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Mb  -  myoglobin

Rattus norvegicus

Synonyms: Myoglobin
 
 
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Disease relevance of Mb

 

High impact information on Mb

  • Skin heme oxygenase is locally elevated by stimuli such as tissue injury and injections of whole blood, myoglobin, and hematin [5].
  • Effects of inorganic iron and myoglobin on in vitro proximal tubular lipid peroxidation and cytotoxicity [6].
  • Perfusion of the LS for less than 2 min with cast-forming proteins (Bence Jones protein [BJP3] and myoglobin) decreased chloride absorption and elevated early distal tubule fluid (ED) [Cl-], compared with results obtained with control perfusions that used ATF alone [7].
  • Putrescine itself enhanced the reperfusion-evoked release of myoglobin and protein in the absence of DFMO [8].
  • In resting glands, the tracers microperoxidase , cytochrome c, myoglobin, tyrosinase (subunits), and hemoglobin were restricted to the luminal space of the acini and ducts [9].
 

Chemical compound and disease context of Mb

  • Deferoxamine addition, reported to protect against in vivo acute renal failure, paradoxically increased .OH levels (approximately 25%) in myoglobin-loaded, but not control, PTSs [10].
  • The present study was undertaken to assess whether isoflurane anesthesia might confer in vivo cytoprotection, possibly by causing renal tubular inorganic fluoride exposure, thereby mitigating a combined myoglobin/ATP depletion model of acute renal failure (glycerol-induced ARF) [11].
  • MEASUREMENTS AND MAIN RESULTS: Blood collections were used to measure blood glucose, bacteremia, plasma protein C, D-dimer, hormones, chemokines, cytokines, and myoglobin (as a marker of organ damage) [12].
  • BDM-mediated inhibition of contracture was associated with accelerated cell injury, as defined by: the uptake of an extracellular marker (trypan blue) by the cardiomyocytes, by direct analysis of myoglobin released into the supernatant and by ultrastructural demonstration of defects in sarcolemmal membrane integrity [13].
  • We tested the hypothesis that endothelin-1, the most potent renal vasoconstrictor known, plays a role in the renal toxicity of myoglobin [14].
 

Biological context of Mb

  • When oxygen consumption was increased by carbonyl cyanide m-chlorophenylhydrazone (CCCP) during superfusion of cells with 4% oxygen, PO(2) at the cell core dropped to 2.3 mmHg, whereas Mb near the plasma membrane was almost fully saturated with oxygen [15].
  • These findings show that Mb gene expression is induced by T3 [16].
  • Heat acclimation (33 degrees C for 4 weeks, 11 weeks old) did not influence Mb levels of the tissues [17].
  • We examine this phenomenon by analyzing the behavior and the kinetics of Mb oxygenation and cytochrome aa3 (cytaa3) redoxation [18].
  • It is concluded that the observed changes in renal blood flow contribute to the known direct nephrotoxic potential of Mb [3].
 

Anatomical context of Mb

  • The results suggest that bradykinin-induced NO does not interact significantly with cellular Mb to produce an NMR-detectable quantity of metMb in the perfused rat myocardium [19].
  • It is difficult, and in some cases impossible, to study the relationship between the myoglobin concentration and the oxidative capacity of individual muscle cells because myoglobin has to be fixed in situ whereas determination of oxidative capacity, for example, succinate dehydrogenase activity, requires unfixed cryostat sections [20].
  • Myoglobin plays various roles in oxygen supply to muscle mitochondria [20].
  • On ligation of the left anterior descending coronary artery, the Mb signal at 78 parts/million (ppm) appears, along with a peak shoulder assigned to the corresponding signal of Hb [21].
  • After cryolesion of the sciatic nerve, the Mb concentrations in the tibialis anterior, peroneus longus, and EDL muscles increased, reaching maximal values on days 16-21 [22].
 

Associations of Mb with chemical compounds

  • In the same spectral region, nitrite oxidation of Mb produces a set of signals at -3.7 and -4.7 ppm at 35 degrees C. Previous studies have confirmed the visibility of metMb signals in perfused rat myocardium [19].
  • Bradykinin still triggers a similar physiological response even in the presence of CO that is sufficient to inhibit 86% Mb [19].
  • In solution, nitrite oxidization of Mb produces a characteristic set of paramagnetically shifted (1)H NMR signals [19].
  • The results show that it is possible to use serial sections for the determination of the myoglobin concentration and succinate dehydrogenase activity, and indicate that myoglobin can lead to a substantial reduction (18-60%) of the extracellular oxygen tension required to prevent an anoxic core in muscle cells [20].
  • Despite the increased respiration and work, no deoxymyoglobin signal is detected, implying that the intracellular O2 level still saturates MbO2, well above the PO2 at 50% saturation of Mb [21].
 

