S, Bolognesi, M, De Sanctis, D, Marden, MC, Kiger, L, Moens, L, Dewilde, S, Nevo, E, Avivi, A, Weber, RE, Fago, A, Burmester, T

J. Inorg. Biochem. 2005
28393874 Cytoglobin regulates blood pressure and vascular tone through nitric oxide metabolism in the vascular wall

Liu, X, El-Mahdy, MA, Boslett, J, Varadharaj, S, Hemann, C, Abdelghany, TM, Ismail, RS, Little, SC, Zhou, D, Thuy, LT, Kawada, N, Zweier, JL

Nat Commun 2017
24477516 The globin superfamily: functions in nitric oxide formation and decay

Tejero, J, Gladwin, MT

Biol. Chem. 2014
23388387 Expression patterns and adaptive functional diversity of vertebrate myoglobins

Helbo, S, Weber, RE, Fago, A

Biochim. Biophys. Acta 2013
22115833 Androglobin: a chimeric globin in metazoans that is preferentially expressed in Mammalian testes

Hoogewijs, D, Ebner, B, Germani, F, Hoffmann, FG, Fabrizius, A, Moens, L, Burmester, T, Dewilde, S, Storz, JF, Vinogradov, SN, Hankeln, T

Mol. Biol. Evol. 2012
24859377 Myoglobin functions in the heart

Hendgen-Cotta, UB, Kelm, M, Rassaf, T

Free Radic. Biol. Med. 2014
24811692 Function and evolution of vertebrate globins

Burmester, T, Hankeln, T

Acta Physiol (Oxf) 2014
12475928 Neuroglobin and cytoglobin. Fresh blood for the vertebrate globin family

Pesce, A, Bolognesi, M, Bocedi, A, Ascenzi, P, Dewilde, S, Moens, L, Hankeln, T, Burmester, T

EMBO Rep. 2002
20933319 Structure and reactivity of hexacoordinate hemoglobins

Kakar, S, Hoffman, FG, Storz, JF, Fabian, M, Hargrove, MS

Biophys. Chem. 2010
27825818 Neuroglobin: From structure to function in health and disease

Ascenzi, P, di Masi, A, Leboffe, L, Fiocchetti, M, Nuzzo, MT, Brunori, M, Marino, M

Mol. Aspects Med. 2016
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