MB

Official Full Name

myoglobin

Organism

Homo sapiens

Gene ID

4151

Background

This gene encodes a member of the globin superfamily and is predominantly expressed in skeletal and cardiac muscles. The encoded protein forms a monomeric globular haemoprotein that is primarily responsible for the storage and facilitated transfer of oxygen from the cell membrane to the mitochondria. This protein also plays a role in regulating physiological levels of nitric oxide. Multiple transcript variants encoding distinct isoforms exist for this gene. [provided by RefSeq, May 2020]

Synonyms

MYOSB; PVALB

Cat.No.	Product Name	Price
CSC-DC009265	Panoply™ Human MB Knockdown Stable Cell Line	Inquiry
CSC-SC009265	Panoply™ Human MB Over-expressing Stable Cell Line	Inquiry

Cat.No.	Product Name	Price
LV17861L	human MB (NM_203378) lentivirus particles	Inquiry

Cat.No.	Product Name	Price
SHH338727	shRNA set against Rat MB (NM_001035007.1)	Inquiry
SHR154512	shRNA set against Human MB(NM_005368.2)	Inquiry
SHW002970	shRNA set against Chicken MB (NM_001167752)	Inquiry
SHW016750	shRNA set against Danio rerio MB (NM_200586)	Inquiry

Cat.No.	Product Name	Price
MiUTR3H-01477	MB miRNA 3'UTR clone	Inquiry
CDCB178225	Danio rerio MB ORF Clone (NM_200586)	Inquiry
MiUTR1R-03709	MB miRNA 3'UTR clone	Inquiry
MiUTR1H-06127	MB miRNA 3'UTR clone	Inquiry
CDFR011696	Rat Mb cDNA Clone(NM_021588.2)	Inquiry
CDFH011141	Human MB cDNA Clone(NM_005368.2)	Inquiry
CDFG013499	Human MB cDNA Clone(NM_203378.1)	Inquiry
CDFG013497	Human MB cDNA Clone(NM_203378.1)	Inquiry
CDFG013495	Human MB cDNA Clone(NM_203377.1)	Inquiry
MiUTR3H-01476	MB miRNA 3'UTR clone	Inquiry
CDCS412223	Human MB ORF Clone (BC018001)	Inquiry
CDCS412222	Human MB ORF Clone (BC014547)	Inquiry
CDCR327350	Human MB ORF Clone(NM_203378.1)	Inquiry
CDCR327348	Human MB ORF Clone(NM_203377.1)	Inquiry
CDCR290321	Human MB ORF Clone(NM_005368.2)	Inquiry
CDCR252077	Mouse Mb ORF Clone(NM_013593.3)	Inquiry
CDCR240225	Mouse Mb ORF Clone(NM_001164048.1)	Inquiry
CDCR240224	Mouse Mb ORF Clone(NM_001164047.1)	Inquiry
CDCB186983	Rabbit MB ORF clone (XM_008257090.1)	Inquiry
CDCR378743	Rat Mb ORF Clone(NM_021588.2)	Inquiry
CDCB164445	Chicken MB ORF Clone (NM_001167752)	Inquiry

Detailed Information

Myoglobin (MB) is an important intracellular pigment protein in mammalian type I, type II A skeletal muscle and myocardial tissue cytoplasm. MB (Mr17600) consists of a 153 amino acid residue consisting of a multi-peptide chain and a prosthetic heme. MB includes a non-helical region with 5 amino acid residues at the N-terminus, 5 amino acid residues at the C-terminus, and amino acid residues Pro, Ile, Ser, Thr, Asn, etc. at the inflection point. The polar amino acid is distributed on the surface of the molecule. Moreover, a pocket-shaped cavity exists inside, and hemoglobin is present in the cavity. The binding of the hydrophobic gap contained in the folding process to heme is an important step in obtaining its biological activity.

MB function

As an important constitutive protein in muscle, MB has been widely accepted for its oxygen storage function. Especially in aquatic mammals and bird muscles, MB can provide oxygen for muscle contraction during long-term respiratory pauses. When diving, animals can't rely on breathing to meet the oxygen demand. The oxygen stored in the MB can be dissociated to maintain the oxygen demand of muscle contraction. In different types of muscle tissue, the MB concentration in the muscles with higher oxygen consumption is also higher, and the MB concentration in the muscles of the long-term sustained contraction is the highest. These all prove the oxygen storage function of MB.

Studies have shown that MB, as a nitrite reductase, plays an extremely important role in regulating intracellular NO levels and mitochondrial respiration. The lack of MB not only increases impaired myocardial function, but also increases the risk of endogenous or exogenous oxidative damage. The results suggest that MB may be an important factor in influencing redox reactions and protecting the heart from oxidative damage during myocardial metabolism. In patients with pulmonary embolism, myoglobin can be a powerful early warning indicator for fatal pulmonary embolism. By controlling the homeostasis of nitric oxide, it has protective effects on myocardial hypoxia and myocardial ischemia-reperfusion injury.

Figure 1. Myoglobin’s role as an oxygen (O2) sensor.( Hendgen-Cotta, et al, 2014)

In an in vitro solution, the presence of MB accelerates the rate of diffusion of oxygen in the solution. The high affinity of MB for O2 gives MB the ability to act as an oxygen transporter relative to the very low solubility of free oxygen in solution and plays a role in promoting oxygen transport. By measuring the oxygen affinity of terrestrial and terrestrial birds and mammalian MB, the researchers found that MB, which requires long-term diving, showed a higher oxygen affinity than terrestrial birds and mammals. Some researchers have used simulation methods to map 3D images of oxygen and MB combined with their internal migration.

Relationship between MB and myocardial infarction

MB is a small molecule protein found in the cytoplasm. It is released from the cell into the blood as soon as the myocardial infarction occurs, so it can be used for early diagnosis of myocardial infarction. Multiple factor analysis has shown that MB is more predictive of diagnosis than troponin, and MB maintains the best independent predictive mortality rate for myocardial infarction. Studies have shown that MB is an independent predictor of mortality in patients over 6 months. The researchers found that MB is the only marker used to diagnose the hyperacute phase of acute myocardial infarction. Although MB has a high predictive ability to predict death, the ability to predict reinfarction is low.

References:

Silverstein, T. P. , Kirk, S. R. , Meyer, S. C. , & Holman, M. F. . (2015). Myoglobin structure and function: a multiweek biochemistry laboratory project. Biochemistry and Molecular Biology Education, 43(3), 181-188.
Hendgen-Cotta, U. B. , Kelm, M. , & Rassaf, T. . (2014). Myoglobin functions in the heart. Free Radical Biology and Medicine, 73, 252-259.
Schwarze, K. , Campbell, K. L. , Hankeln, T. , Storz, J. F. , Hoffmann, F. G. , & Burmester, T. . (2014). The globin gene repertoire of lampreys: convergent evolution of hemoglobin and myoglobin in jawed and jawless vertebrates. Molecular Biology & Evolution, 31(10), 2708-2721.

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