Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi

Myoglobin (Mb)

  • Niharika Swain
  • Shilpa Patel
  • Rashmi Maruti Hosalkar
Reference work entry
DOI: https://doi.org/10.1007/978-3-319-67199-4_102005

Synonyms

Historical Background

Myoglobin (Mb) is a monomeric, cytoplasmic hemoprotein with rich and varied history, thus becoming an object of renewed interest owing to its role beyond those previously described. In 1987, Mörner first identified and differentiated Mb from hemoglobin (Hb) by their differences in absorption spectra and further termed it as myochrome (Garry and Mammen 2007). Interestingly, it is the first protein upon which a three-dimensional structure was determined. The notation Mb was introduced by Günther, who confirmed the results of Mörner in 1921 (Hendgen-Cotta et al. 2010). The term Mb has been given owing to its functional and structural similarity with Hb. For a long time, it was believed that expression of Mb in vertebrates was restricted to muscle tissue like cardiomyocytes, oxidative skeletal myofibers, and vascular smooth muscle cells and its associated diseases (Hendgen-Cotta et al. 2010). However, recent studies have...

This is a preview of subscription content, log in to check access.

References

  1. Blanchetot A, Wilson V, Wood D, Jeffreys AJ. The seal Mb gene: an unusually long globin gene. Nature. 1983;301(5902):732–4.CrossRefPubMedGoogle Scholar
  2. Brune B. Nitric oxide: NO apoptosis or turning it ON? Cell Death Differ. 2003;10(8):864–9. doi:10.41038/sj.cdd.4401261.CrossRefPubMedGoogle Scholar
  3. Brunori M. Nitric oxide, cytochrome-c oxidase and Mb. Trends Biochem Sci. 2001;26(1):21–3. doi:10.1016/S0968-0004(00)01698-4.CrossRefPubMedGoogle Scholar
  4. Brunori M. Mb strikes back. Protein Sci. 2010;19(2):195–201. doi:10.1002/pro.300.CrossRefPubMedGoogle Scholar
  5. Burmester T, Ebner B, Weich B, Hankeln T. Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues. Mol Biol Evol. 2002;19(4):416–21.CrossRefPubMedGoogle Scholar
  6. Dierks P, van Ooyen A, Cochran MD, Dobkin C, Reiser J, Weissmann C. Three regions upstream from the cap site are required for efficient and accurate transcription of the rabbit beta-globin gene in mouse 3T6 cells. Cell. 1983;32(3):695–706. doi:10.1016/0092-8674(83)90055-7.CrossRefPubMedGoogle Scholar
  7. Flonta SE, Arena S, Pisacane A, Michieli P, Bardelli A. Expression and functional regulation of Mb in epithelial cancers. Am J Pathol. 2009;175(1):201–6. doi:10.2353/ajpath.2009.081124.CrossRefPubMedPubMedCentralGoogle Scholar
  8. Fraser J, de Mello LV, Ward D, Rees HH, Williams DR, Fang Y, et al. Hypoxia-inducible Mb expression in nonmuscle tissues. Proc Natl Acad Sci U S A. 2006;103(8):2977–81. doi:10.1073/pnas.0508270103.CrossRefPubMedPubMedCentralGoogle Scholar
  9. Frauenfelder H, McMahon BH, Austin RH, Chu K, Groves JT. The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of Mb. Proc Natl Acad Sci U S A. 2001;98(5):2370–4. doi:10.1073/pnas.041614298.CrossRefPubMedPubMedCentralGoogle Scholar
  10. Garry DJ, Mammen PP. Molecular insights into the functional role of Mb. Adv Exp Med Biol. 2007;618:181–93. doi:10.1007/978-0-387-75434-5_14.CrossRefPubMedGoogle Scholar
  11. Grosveld GC, de Boer E, Shewmaker CK, Flavell RA. DNA sequences necessary for transcription of the rabbit beta-globin gene in vivo. Nature. 1982;295(5845):120–6. doi:10.1038/295120a0.CrossRefPubMedGoogle Scholar
  12. Helbo S, Weber RE, Fago A. Expression patterns and adaptive functional diversity of vertebrate Mbs. Biochim Biophys Acta. 2013;1834(9):1832–9. doi:10.1016/j.bbapap.2013.01.037.CrossRefPubMedGoogle Scholar
  13. Hendgen-Cotta UB, Flögel U, Kelm M, Rassaf T. Unmasking the Janus face of Mb in health and disease. J Exp Biol. 2010;213(Pt16):2734–40. doi:10.1242/jeb.041178.CrossRefPubMedGoogle Scholar
  14. Jeffreys AJ, Wilson V, Blanchetot A, Weller P, Geurts van Kessel A, Spurr N, Solomon E, Goodfellow P. The human Mb gene: a third dispersed globin locus in the human genome. Nucleic Acids Res. 1984;12(7):3235–43. doi:10.1093/nar/12.7.3235.CrossRefPubMedPubMedCentralGoogle Scholar
  15. Kamga C, Krishnamurthy S, Shiva S. Mb and mitochondria: a relationship bound by oxygen and nitric oxide. Nitric Oxide. 2012;26(4):251–8. doi:10.1016/j.niox.2012.03.005.CrossRefPubMedPubMedCentralGoogle Scholar
  16. Kendrew JC, Bodo G, Dintzis HM, Parrish RG, Wyckoff H, Philips DC. A 3-Dimensional model of the Mb molecule obtained by X-ray analysis. Nature. 1958;181(4610):662–6.CrossRefPubMedGoogle Scholar
  17. Lin PC, Kreutzer U, Jue T. Mb translational diffusion in rat myocardium and its implication on intracellular oxygen transport. J Physiol. 2007;578(Pt2):595–603. doi:10.1113/jphysiol.2006.116061.CrossRefPubMedGoogle Scholar
  18. Michieli P. Hypoxia, angiogenesis and cancer therapy: to breathe or not to breathe? Cell Cycle. 2009;8(20):3291–6. doi:10.4161/cc.8.20.9741.CrossRefPubMedGoogle Scholar
  19. Ordway GA, Garry DJ. Mb: an essential hemoprotein in striated muscle. J Exp Biol. 2004;207(Pt 20):3441–6. doi:10.1242/jeb.01172.CrossRefPubMedGoogle Scholar

Copyright information

© Springer International Publishing AG 2018

Authors and Affiliations

  • Niharika Swain
    • 1
  • Shilpa Patel
    • 1
  • Rashmi Maruti Hosalkar
    • 2
    • 3
  1. 1.MGM Dental College and HospitalNavi MumbaiIndia
  2. 2.Indian Association of Oral and Maxillofacial PathologistsMumbaiIndia
  3. 3.Maharashtra State Dental CouncilMumbaiIndia