The emerging roles of somatic globins in cardiovascular redox biology and beyond

Rahaman, Mizanur; Straub, Adam C.

doi:10.1016/j.redox.2013.08.001

Cited by 22 publications

(27 citation statements)

References 71 publications

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“…Today, this paradigm in RBC remains unchanged. However we 3 , and others 4,5 , have demonstrated that Hbα is expressed in the blood vessel wall but in contrast to other globins in the blood vessel wall 3,6,7 , Hbα localization and physiological effects are concentrated at myoendothelial junctions (MEJs) in the endothelial cells (EC) lining the lumen of blood vessels.…”

Section: Introductionmentioning

confidence: 89%

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Hemoglobin α in the blood vessel wall

Butcher

Johnson

Beers

et al. 2014

Free Radical Biology and Medicine

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Hemoglobin has been studied and well haracterized in red blood cells for over one hundred years. However, new work has indicated that the hemoglobin alpha subunit (Hbα) is also found within the blood vessel wall, where it appears to localize at the myoendothelial junction (MEJ) and plays a role in regulating nitric oxide (NO) signaling between endothelium and smooth muscle. This discovery has created a new paradigm for control of endothelial nitric oxide synthase activity, nitric oxide diffusion, and ultimately, control of vascular tone and blood pressure. This review will discuss the current knowledge of hemoglobin’s properties as a gas exchange molecule in the blood stream, and extrapolate the properties of Hbα biology to the MEJ signaling domain. Specifically, we propose that Hbα is present at the MEJ to regulate NO release and diffusion in a restricted physical space, which would have powerful implications for the regulation of blood flow in peripheral resistance arteries.

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Section: Introductionmentioning

confidence: 89%

“…Finally, excess NO may be scavenged by free hemoglobin alpha (Hbα) at the MEJ through reaction with oxyhemoglobin alpha (fast), or NO may be chelated through reaction with methemoglobin alpha (slow). Cytochrome B5 reductase (CyB5R3) converts methemoglobin alpha to Hbα, which readily binds oxygen 3,6,21–23 .…”

Section: Figurementioning

confidence: 99%

Hemoglobin α in the blood vessel wall

Butcher

Johnson

Beers

et al. 2014

Free Radical Biology and Medicine

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“…In red blood cells, hemoglobin exists as a heterotetramer of two hemoglobin α (Hba) and two hemoglobin β (Hbb) subunits. However, studies have now shown that various cell types other than erythrocytes, such as macrophages, epithelial cells, and neurons, also contain hemoglobin (Rahaman and Straub 2013). The discovery of Hba and/or Hbb expression in diverse cell types suggests that they have other roles in addition to their role in O 2 and CO 2 transport.…”

Section: Introductionmentioning

confidence: 99%

Neuronal Hemoglobin Expression and Its Relevance to Multiple Sclerosis Neuropathology

et al. 2016

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Multiple sclerosis (MS) is characterized by demyelination and progressive neurological disability. Previous studies have reported defects to mitochondria in MS including decreased expression of nuclear encoded electron transport chain subunit genes and inhibition of respiratory complexes. We previously reported increased levels of the hemoglobin β subunit (Hbb) in mitochondrial fractions isolated from postmortem MS cortex compared to controls. In the present study, we performed immunohistochemistry to determine the distribution of Hbb in postmortem MS cortex and identified proteins which interact with Hbb by liquid chromatography tandem mass spectrometry (LC-MS/MS). We found that Hbb was enriched in pyramidal neurons in internal layers of the cortex and interacts with subunits of ATP synthase, histones, and a histone lysine demethylase. We also found that Hbb is present in the nucleus and that expression of Hbb in SH-SY5Y neuroblastoma cells increased trimethylation of histone H3 on lysine 4 (H3K4me3), a histone mark that regulates cellular metabolism. These data suggest that Hbb may be a part of a mechanism linking neuronal energetics with epigenetic changes to histones in the nucleus and may provide neuroprotection in MS by supporting neuronal metabolism.

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“…Many single domain hexacoordinate Hbs have been associated with electron transfer rather than ligand transport [45]. Neuroglobin has links to cytochrome mediated apoptosis [46], NOD reactions [47][48][49][50], and nitrite reduction [22]. Cytoglobin uses lipid peroxidation [51] and auto-oxidation [45] as components of its function.…”

Section: The Role Of Ese In Hbs-mentioning

confidence: 99%