Membrane-bound globin X protects the cell from reactive oxygen species

Koch, Jonas; Burmester, Thorsten

doi:10.1016/j.bbrc.2015.11.105

Cited by 22 publications

(11 citation statements)

References 39 publications

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“…In this respect, the recent finding that globins may indeed be attached to the cell membrane has received particular interest: using cell biological and biochemical methods, it has been demonstrated that the GbX protein of the zebrafish Danio rerio is bound to the cell membrane via N-terminal myristoylation and S-palmitoylation (Blank et al, 2011). Furthermore, it has been shown that GbX is able to protect cells from ROS in vitro (Koch and Burmester, 2016). This precludes a standard respiratory function of GbX and instead suggests a role in the protection of membrane lipids from oxidative stress (Koch and Burmester, 2016).…”

Section: N-terminal Protein Acylation Motifs Are Widespread In Most Amentioning

confidence: 99%

“…Furthermore, it has been shown that GbX is able to protect cells from ROS in vitro (Koch and Burmester, 2016). This precludes a standard respiratory function of GbX and instead suggests a role in the protection of membrane lipids from oxidative stress (Koch and Burmester, 2016). Based on these previous findings we performed a systematic bioinformatics search for the presence of candidate protein acylation sites in arthropod GbX and GbXL, but also in the HbL variants.…”

Section: N-terminal Protein Acylation Motifs Are Widespread In Most Amentioning

confidence: 99%

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The Globin Gene Family in Arthropods: Evolution and Functional Diversity

et al. 2020

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Section: N-terminal Protein Acylation Motifs Are Widespread In Most Amentioning

confidence: 99%

Section: N-terminal Protein Acylation Motifs Are Widespread In Most Amentioning

confidence: 99%

The Globin Gene Family in Arthropods: Evolution and Functional Diversity

et al. 2020

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“…Furthermore, localization of MB in close proximity to the cell membrane has not yet been described. We, therefore, hypothesize that MB might protect the cell membrane against ROS as described for membranebound globin X (23).…”

Section: Discussionmentioning

confidence: 85%

Ectopic Myoglobin Expression Is Associated with a Favourable Outcome in Head and Neck Squamous Cell Carcinoma Patients

Meller

Ellen

Gevensleben

et al. 2016

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Abstract. Background/Aim: Ectopic myoglobin (MB)expressionMyoglobin (MB) is a cytoplasmatic monomeric oxygenbinding hemoprotein known to be localized mainly in cardiac myocytes and mitochondrial-rich skeletal muscles. In contrast to its relative haemoglobin, MB is only found in the blood stream after muscle injury. The functional paradigm of MB is the storage and intracellular transport of oxygen (O 2 ) (1, 2) to the mitochondria for oxidative phosphorylation within the myocyte. However, MB also maintains homeostasis of the nitric oxide free radical (NO•) in muscle through scavenging or producing NO• molecules (3, 4) and appropriating excessive reactive oxygen species (ROS) (5). In addition, MB is able to bind fatty acids with physiological binding constants in vitro (6). On the other hand, MB-knockout mice are viable and exhibit normal exercise capacity but their survival depends on the activation of compensating mechanisms, i.e. increasing capillary densities and haematocrit (7,8).In the last years, the existence of non-muscle MB has been increasingly acknowledged, demonstrating MB, e.g., in the liver, brain or gills of carps (9) and in humans, 6235

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“…In three-spined stickleback, neuroglobin transcription in erythrocytes was the most active of any tissue, and even more active than that of Hb. Globin x is a membrane-bound globin, 169 which can also take part in either redox 170 or NO 171 regulation. 168 As discussed above, all of these signalling systems may be active in erythrocytes and can involve Hb.…”

Section: The Functions Of "New" Globinsmentioning

confidence: 99%

Regulation of erythrocyte function: Multiple evolutionary solutions for respiratory gas transport and its regulation in fish

2019

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Gas transport concepts in vertebrates have naturally been formulated based on human blood. However, the first vertebrates were aquatic, and fish and tetrapods diverged hundreds of millions years ago. Water-breathing vertebrates live in an environment with low and variable O 2 levels, making environmental O 2 an important evolutionary selection pressure in fishes, and various features of their gas transport differ from humans. Erythrocyte function in fish is of current interest, because current environmental changes affect gas transport, and because especially zebrafish is used as a model in biomedical studies, making it important to understand the differences in gas transport between fish and mammals to be able to carry out meaningful studies. Of the close to thirty thousand fish species, teleosts are the most species-numerous group.However, two additional radiations are discussed: agnathans and elasmobranchs.The gas transport by elasmobranchs may be closest to the ancestors of tetrapods. The major difference in their haemoglobin (Hb) function to humans is their high urea tolerance. Agnathans differ from other vertebrates by having Hbs, where cooperativity is achieved by monomer-oligomer equilibria. Their erythrocytes also lack the anion exchange pathway with profound effects on CO 2 transport. Teleosts are characterized by highly pH sensitive Hbs, which can fail to become fully O 2 -saturated at low pH. An adrenergically stimulated Na + /H + exchanger has evolved in their erythrocyte membrane, and plasma-accessible carbonic anhydrase can be differentially distributed among their tissues. Together, and differing from other vertebrates, these features can maximize O 2 unloading in muscle while ensuring O 2 loading in gills. K E Y W O R D Sadrenergically stimulated Na + /H + exchange, anion exchange, Bohr effect, carbonic anhydrase, erythrocyte, oxygen equilibrium curve (OEC), Root effect 2 of 16 | NIKINMAA et Al.3 40 ) stabilize the T-state (these so-called allosteric effectors bind to sites other than the O 2 binding site). The overall OEC of Hb molecules is determined by the probabilities of T-or R-state occurrence; the equilibrium between T-and R-states is virtually instantaneous.F I G U R E 4 O 2 equilibrium curves of rainbow trout (A) at resting plasma pH (7.65) and (B) at pH 7.40, where the Root effect has been induced (ie, O 2 saturation approaches asymptotically a value below full saturation, in this case maximal O 2 saturation is 69%, ie, Root effect 31%; data from 98 )

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Membrane-bound globin X protects the cell from reactive oxygen species

Cited by 22 publications

References 39 publications

The Globin Gene Family in Arthropods: Evolution and Functional Diversity

The Globin Gene Family in Arthropods: Evolution and Functional Diversity

Ectopic Myoglobin Expression Is Associated with a Favourable Outcome in Head and Neck Squamous Cell Carcinoma Patients

Regulation of erythrocyte function: Multiple evolutionary solutions for respiratory gas transport and its regulation in fish

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