Biochemistry, Myoglobin (2024)

Introduction

Myoglobin is a protein mainly in the striped muscles of vertebrates.MB is the gene that codes for myoglobin in people.It as an oxygen storage protein in muscles.A role in the detoxification of reactive types of oxygen.Myoglobin is the reason for the red color of the muscle of most vertebrates.[1][2]

Fundamentals

Myoglobin is one of the members of the Globin super family, which also includes hemoglobin.In the different bond to oxygen.Myoglobin does not -in contrast to hemoglobin, which binds to oxygen cooperative as a result of its tetramer character.For his cooperative a higher affinity for oxygen than hemoglobin.. Myoglobin is also executed in much lower concentrations in smooth muscles, endothelial and even tumor cells.[1][2]

Matter of concern

The role of myoglobin as a marker of a illness -reduced disease.[3]

Cellulært -Niveau

Myoglobin occurs in the highest concentration in the striped muscles of vertebrates.[2]

The expression of the MB gene is also reported in various tumor cell lines such as breast carcinoma, colon carcinoma, acute leukemia, dessmoplastic small round cell tumors and non-small-lung cancer.[4]

Molecular level

Myoglobin is a single polypeptide chain of 154 amino acids.Ion interacts with six different ligands, one of which acts as the binding site of oxygen.[1]

Serve

The primary function of myoglobin is to deliver oxygen to the muscle.And like an oxygen reservoir muscles.[1]

Mechanism

Myoglobin contains an Fe (II) Kation bound by a heme group, giving it the option to bind to oxygen can.Oxygen can bind to the Hemreest of Myoglobin because of the interaction of the IJzen ions with six competition.Common plan with the iron., such as Co, Nitriet and Azidmolecules.For example, Co binds strongly to myoglobin, just like with hemoglobin that forms carboxymyoglobin.[1]

In its reduced form, Fe (II), myoglobin can be bound by oxygen (oxymyoglobin) or not (deoxymyoglobin).[5]This binding is the reason why the oxygen saturation curve of myoglobin is hyperbolic and is characteristic of the normal Michaelis-Mentenszymkinetics.

To test

Myoglobin test can occur in the blood or urine.

With regard to rabdomyolysis, myoglobin tests in the urine can result from the combination of urine flour and microscopy.Rhabdomyolyse.urin Myoglobin is also not used routinely.[6]A urine test can reliably predict the absence of myoglobinuria.[7]

Moreover, myoglobin is a sensitive marker for acute myocardial infarction.After the start of the event.Camers, the use of this biomarker for myocardial infarction must be in combination with other criteria in favor of the diagnosis of a heart attack.[8]

Pudding

Myoglobin Knock Models are made to try to understand his functions more clearly., showed cellular and molecular adaptive reactions to the lack of the lack of myoglobin.This included a higher capillary density in the heart to improve the oxygen supply.[9]

Myoglobin also plays a role in the pathophysiology of rabdomyolysis.The cell.The other mechanism is due to oxidation injury.[10]

Clinical

Myoglobin's most important clinical significance comes with his association with muscle damage.Occasionally it correlates with rabdomyolysis and myocardial infarction.Causing damage.Alcohol consumption.Attacks can also cause rabdomyolysis.[11]Excessive myoglobin excretion in the urine can cause the color to be red or brown.[10]

Myoglobin can also be detected in the urine as a result of hereditary myopathies.[12]

Myoglobin can be detected in the serum after acute myocardial infarction.However, as described above, it is not in the guidelines of the diagnosis.[8]

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References

1.: Ordway GA, Garry dj.myoglobin: an essential hemoprotein in striped muscles.J Exp Biol.2004 Sep;207(PT 20): 3441-6.[[PubMed: 15339940]
2.: Koch J, Lüdemann J, Spies R, Last M, Amemiya CT, Burmester T. Unusual diversity of myoglobings in the pulmonary fishing.Mol Biol Evol.2016 dec;33(12): 3033-3041.[[PubMed: 27512111]
3.: Servonnet A, Dubost C, Martin G, Lofrer B, Fontan E Franca F, Delacour H. [Myoglobin: Stadig in 2017?].].Ann BioL Clin (Paris).2018 01. april;76(2): 137-141.[[PubMed: 29623882]
4.: Bicker A, Dietrich D, Gleixner E, Kristiansen G, Gorr Ta, Hankeln T. Extensive transcriptional complexity during hypoxia-regulated expression of myoglobin gene in cancer.Hum mol genet.January 15, 2014;23(2): 479-90.[[PubMed: 24026678]
5.: Silverstein TP, Kirk SR, Meyer SC, Holman Kl.myoglobin Structure and Function: a Mulweek Biokemi Labory project.Biochem Mol Biol Educ.2015 May-June;43(3): 181-8.[[PubMed: 25726810]
6.: Sauret JM, Marinides G, Wang Gk.Rhabdomyolyse.Is a general practitioner.2002 March.01;65(5): 907-12.[[PubMed: 11898964]
7.: Schifman RB, Luevano Dr.Value and use of urine examination to myoglobinuri.Arch Pathol Lab Med.2019 nov;143(11): 1378-1381.[[PubMed: 31116043]
8.: Aydin S, Ugur K, Aydin S, Sahin I, Yardim M. Biomarkers in acute myocardial infarction: current perspectives.VASC Health Risk Manag.2019;15: 1-10.[[PMC Gratis Artikel: PMC6340361] [PubMed: 30697054]
9.: Meeson AP, Radford N, Shelton JM, Mammen PP, Dimaio JM, Hutcheson K, King Y, Elterman J, Williams RS, Garry DJ.Adaptive mechanisms that retain heart function in mice without myoglobin.Bypass.2001 13. april;88(7): 713-20.[[PubMed: 11304494]
10.: Zimmerman JL, Shen MC.RHABDOMYOLYSE.Chest.2013 SEP;144(3): 1058-1065.[[PubMed: 24008958]
11.: Zutt R, van der Kooi AJ, Linthorst Ge, Wanders RJ, De Visser M. Rhabdomyolysis: Review of the Literature.Neuromuscul disorder.2014 augustus;24(8): 651-9.[[PubMed: 24946698]
12.: Boat E, Emmanuele V, Dimauro SB.Metabolic Myoglobinuri.Curr Neurol Neurosci Rep.2015 October;15(10): 69.[[PubMed: 26319173]

: Revelation:Trey Vanek does not explain a relevant financial relationship with unjustified companies.
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