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Annales de Biologie Clinique Apr 2018The clinical biologist plays a role as a consultant for the relevant use of biological examination. Advisory activities of the medical laboratory may help physician in... (Review)
Review
The clinical biologist plays a role as a consultant for the relevant use of biological examination. Advisory activities of the medical laboratory may help physician in diagnosis or therapeutic algorithm, avoiding redundant ordering or useless tests. In this context, we performed a review of literature about the clinically interest of myoglobin assays. The indications of myoglobin's assays appear fairly limited. It is no longer mentioned in the European guidelines for the management of acute coronary syndromes in patients presenting without persistent ST-segment elevation. In patients with rhabdomyolysis myoglobin is neither a diagnostic nor a prognostic criterion. Its interest in predicting the occurrence of acute renal failure is also discussed. The most recent clinico-biological score (such as the McMahon score) do not integrate it. In this context, we decided to stop performing myoglobin assay.
Topics: Acute Kidney Injury; Biomarkers; Diagnostic Tests, Routine; Humans; Myoglobin; Predictive Value of Tests; Rhabdomyolysis
PubMed: 29623882
DOI: 10.1684/abc.2018.1326 -
Cellular and Molecular Life Sciences :... Sep 1998The distribution, physiological function, amino acid sequence and gene structure of myoglobin and myoglobin-like proteins from various taxa are summarized, and their... (Review)
Review
The distribution, physiological function, amino acid sequence and gene structure of myoglobin and myoglobin-like proteins from various taxa are summarized, and their evolution is discussed. Although it has long been thought that all haemoglobins and myoglobins have evolved from a common ancestral gene, the knowledge presently accumulated about the structures of these proteins suggests that there may be three distinct origins: a 'universal globin', a 'compact globin' and an 'IDO-like globin'.
Topics: Amino Acid Sequence; Animals; Eukaryotic Cells; Evolution, Molecular; Hemoglobins; Humans; Invertebrates; Models, Molecular; Molecular Sequence Data; Myoglobin; Oxygen; Phylogeny; Prokaryotic Cells; Protein Conformation; Sequence Homology, Amino Acid; Vertebrates
PubMed: 9791540
DOI: 10.1007/s000180050227 -
The Journal of Experimental Biology Sep 2004Myoglobin is a cytoplasmic hemoprotein, expressed solely in cardiac myocytes and oxidative skeletal muscle fibers, that reversibly binds O2 by its heme residue, a... (Review)
Review
Myoglobin is a cytoplasmic hemoprotein, expressed solely in cardiac myocytes and oxidative skeletal muscle fibers, that reversibly binds O2 by its heme residue, a porphyrin ring:iron ion complex. Since the initial discovery of its structure over 40 years ago, wide-ranging work by many investigators has added importantly to our understanding of its function and regulation. Functionally, myoglobin is well accepted as an O2-storage protein in muscle, capable of releasing O2 during periods of hypoxia or anoxia. Myoglobin is also thought to buffer intracellular O2 concentration when muscle activity increases and to facilitate intracellular O2 diffusion by providing a parallel path that augments simple diffusion of dissolved O2. The use of gene targeting and other molecular biological techniques has revealed important new insights into the developmental and environmental regulation of myoglobin and provided additional functions for this hemoprotein such as scavenging nitric oxide and reactive O2 species. These recent findings, coupled with additional emerging technologies and the discovery of other tissue globins, provide a framework for addressing new questions about myoglobin and readdressing old ones.
Topics: Animals; Binding Sites; Muscle, Skeletal; Myoglobin; Nitric Oxide; Oxygen; Protein Conformation; Reactive Oxygen Species
PubMed: 15339940
DOI: 10.1242/jeb.01172 -
CRC Critical Reviews in Clinical... 1978Myoglobin is the oxygen-binding protein characteristic of skeletal and cardiac muscle. With muscle disease or dysfunction, myoglobin may enter the circulation, and after... (Review)
Review
Myoglobin is the oxygen-binding protein characteristic of skeletal and cardiac muscle. With muscle disease or dysfunction, myoglobin may enter the circulation, and after renal clearance, it may also appear in the urine. Therefore, the presence of myoglobinemia and myoglobinuria may serve as indicators of the presence and severity of muscle disease. With newly developed methods of detection, myoglobinemia and myoglobinuria are now recognized as complications of trauma, ischemia, surgery, states of exertion and stress, metabolic abnormalities, inherited enzyme disorders, toxin and drug actions, and inflammatory states. Infarction of the heart muscle also can be detected by myoglobin assay. Persistent myoglobinuric states may be complicated by renal failure and electrolyte imbalance. The diagnosis of myoglobinemia and myoglobinuria can be now confirmed with the use of immunoassay techniques. Although not yet widely available, they offer the possibility of the specificity and sensitivity needed for clinical use.