Regulatory relationships of Mb

 

Other interactions of Mb

  • The middle and caudal sections had significantly higher mean levels of CS, LDH, and Mb than the cranial section, which may be correlated with power production during swimming [24].
  • Distribution and nature of the reactive substance to Mb antiserum were compared to those of desmin antiserum [25].
  • HO-2 utilized as substrate, Fe-protoporphyrin, Fe-hematoporphyrin, and Fe-hematoporphyrin acetate; it did not degrade intact purified rat liver cytochromes b5 and P-450 LM2, catalase, cytochrome c, hemoglobin, or myoglobin [26].
  • Increased glomerular filtration and tubular uptake of LMWP were induced by i.v. and i.p. injections of myoglobin and cationic and anionic lysozyme [27].
  • Hence, the heme pocket interior in cytochrome b5 is judged much less polar and less sterically accommodating than that of myoglobin [28].
 

Analytical, diagnostic and therapeutic context of Mb

  • It also seems reasonable that the peroxidative activity of Mb(IV), during oxygenated reperfusion, might lead to cellular damage if this hypervalent form of Mb is not reduced [29].
  • Here we investigate, by dose-response (0.3-100 microg/100 g BW, i.p., 5 days) and time-course studies (100 microg/100 g BW, i.v., from 0.5 to 24h), whether T3 affects the Mb mRNA and protein expression in atrium (A) and ventricle (V), by Northern and Western blot [30].
  • Radioimmunoassay of myoglobin (Mb) was performed in rat hind limb muscles after surgical denervation and during reinnervation following cryolesion of the sciatic nerve [22].
  • However, the [Mb] expressed as mg g(-1) protein weight was not significantly different between the ablation and control groups throughout the experimental period [1].
  • Rat Mb was isolated from the skeletal muscle; monospecificity of the rat antiserum was confirmed by the immunoblotting procedures [25].

