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Expression levels of myoglobin in muscle and non-muscle tissues of rainbow trout Oncorhynchus mykiss
Study identifies a recurrent c.292C>T (p.His98Tyr) substitution in MB in fourteen members of six European families suffering from an autosomal dominant progressive myopathy with highly characteristic sarcoplasmic inclusions in skeletal and cardiac muscle. Myoglobinopathy manifests in adulthood with proximal and axial weakness that progresses to involve distal muscles and causes respiratory and cardiac failure.
The results showed that the MI-based bio-sensing system had high selectivity and sensitivity for detection of Cardiac biomarkers . Compared with the control region, ultrasensitive detections of CRP and Mb were accomplished with the detection limits of 1.0 pg/mL and 0.1 pg/mL, respectively.
Report morphology of myoglobin casts in renal biopsies with acute kidney injury.
Myoglobin is associated with larger hematoma volume and growth after adjusting potential confounding factors in intracerebral hemorrhage.
we found that the A79G polymorphism of the MB gene plays an important role in influencing the development of exercise-induced skeletal muscle damage.
Electroanalysis of myoglobin as a marker of acute myocardial infarction by means of screenprinted electrodes modified with multiwalled carbon nanotubes and polymeric artificial antibodies is developed. Plastic antibodies to myoglobin (molecularly imprinted polymers, MIPs) based on o-phenylenediamine were produced by electropolymerization. Molecular imprinting technology in biosensor analysis was used.
In the absence of Mb, the Y-shape structure remains intact. So, a weak electrochemical signal is observed. Upon addition of target, the DApt leave the CS and bind to Mb, leading to disassembly of Y-shape structure and following the addition of Exo I, a strong electrochemical signal could be recorded.
analysis of myoglobin gene regulatory networks in breast and prostate cancer
Data show that with the myoglobin (MYO) monoclonal antibody of high specificity and affinity, a one-step sandwich ELISA for detecting MYO has been established successfully, which provides a basis for the development of domestic ELISA kit.
Misfolding and amyloid aggregation of apomyoglobin.
A non-ischemic serum myoglobin release is rare, but could be associated in subgroups of patients.
Data show that chimeric neuroglobin and myoglobin were generated by swapping a regulatory segment.
Findings indicate that myoglobin (Mb) and neuroglobin (Ngb) can be expressed in nonmuscle and non-neural contexts.
Analogous to breast cancer, MB expression in prostate cancer is associated with steroid hormone signaling and markers of hypoxia
the novel cancer-associated MB splice variants exhibited increased expression in tumor cells subjected to experimental hypoxia; the novel gene regulatory mechanisms unveiled in this study support the idea of a non-canonical role of MB during carcinogenesis
Blood myoglobin could serve as a valuable early predictor and marker of rhabdomyolysis and acute myoglobinuric kidney injury
High myoglobin expression is associated with renal cell carcinoma.
Our LFIA performance was additionally compared with electrochemiluminescence immunoassay (ECLI) detection for simultaneous determination of hs-cTnI and myoglobin in patients with suggestive of acute myocardial infarction .
Hydrophobic effect drives oxygen uptake in myoglobin via histidine E7.
MD simulations supported NMR results indicating interesting structural/dynamical differences in the average volume and occurrence of the main cavities lining Mb prosthetic group.
The authors here unravel a novel role of cardiac myoglobin in governing fatty acid metabolism to ensure the physiological energy production through beta-oxidation, preventing myocardial lipid accumulation and preserving cardiac functions.
Inhibition of mammalian target of rapamycin (mTOR) activation using rapamycin restored Mb mRNA expression to control levels. Lipid supplementation had no effect on Mb gene expression. Thus, IGF-1-induced anabolic signaling can be a strategy to improve muscle size under mild hypoxia, but lowers Mb gene expression
Myoglobin overexpression inhibits reperfusion in the ischemic mouse hindlimb through impaired angiogenesis but not arteriogenesis
Chronic exercise downregulates myocardial myoglobin and attenuates nitrite reductase capacity during ischemia-reperfusion.
Show a high capacity of myoglobin-deficient mice to adapt to catecholamine induced cardiac stress which is associated with activation of a distinct cardiac gene expression program.
Endogenous nitrite reduction to NO. via the heme globin myoglobin enhances blood flow and matches O(2) supply to increased metabolic demands under hypoxic conditions.
Myoglobin is present in the murine vasculature and contributes significantly to nitrite-induced vasodilation
myoglobin constitutes the important barrier that efficiently protects the heart from nitrosative stress
Findings demonstrate that myoglobin serves as an important cytoplasmic buffer of iNOS-derived NO, which determines the functional consequences of iNOS overexpression.
myoglobin is an important cytoplasmic cardiac hemoprotein that functions in regulating NO homeostasis within cardiomyocytes.