Topics: Humans; Muscular Diseases; Myocardial Infarction; Myoglobin; Myoglobinuria; Radioimmunoassay
PubMed: 401372
DOI: 10.3109/10408367809150922 -
Biophysical Chemistry Aug 2000Conformational fluctuations have been invoked to explain the observation that the diffusion of small ligands through a protein is a global phenomenon, as suggested (for... (Review)
Review
Conformational fluctuations have been invoked to explain the observation that the diffusion of small ligands through a protein is a global phenomenon, as suggested (for example) by the oxygen induced fluorescence quenching of buried tryptophans. In enzymes processing large substrates, a channel to the catalytic site is often seen in the crystal structure; on the other hand in small globular proteins, it is not known if the cavities identified in the interior space are important in controlling their function by defining specific pathways in the diffusion to the active site. This point is addressed in this paper, which reports some relevant results obtained on myoglobin, the hydrogen atom of molecular biology. Protein conformational relaxations have been extensively investigated with myoglobin because the photosensivity of the adduct with CO, O2 and NO allows us to follow events related to the migration of the ligand through the matrix. Results obtained by laser photolysis, molecular dynamics simulations, X-ray diffraction of intermediate states of wt type and mutant myoglobins are briefly summarized. Crystallographic data on the photochemical intermediate of a new triple mutant of sperm whale myoglobin (Mb-YQR) show, for the first time, the photolyzed CO* sitting in one of the Xe-binding cavities, removed from the heme group. These results support the viewpoint that pre-existing 'packing defects' in the protein interior play a major role in controlling the dynamics of ligand binding, including oxygen, and thereby acquire a survival value.
Topics: Animals; Binding Sites; Crystallography, X-Ray; Ligands; Models, Molecular; Mutation; Myoglobin; Oxygen; Protein Binding; Protein Conformation
PubMed: 11026686
DOI: 10.1016/s0301-4622(00)00142-3 -
Journal of Inorganic Biochemistry Aug 2022Globins play a key role in regulating nitric oxide (NO) levels in all forms of life. Five key reactions of NO with mammalian muscle myoglobin (Mb) and red blood cell... (Review)
Review
Globins play a key role in regulating nitric oxide (NO) levels in all forms of life. Five key reactions of NO with mammalian muscle myoglobin (Mb) and red blood cell hemoglobin (Hb) have been examined: (1) reversible NO binding to Fe(II) forms; (2) reversible NO binding to Fe(III) forms; (3) NO dioxygenation by Fe(II)O complexes; (4) autoxidation of Fe(II)NO complexes in the presence of O; and (5) autoreduction of Fe(III)NO complexes. NO reacts rapidly and almost irreversibly with deoxyMb(FeII) in the absence of O, whereas it reacts much more slowly and weakly with metMb(FeIII). The reaction of NO with Mb(FeII)O is very rapid and results in oxidation of the iron atom and dioxygenation of NO to nitrate. Autoxidation of Mb(FeII)NO in air is determined by the slow rate of NO dissociation from the Fe(II)NO complex, which is followed by rapid O binding to the newly formed deoxyMb(FeII) and dioxygenation of the displaced NO to generate NO and metMb(FeIII). MetMb(FeIII)NO autoreduces slowly by addition of a hydroxide ion to bound NO to generate nitrous acid and reduced deoxyMb(FeII), which immediately binds another NO to generate Mb(FeII)NO as the final product. The reverse of this process involves nitrite reduction to NO by deoxyMb(FeII), which can occur on physiological time scales when the globin concentration is in the millimolar range. The relevance of these processes to the regulation of NO metabolism by hemoglobins and myoglobins in humans and other organisms is discussed.
