Identification of Myoglobin in Human Smooth Muscle

Yang, Qi; Sutton, Lee; Riggs, Austen

doi:10.1074/jbc.273.36.23426

Cited by 72 publications

(65 citation statements)

References 28 publications

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“…Vascular smooth muscle cells do appear to express Myg (18). although the level of expression within smooth muscle cells and its precise cellular location remains uncharacterized.…”

Section: Figmentioning

confidence: 99%

“…An important question is whether the nonmuscle expression of this gene is biologically meaningful; does such expression truly represent expression within different cell types within the liver, gill, or brain, or might expression occur in smooth muscle or endothelial cells within the tissue microvasculature (18), or does the expression merely represent slippage of transcriptional control within tissue cells? In the liver of hypoxic carp, Myg constitutes up to 1.5% of the protein extract applied to the 2D gels and revealed by silver staining (see Fig.…”

Section: Figmentioning

confidence: 99%

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Hypoxia-inducible myoglobin expression in nonmuscle tissues

Fraser

Mello

Ward

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

155

138

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Myoglobin (Myg) is an oxygen-binding hemoprotein that is widely thought to be expressed exclusively in oxidative skeletal and cardiac myocytes, where it plays a key role in coping with chronic hypoxia. We now show in a hypoxia-tolerant fish model, that Myg is also expressed in a range of other tissues, including liver, gill, and brain. Moreover, expression of Myg transcript was substantially enhanced during chronic hypoxia, the fold-change induction being far greater in liver than muscle. By using 2D gel electrophoresis, we have confirmed that liver expresses a protein corresponding to the Myg-1 transcript and that it is significantly up-regulated during hypoxia. We have also discovered a second, unique Myg isoform, distinct from neuroglobin, which is expressed exclusively in the neural tissue but whose transcript expression was unaffected by environmental hypoxia. Both observations of nonmuscle expression and a brain-specific isoform are unprecedented, indicating that Myg may play a much wider role than previously understood and that Myg might function in the protection of tissues from deep hypoxia and ischemia as well as in reoxygenation and reperfusion injury.

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“…Vascular smooth muscle cells do appear to express Myg (18). although the level of expression within smooth muscle cells and its precise cellular location remains uncharacterized.…”

Section: Figmentioning

confidence: 99%

Section: Figmentioning

confidence: 99%

Hypoxia-inducible myoglobin expression in nonmuscle tissues

Fraser

Mello

Ward

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

155

138

View full text Add to dashboard Cite

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“…The notation myoglobin was introduced by Günther, who confirmed the results of Mörner in 1921(Günther, 1921. For a long time, the general consensus persisted that in vertebrates the expression of myoglobin is restricted to muscle tissue like cardiomyocytes, oxidative skeletal myofibers (Millikan, 1939;Wittenberg and Wittenberg, 1989) and vascular smooth muscle cells (Qiu et al, 1998;Rayner et al, 2009). However, recent studies in fish surprisingly revealed a widespread non-muscle expression under normoxia and in response to hypoxia, including liver, kidney, gills and brain (Cossins et al, 2009;Fraser et al, 2006;van der Meer et al, 2005).…”

Section: Myoglobin -The Basicsmentioning

confidence: 69%

Unmasking the Janus face of myoglobin in health and disease

Hendgen‐Cotta

Flögel

Kelm

et al. 2010

Journal of Experimental Biology

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SummaryFor more than 100 years, myoglobin has been among the most extensively studied proteins. Since the first comprehensive review on myoglobin function as a dioxygen store by Millikan in 1939 and the discovery of its structure 50 years ago, multiple studies have extended our understanding of its occurrence, properties and functions. Beyond the two major roles, the storage and the facilitation of dioxygen diffusion, recent physiological studies have revealed that myoglobin acts as a potent scavenger of nitric oxide (NO • ) representing a control system that preserves mitochondrial respiration. In addition, myoglobin may also protect the heart against reactive oxygen species (ROS), and, under hypoxic conditions, deoxygenated myoglobin is able to reduce nitrite to NO • leading to a downregulation of the cardiac energy status and to a decreased heart injury after reoxygenation. Thus, by controlling the NO • bioavailability via scavenging or formation, myoglobin serves as part of a sensitive dioxygen sensory system. In this review, the physiological relevance of these recent findings are delineated for pathological states where NO • and ROS bioavailability are known to be critical determinants for the outcome of the disease, e.g. ischemia/reperfusion injury. Detrimental and beneficial effects of the presence of myoglobin are discussed for various states of tissue oxygen tension within the heart and skeletal muscle. Furthermore, the impact of myoglobin on parasite infection, rhabdomyolysis, hindlimb and liver ischemia, angiogenesis and tumor growth are considered.

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“…(deoxy-Mb) at 435 and 207 mM Ϫ1 cm Ϫ1 (MbCO) at 423 nm (28). The titration experiments were performed under anaerobic conditions.…”

mentioning

confidence: 99%

Identification of a Thiol/Disulfide Redox Switch in the Human BK Channel That Controls Its Affinity for Heme and CO

Morgan

Ragsdale

2010

Journal of Biological Chemistry

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Heme is a required prosthetic group in many electron transfer proteins and redox enzymes. The human BK channel, which is a large- RCK1 and RCK2) of the BK channel. The HBD includes a CXXCH motif in which histidine serves as the axial heme ligand and the two cysteine residues can form a reversible thiol/disulfide redox switch that regulates affinity of the HBD for heme. The reduced dithiol state binds heme (K d ‫؍‬ 210 nM) 14-fold more tightly than the oxidized disulfide state. Furthermore, the HBD is shown to tightly bind CO (K d ‫؍‬ 50 nM) with the Cys residues in the CXXCH motif regulating affinity of the HBD for CO. This HBD is also shown to interact with heme oxygenase-2. We propose that the thiol/disulfide switch in the HBD is a mechanism by which activity of the BK channel can respond quickly and reversibly to changes in the redox state of the cell, especially as it switches between hypoxic and normoxic conditions.

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Identification of Myoglobin in Human Smooth Muscle

Cited by 72 publications

References 28 publications

Hypoxia-inducible myoglobin expression in nonmuscle tissues

Hypoxia-inducible myoglobin expression in nonmuscle tissues

Unmasking the Janus face of myoglobin in health and disease

Identification of a Thiol/Disulfide Redox Switch in the Human BK Channel That Controls Its Affinity for Heme and CO

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