References

  1. Adaptation of myoglobin in compensatory hypertrophied rat muscle. Masuda, K., Kano, Y., Katsuta, S. Acta Physiol. Scand. (1997) [Pubmed]
  2. Dynamics of tissue oxygenation in isolated rabbit heart as measured with near-infrared spectroscopy. de Groot, B., Zuurbier, C.J., van Beek, J.H. Am. J. Physiol. (1999) [Pubmed]
  3. Disturbances in renal microcirculation induced by myoglobin and hemorrhagic hypotension in anesthetized rat. Vetterlein, F., Hoffmann, F., Pedina, J., Neckel, M., Schmidt, G. Am. J. Physiol. (1995) [Pubmed]
  4. Induction of heme oxygenase is a rapid, protective response in rhabdomyolysis in the rat. Nath, K.A., Balla, G., Vercellotti, G.M., Balla, J., Jacob, H.S., Levitt, M.D., Rosenberg, M.E. J. Clin. Invest. (1992) [Pubmed]
  5. Bile pigment formation by skin heme oxygenase: studies on the response of the enzyme to heme compounds and tissue injury. Maines, M.D., Cohn, J. J. Exp. Med. (1977) [Pubmed]
  6. Effects of inorganic iron and myoglobin on in vitro proximal tubular lipid peroxidation and cytotoxicity. Zager, R.A., Foerder, C.A. J. Clin. Invest. (1992) [Pubmed]
  7. Mechanisms of intranephronal proteinaceous cast formation by low molecular weight proteins. Sanders, P.W., Booker, B.B., Bishop, J.B., Cheung, H.C. J. Clin. Invest. (1990) [Pubmed]
  8. Polyamines mediate uncontrolled calcium entry and cell damage in rat heart in the calcium paradox. Koenig, H., Goldstone, A.D., Trout, J.J., Lu, C.Y. J. Clin. Invest. (1987) [Pubmed]
  9. Alteration of tight junctional permeability in the rat parotid gland after isoproterenol stimulation. Mazariegos, M.R., Tice, L.W., Hand, A.R. J. Cell Biol. (1984) [Pubmed]
  10. Intracellular myoglobin loading worsens H2O2-induced, but not hypoxia/reoxygenation-induced, in vitro proximal tubular injury. Zager, R.A. Circ. Res. (1993) [Pubmed]
  11. Anesthetic effects on the glycerol model of rhabdomyolysis-induced acute renal failure in rats. Lochhead, K.M., Kharasch, E.D., Zager, R.A. J. Am. Soc. Nephrol. (1998) [Pubmed]
  12. Evaluation of protein C and other biomarkers as predictors of mortality in a rat cecal ligation and puncture model of sepsis. Heuer, J.G., Sharma, G.R., Gerlitz, B., Zhang, T., Bailey, D.L., Ding, C., Berg, D.T., Perkins, D., Stephens, E.J., Holmes, K.C., Grubbs, R.L., Fynboe, K.A., Chen, Y.F., Grinnell, B., Jakubowski, J.A. Crit. Care Med. (2004) [Pubmed]
  13. Effects of 2,3-butanedione monoxime (BDM) on contracture and injury of isolated rat myocytes following metabolic inhibition and ischemia. Armstrong, S.C., Ganote, C.E. J. Mol. Cell. Cardiol. (1991) [Pubmed]
  14. Role of endothelin in acute renal failure due to rhabdomyolysis in rats. Karam, H., Bruneval, P., Clozel, J.P., Löffler, B.M., Bariéty, J., Clozel, M. J. Pharmacol. Exp. Ther. (1995) [Pubmed]
  15. Mitochondrial respiratory control can compensate for intracellular O(2) gradients in cardiomyocytes at low PO(2). Takahashi, E., Asano, K. Am. J. Physiol. Heart Circ. Physiol. (2002) [Pubmed]
  16. Thyroid hormone stimulates myoglobin expression in soleus and extensorum digitalis longus muscles of rats: concomitant alterations in the activities of Krebs cycle oxidative enzymes. dos Santos, R.A., Giannocco, G., Nunes, M.T. Thyroid (2001) [Pubmed]
  17. Muscle myoglobin as determined by electrophoresis in thermally acclimated rat. Ohno, T., Kuroshima, A. Jpn. J. Physiol. (1986) [Pubmed]
  18. The role of myoglobin in retarding oxygen depletion in anoxic heart. Marzouki, L., Jarry, G., Janati-Idrissi, R., Amri, M. Arch. Physiol. Biochem. (2002) [Pubmed]
  19. Role of myoglobin as a scavenger of cellular NO in myocardium. Kreutzer, U., Jue, T. Am. J. Physiol. Heart Circ. Physiol. (2004) [Pubmed]
  20. Determination of myoglobin concentration and oxidative capacity in cryostat sections of human and rat skeletal muscle fibres and rat cardiomyocytes. van Beek-Harmsen, B.J., Bekedam, M.A., Feenstra, H.M., Visser, F.C., van der Laarse, W.J. Histochem. Cell Biol. (2004) [Pubmed]
  21. Oxygen supply and oxidative phosphorylation limitation in rat myocardium in situ. Kreutzer, U., Mekhamer, Y., Chung, Y., Jue, T. Am. J. Physiol. Heart Circ. Physiol. (2001) [Pubmed]
  22. Myoglobin in rat hind limb muscles after denervation and during reinnervation. Askmark, H., Carlson, M., Roxin, L.E. Muscle Nerve (1984) [Pubmed]
  23. Heme oxygenase is not expressed as a stress protein after renal ischemia. Paller, M.S., Nath, K.A., Rosenberg, M.E. J. Lab. Clin. Med. (1993) [Pubmed]
  24. Metabolic indicators in the skeletal muscles of harbor seals (Phoca vitulina). Polasek, L.K., Dickson, K.A., Davis, R.W. Am. J. Physiol. Regul. Integr. Comp. Physiol. (2006) [Pubmed]
  25. Anti-rat myoglobin antisera in the immunocytochemical diagnosis of rhabdomyosarcomas of rats. Takahashi, K., Maita, K., Shirasu, Y., Taniguchi, H., Yoshikawa, Y. Vet. Pathol. (1988) [Pubmed]
  26. Purification and characterization of the major constitutive form of testicular heme oxygenase. The noninducible isoform. Trakshel, G.M., Kutty, R.K., Maines, M.D. J. Biol. Chem. (1986) [Pubmed]
  27. Effect of low molecular weight proteins and dextran on renal cathepsin B and L activity. Olbricht, C.J., Gutjahr, E., Cannon, J.K., Irmler, H., Tisher, C.C. Kidney Int. (1990) [Pubmed]
  28. 1H NMR study of the role of heme carboxylate side chains in modulating heme pocket structure and the mechanism of reconstitution of cytochrome b5. Lee, K.B., La Mar, G.N., Pandey, R.K., Rezzano, I.N., Mansfield, K.E., Smith, K.M. Biochemistry (1991) [Pubmed]
  29. Detection of ferryl myoglobin in the isolated ischemic rat heart. Arduini, A., Eddy, L., Hochstein, P. Free Radic. Biol. Med. (1990) [Pubmed]
  30. Thyroid hormone stimulates myoglobin gene expression in rat cardiac muscle. Giannocco, G., DosSantos, R.A., Nunes, M.T. Mol. Cell. Endocrinol. (2004) [Pubmed]
 
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