Topics: Animals; Ferric Compounds; Globins; Hemoglobins; Humans; Mammals; Myoglobin; Nitric Oxide; Nitrites; Oxidation-Reduction
PubMed: 35599166
DOI: 10.1016/j.jinorgbio.2022.111839 -
Comparative Biochemistry and... Oct 1998The distribution, isolation, spectral and oxygen-binding properties, stability of ferrous state (autoxidation), amino acid sequence and gene structure of indoleamine... (Comparative Study)
Comparative Study Review
The distribution, isolation, spectral and oxygen-binding properties, stability of ferrous state (autoxidation), amino acid sequence and gene structure of indoleamine 2,3-dioxygenase (IDO)-like myoglobins are summarized, and their evolution is discussed. Although it has long been thought that all hemoglobins and myoglobins have evolved from a common ancestral gene encoding a 14-16 kDa polypeptide, the discovery of IDO-like myoglobin from several gastropod molluscs clearly indicates that there was an alternative pathway for myoglobin evolution.
Topics: Amino Acid Sequence; Animals; Base Sequence; DNA, Complementary; Evolution, Molecular; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Molecular Sequence Data; Mollusca; Myoglobin; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Tryptophan; Tryptophan Oxygenase
PubMed: 9972288
DOI: 10.1016/s0305-0491(98)10086-x -
Trends in Cardiovascular Medicine Apr 2003Myoglobin (Mb) is an intensely studied hemoprotein that is restricted mainly to the heart and oxidative myofibers in skeletal muscle. Previous physiologic and... (Review)
Review
Myoglobin (Mb) is an intensely studied hemoprotein that is restricted mainly to the heart and oxidative myofibers in skeletal muscle. Previous physiologic and pharmacologic studies have supported a role for Mb in facilitated oxygen transport or as an oxygen reservoir in striated muscle. Transgenic and gene disruption technologies have been utilized to produce mice that lack Mb. Studies utilizing these transgenic mouse models support the notion that Mb may have multiple, diverse functions in the heart. Future studies using these emerging technologies will further enhance the understanding of the role of Mb and other hemoproteins in cardiovascular biology.
Topics: Animals; Heart; Humans; Myoglobin
PubMed: 12691675
DOI: 10.1016/s1050-1738(02)00256-6 -
Journal of Agricultural and Food... Nov 2023Myoglobin is the main factor responsible for muscle pigmentation in tuna; muscle color depends upon changes in the oxidative state of myoglobin. The tuna industry has... (Review)
Review
Myoglobin is the main factor responsible for muscle pigmentation in tuna; muscle color depends upon changes in the oxidative state of myoglobin. The tuna industry has reported muscle greening after thermal treatment involving metmyoglobin (MetMb), trimethylamine oxide (TMAO), and free cysteine (Cys). It has been proposed that this pigmentation change is due to a disulfide bond between a unique cysteine residue (Cys10) found in tuna MetMb and free Cys. However, no evidence has been given to confirm that this reaction occurs. In this review, new findings about the mechanism of this greening reaction are discussed, showing evidence of how free radicals produced from Cys oxidation under thermal treatment participate in the greening of tuna and horse muscle during thermal treatment. In addition, the reaction conditions are compared to other green myoglobins, such as sulfmyoglobin, verdomyoglobin, and cholemyoglobin.
Topics: Animals; Horses; Myoglobin; Cysteine; Metmyoglobin; Oxidation-Reduction; Muscles
PubMed: 37943570
DOI: 10.1021/acs.jafc.3c02109 -
Science (New York, N.Y.) Jun 1992Myoglobin was found in the nitrogen-fixing cyanobacterium Nostoc commune. This cyanobacterial myoglobin, referred to as cyanoglobin, was shown to be a soluble...
Myoglobin was found in the nitrogen-fixing cyanobacterium Nostoc commune. This cyanobacterial myoglobin, referred to as cyanoglobin, was shown to be a soluble hemoprotein of 12.5 kilodaltons with an amino acid sequence that is related to that of myoglobins from two lower eukaryotes, the ciliated protozoa Paramecium caudatum and Tetrahymena pyriformis. Cyanoglobin is encoded by the glbN gene, which is positioned between nifU and nifH-two genes essential for nitrogen fixation-in the genome of Nostoc. Cyanoglobin was detected in Nostoc cells only when they were starved for nitrogen and incubated microaerobically.
Topics: Amino Acid Sequence; Chromosome Mapping; Cloning, Molecular; Cyanobacteria; Electrophoresis, Polyacrylamide Gel; Molecular Sequence Data; Myoglobin; Polymerase Chain Reaction; Sequence Homology, Nucleic Acid
PubMed: 1609281
DOI: 10.1126/science.256.5064.1690