Myoglobinuria
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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]; Associate Editor(s)-in-Chief: Aksiniya Stevasarova, M.D.; Venkata Sivakrishna Kumar Pulivarthi M.B.B.S [2]
Overview
Myoglobinuria is the presence of myoglobin in the urine, usually associated with rhabdomyolysis or muscle destruction.
- Myoglobin (Mb or MB) is an iron- and oxygen-binding protein found in muscles. Myoglobin is present in muscle cells as a reserve of oxygen.In humans, myoglobin is only found in the bloodstream after muscle injury. It is an abnormal finding, and can be diagnostically relevant when found in blood.[1]
- Myoglobin is the primary oxygen-carrying pigment of muscle tissues.[2] High concentrations of myoglobin in muscle cells allow organisms to hold their breath for a longer period of time. Diving mammals such as whales and seals have muscles with particularly high abundance of myoglobin.[1] Myoglobin is found in Type I muscle, Type II A and Type II B, but most texts consider myoglobin not to be found in smooth muscle.
References
- ↑ 1.0 1.1 Nelson DL, Cox MM (2000). Lehninger Principles of Biochemistry (3rd ed.). New York: Worth Publishers. p. 206. ISBN 0-7167-6203-X. (Google books link is the 2008 edition)
- ↑ Ordway GA, Garry DJ (Sep 2004). "Myoglobin: an essential hemoprotein in striated muscle". The Journal of Experimental Biology. 207 (Pt 20): 3441–6. doi:10.1242/jeb.01172. PMID 15339940.
Historical Perspective
Myoglobin was the first protein to have its three-dimensional structure revealed by X-ray crystallography.[1] This achievement was reported in 1958 by John Kendrew and associates.[2] For this discovery, John Kendrew shared the 1962 Nobel Prize in chemistry with Max Perutz.[3] Despite being one of the most studied proteins in biology, its physiological function is not yet conclusively established: mice genetically engineered to lack myoglobin can be viable and fertile but show many cellular and physiological adaptations to overcome the loss. Through observing these changes in myoglobin-deplete mice, it is hypothesised that myoglobin function relates to increased oxygen transport to muscle, oxygen storage and as a scavenger of reactive oxygen species.[4]
References
- ↑ (U.S.) National Science Foundation: Protein Data Bank Chronology (Jan. 21, 2004). Retrieved 3.17.2010
- ↑ Kendrew JC, Bodo G, Dintzis HM, Parrish RG, Wyckoff H, Phillips DC (Mar 1958). "A three-dimensional model of the myoglobin molecule obtained by x-ray analysis". Nature. 181 (4610): 662–6. Bibcode:1958Natur.181..662K. doi:10.1038/181662a0. PMID 13517261.
- ↑ The Nobel Prize in Chemistry 1962
- ↑ Garry DJ, Kanatous SB, Mammen PP (2007). "Molecular insights into the functional role of myoglobin". Advances in Experimental Medicine and Biology. 618: 181–93. doi:10.1007/978-0-387-75434-5_14. PMID 18269197.
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