The role of myoglobin as intracellular nitric oxide(NO) scavenger is small, and increase in mitochondrial superoxide in SOD heterozygous mice may cause decrease NO bioavailability and alter control of myocardial O2 consumption by NO.
analysis of amyloid-forming apomyoglobin mutant W7FW14F
Mb is a key element influencing redox pathways in cardiac muscle to functionally and metabolically protect the heart from oxidative damage.
importance of oxygen supply and nitric oxide scavenging by myoglobin is clearly demonstrated at the conscious animal level
lack of myoglobin causes a biochemical shift in cardiac substrate utilization from fatty acid to glucose oxidation.
In myoglobin-containing mouse heart endogenous chromophores interfere with Fura-2 fluorometry in myocardial ischemia.
testosterone and training have differential effects on the concentration of myoglobin in some, but not all muscles
myoglobin and the heme globin family subserve a critical function as an intrinsic nitrite reductase that regulates responses to cellular hypoxia and reoxygenation.
Hypoxia reprograms calcium signaling and regulates myoglobin expression.
It regulates endometrial remodeling in the porcine endometrial tissues during follicular and luteal phase.
Results describe the specific and non-specific xenon-protein interactions of 129Xe and pig metmyoglobin as a function of the xenon and protein concentrations.
demonstrate the generalization of 2D-IR exchange spectroscopy to nonequilibrium systems and its application to map light-triggered migration of ligands between different sites in a protein
Similar conclusions are obtained both for pig cyano-myoglobin and for horse cyano-myoglobin, the structural deformation being in the former of minor entity
These results suggest an important role of genetics in meat color variation for cattle raised under the tropic conditions.
Glycine at E14 in myoglobin enhances autoxidation and hemin loss rates.
A spectroscopic study involving apomyoglobin (Apo-Mb) and cyclodextrin (CyD) of various cavity sizes as model globular protein and synthetic receptors, respectively, using steady-state and picosecond-resolved techniques, is detailed here.
Determination of a representative formal redox potentials of the Fe(II)/Fe(III) redox couple cyanhaemoglobin/cyanmethaemoglobin and the myoglobin/metmyoglobin , at pH=7 and related to the state in solution, was the objective of this work.
Methylglyoxal interacts with myoglobin by Maillard reaction. Methylglyoxal-modification leads to amyloid-like aggregation of Mb at longer incubation time.
Results suggest that the regions of apomyoglobin that resist denaturant perturbations form during the earlier stages of folding.
The study applies hydrogen/deuterium exchange (HDX) mass spectrometry (MS) for probing the conformational dynamics of the model protein myoglobin (Mb) in the presence of N(2) bubbles.
Using a coarse-grained symmetrized Go model, study performed a series of folding simulations of two apo-myoglobin molecules restrained at a high density, addressing competition of formation of a domain-swapped dimer with folding to two monomer structures.
This work presents a thorough investigation of the hydration dependence of myoglobin dynamics.
Equine carbonmonoxy Mb contains 4.5 +/- 1.0 ordered internal water molecules with a mean survival time of 5.6 +/- 0.5 mus at 25 degrees C.
this report presents a series of time-resolved UV/vis spectroscopy experiments in which no ferrylMb was detected when oxyMb and NO reacted.
The stretching mode of nitric oxide (NO) in ferric MB(III)NO consists of a major band at 1922 cm(-1) (97.7%) and a minor band at 1902 cm(-1) (2.3%), suggesting that ferric MB(III)NO in room temperature solution has two conformational substates.
The study computes electron transfer rates for the [myoglobin(wt), cytochrome b5] complex.
The ultrafast equilibrium fluctuations of the Fe(III)-NO complex of a single point mutation of Myoglobin (H64Q) have been studied using Fourier Transform 2D-IR spectroscopy.
Various structural models for the first stable HNO heme protein complex, MbHNO (Mb, myoglobin), were examined by quantum chemical calculations.
Results describe a correlation between glycation-induced structural and functional modifications of the heme protein myoglobin.
Electrospray ionization mass spectrometry (ESI-MS) was employed to monitor the heme release and the conformational changes of myoglobin (Mb) under different solvent conditions, and to observe ligand bindings of Mb.
The result indicates that the coupled protein motions involve collective motions extended over entire myoglobin correlated with local gating motions at the channels.
Results describe the crystal structure of peroxymyoglobin generated through cryoradiolytic reduction of myoglobin compound III.
Cell-specific distribution of Mb within non-muscle tissues in zebrafish plays an important role in the regulation of microvascular, renal and brain function.
myoglobin plays a crucial role in zebrafish development and is important for angiogenesis and gut development
This gene encodes a member of the globin superfamily and is expressed in skeletal and cardiac muscles. The encoded protein is a haemoprotein contributing to intracellular oxygen storage and transcellular facilitated diffusion of oxygen. At least three alternatively spliced transcript variants encoding the same protein have been reported.