Globin and Globin Gene Structure of the Nerve Myoglobin of Aphrodite aculeata

Dewilde, Sylvia; Blaxter, Mark; Hauwaert, Marie-Louise Van; Vanfleteren, Jacques R.; Esmans, Eddy L.; Marden, Michael; Griffon, Nathalie; Moëns, Luc

doi:10.1074/jbc.271.33.19865

Cited by 71 publications

(55 citation statements)

References 36 publications

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“…Loss of all introns in globin coding genes has been reported for Ascaris Mb, Tetrahymena Hb, and the majority of Chironomus globin genes (13,17,25,66). The absence of a B12.2 or a G7.0 intron in the globin genes, respectively, of Aphrodite and the second domain of Pseudoterranova clearly illustrates that each intron can be excised independently (29,67).…”

Section: Sequencing Of G Intestinalis Hb1 and Structuralmentioning

confidence: 99%

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Structural, Functional, and Genetic Characterization of Gastrophilus Hemoglobin

Dewilde¹,

Blaxter²,

Hauwaert³

et al. 1998

Journal of Biological Chemistry

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Hemoglobin of Gastrophilus intestinalis (Insecta, Diptera), was purified and characterized. At least two isoforms have been identified by isoelectrofocusing, mass spectrometry, and genomic Southern blotting. Functional studies show a high oxygen affinity due to a low ligand dissociation rate (k off ‫؍‬ 2.4 s ؊1 ) and a relatively high autoxidation rate (t1 ⁄2 ‫؍‬ 1.6/h). The globins were separated under denaturing conditions, and the sequence of Hb1 (M r ‫؍‬ 17,965 ؎ 2) was determined at the protein and DNA level. The open reading frame codes for a polypeptide of 150 amino acids. Although the globin is distantly related to globins from other species, it has a low penalty score against globin templates.Freshly isolated hemoglobin was crystallized from polyethylene glycol. Crystals contain two hemoglobin molecules per asymmetric unit. Solution of the three-dimensional structure by molecular replacement could not be achieved, possibly due to the presence of three protein isoforms in the crystals. In order to determine its threedimensional structure, G. intestinalis Hb1 was overexpressed in Escherichia coli, resulting in a fully functional molecule as confirmed by ligand binding affinity.The globin gene contains two introns at positions D7.0 and G7.0. The D7.0 intron is unprecedented, suggesting that globin gene evolution is much more complex than originally thought.

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Section: Sequencing Of G Intestinalis Hb1 and Structuralmentioning

confidence: 99%

“…A PCR reaction was then performed using the GU1 and oligo(dT) primers. Positive fragments were purified, cloned, and sequenced as described (29). The 5Ј-end was obtained by a rapid amplification of cDNA ends experiment (30).…”

Section: Methodsmentioning

confidence: 99%

Structural, Functional, and Genetic Characterization of Gastrophilus Hemoglobin

Dewilde¹,

Blaxter²,

Hauwaert³

et al. 1998

Journal of Biological Chemistry

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“…Ngb shows Ϸ20% amino acid homology to myoglobin (Mb) and Hb, and Ϸ30% homology to an intracellular nerve globin found in the annelid Aphrodite aculeata (2). Like Mb and Hb, Ngb binds O 2 with high affinity, suggesting a possible role in O 2 storage, transport, or sensing (1,(3)(4)(5).…”

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Neuroglobin-overexpressing transgenic mice are resistant to cerebral and myocardial ischemia

Khan

Wang

Sun

et al. 2006

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

201

195

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Neuroglobin (Ngb), a protein related to myoglobin and hemoglobin but expressed predominantly in the brain, is induced by neuronal hypoxia and cerebral ischemia and protects against hypoxic or ischemic neuronal injury. We engineered transgenic mice that overexpress murine Ngb under the control of a chicken ␤-actin promoter, resulting in enhanced Ngb expression in multiple cell types and multiple tissues, including brain and heart. In Ngb-overexpressing transgenic mice compared with wild-type littermates, the volume of cerebral infarcts after occlusion of the middle cerebral artery was reduced by Ϸ30%, and the volume of myocardial infarcts produced by occlusion of the left anterior descending coronary artery was reduced by Ϸ25%. Ngb overexpression was associated with enhanced expression of endothelial nitric oxide synthase in vascular endothelial cells. These findings extend prior evidence for cytoprotection by Ngb and suggest both direct (parenchymatous) and indirect (vasomotor) protective mechanisms.endothelial nitric oxide synthase ͉ myocardial infarction ͉ stroke

