Myoglobin

From Free net encyclopedia

{{Protbox start

| Name=Myoglobin
| Photo=Myoglobin.png
| Caption=Model of helical domains in myoglobin.
| Gene = HUGO code: MB
| Structure = molecular structure
| Review = role in human pathologies,
 gene knockout}}

{{Protbox function

| Type =Hemoprotein
| Functions = oxygen storage/transport
| Domains = globin
| Diseases= kidney disease, vasospasm}}

{{Protbox location

| Taxa = many metazoan phyla,
 Archaea?,
 protozoan/eubacterial?
| Cells = muscle cells
| Location = cytoplasm
}}

{{Protbox other

| Mods = glycation?,
phosphorylation in whales?
| Names = myoglobin-like proteins in microorganisms
| Interactions = oxygen,
heme,
carbon monoxide,
nitric oxide
| Pages = X-ray crystallography,
Secondary structure}}

Template:Protbox finish

Myoglobin is a single-chain protein of 153 amino acids, containing a heme (iron-containing porphyrin) group in the center. With a molecular weight of 16,700 Daltons, it is the primary oxygen-carrying pigment of muscle tissuesTemplate:Ref. Unlike the blood-borne hemoglobin, to which it is structurally relatedTemplate:Ref, this protein does not exhibit cooperative binding of oxygen. Instead, the binding of oxygen by myoglobin is unaffected by the oxygen pressure in the surrounding tissue. In 1957, John Kendrew and associates successfully determined the structure of myoglobin by high-resolution X-ray crystallography Template:Ref. Image:Myoglobindiffraction.png For this discovery, John Kendrew shared the 1962 Nobel Prize in chemistry with Max Perutz Template:Ref.

1 Role in disease
2 References
3 See also
4 External links

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Role in disease

Myoglobin has been implicated as a cause of acute renal failure following damage to muscle tissue (e.g. rhabdomyolysis, severe crush trauma, malignant hyperthermia, status epilepticus and neuroleptic malignant syndrome), due to its toxicity to renal tubular epitheliumTemplate:Ref.

Myoglobin is a sensitive marker for muscle injury, making it a potential marker for myocardial infarction in patients with chest pain Template:Ref. Its specificity and the cost of the analysis has prevented its widespread use.

During muscle death due to infarction, myoglobin is released, which is toxic to the kidneys. If it is misdiagnosed, it can cause much worse conditions, such as cardiac arrest.

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References

Template:Note {{cite journal

| title = Myoglobin: an essential hemoprotein in striated muscle
| author = George A. Ordway and Daniel J. Garry
| journal = Journal of Experimental Biology
| year = 2004
| volume = 207
| pages = pages 3441–3446
| id = Template:Doi
}}

Template:Note {{cite book

| chapterurl = http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Search&db=books&doptcmdl=GenBookHL&term=myoglobin+AND+mcb%5Bbook%5D+AND+105134%5Buid%5D&rid=mcb.figgrp.540
| chapter = Evolutionary tree showing the globin protein family members myoglobin and hemoglobin
| title = Molecular Cell Biology
| edition = Fourth Edition
| author = Harvey Lodish, Arnold Berk, Lawrence S. Zipursky, Paul Matsudaira, David Baltimore and James Darnell
| year = 2000
| publisher = W. H. FREEMAN
| id = ISBN 0-7167-3136-3
}}

Template:Note Oxy-myoglobin at 0.1 nm resolution: PDB 1A6M. Sperm whale myoglobin at 0.17 nm resolution: PDB 1VXH.
Template:Note The Nobel Prize in Chemistry 1962
Template:Note {{cite journal

| title = Myoglobin clearance by super high-flux hemofiltration in a case of severe rhabdomyolysis: a case report
| author = Toshio Naka, Daryl Jones, Ian Baldwin, Nigel Fealy, Samantha Bates, Hermann Goehl, Stanislao Morgera, Hans H. Neumayer and Rinaldo Bellomo
| journal = Critical Care
| year = 2005
| volume = 9
| pages = pages R90–R95
| id = Template:Doi
}}

Template:Note {{cite journal

| title = Diagnostic utility of new immunoassays for the cardiac markers cTnI, myoglobin and CK-MB mass
| author = M. Weber, M. Rau, K. Madlener, A. Elsaesser, D. Bankovic, V. Mitrovic and C. Hamm
| journal = Clinical Biochemistry
| year = 2005
| volume = 38
| pages = pages 1027–1030
| id = Template:Entrez Pubmed 
}}

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