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“…Since then, nHbs have also been found in, or associated with, nerve tissues of several other invertebrate taxa, such as molluscs, arthropods, nemerteans, and nematode species (4,5). Of these, only the nHbs of A. aculeata (6) and the nemertean worm Cerebratulus lacteus (7) have been characterized at the molecular level.…”

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The Nerve Hemoglobin of the Bivalve Mollusc Spisula solidissima

Dewilde

Ebner

Vinck

et al. 2006

Journal of Biological Chemistry

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Members of the hemoglobin (Hb) superfamily are present in nerve tissue of several vertebrate and invertebrate species. In vertebrates they display hexacoordinate heme iron atoms and are typically expressed at low levels (M). Their function is still a matter of debate. In invertebrates they have a hexa-or pentacoordinate heme iron, are mostly expressed at high levels (mM), and have been suggested to have a myoglobin-like function. The native Hb of the surf clam, Spisula solidissima, composed of 162 amino acids, does not show specific deviations from the globin templates. UV-visible and resonance Raman spectroscopy demonstrate a hexacoordinate heme iron. Based on the sequence analogy, the histidine E7 is proposed as a sixth ligand. Kinetic and equilibrium measurements show a moderate oxygen affinity (P 50 ϳ0.6 torr) and no cooperativity. The histidine binding affinity is 100-fold lower than in neuroglobin. Phylogenetic analysis demonstrates a clustering of the S. solidissima nerve Hb with mollusc Hbs and myoglobins, but not with the vertebrate neuroglobins. We conclude that invertebrate nerve Hbs expressed at high levels are, despite the hexacoordinate nature of their heme iron, not essentially different from other intracellular Hbs. They most likely fulfill a myoglobin-like function and enhance oxygen supply to the neurons.The recent discovery of globin proteins in the nerve cells of mammals and other vertebrates (1) has created much interest in unraveling the cellular functions and potential biomedical implications of these oxygen binding molecules in the metabolism of the vertebrate nervous system (2). Historically, however, "nerve hemoglobins" (nHbs) 4 were first observed in invertebrate taxa. In 1872, Lankester had already recorded the brilliant red color of the ganglia of the polychaete annelid Aphrodite aculeata (3). Since then, nHbs have also been found in, or associated with, nerve tissues of several other invertebrate taxa, such as molluscs, arthropods, nemerteans, and nematode species (4, 5). Of these, only the nHbs of A. aculeata (6) and the nemertean worm Cerebratulus lacteus (7) have been characterized at the molecular level.With few exceptions (e.g. in air-breathing gastropods), the invertebrate nHbs are expressed at high concentrations (in the mM range) and have therefore been suggested to support nerve function by mediating O 2 storage and/or transport during temporary hypoxia (4). For example, in the gastropod mollusc Aplysia depilans, the oxygenation state of the nHb was correlated with the electrical activity of the neural ganglia, and firing was shown to be proportional to the degree of oxygenation of the globin (8). The nHb in the nerve bundles of the bivalve mollusc Tellina alternata was reported to extend the time of O 2 delivery to the nerves during anoxic periods by as much as 30 min, whereas this effect was not demonstrable in the nerves of a related clam species Tagelius plebeius, which lack the nHb (9). In many cases, the nHbs appear to be specifically expressed in the glial cells surr...

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Globin and Globin Gene Structure of the Nerve Myoglobin of Aphrodite aculeata

Cited by 71 publications

References 36 publications

Structural, Functional, and Genetic Characterization of Gastrophilus Hemoglobin

Structural, Functional, and Genetic Characterization of Gastrophilus Hemoglobin

Neuroglobin-overexpressing transgenic mice are resistant to cerebral and myocardial ischemia

The Nerve Hemoglobin of the Bivalve Mollusc Spisula solidissima

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