Hemoglobin function in deep-sea and hydrothermal-vent endemic fish:<i>Symenchelis parasitica</i>(Anguillidae) and<i>Thermarces cerberus</i>(Zoarcidae)

Weber, Roy E.; Hourdez, Stéphane; Knowles, Francis C.; Lallier, François H.

doi:10.1242/jeb.00475

Cited by 36 publications

(9 citation statements)

References 58 publications

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“…5a), the measured enthalpy reflects an intrinsic heat of O 2 binding (Δ H O2 ∼−62 kJ mol −1 ), which corresponds with the value for fish (e.g. eelpout Zoarces viviparus Hb corrected for the heat of solvation) (Weber et al. 2003) and moreover closely agrees with that (−59 kJ mol −1 ) determined calorimetrically for human Hb (Atha & Ackers 1974).…”

supporting

confidence: 83%

Temperature dependence of haemoglobin–oxygen affinity in heterothermic vertebrates: mechanisms and biological significance

Weber¹,

Campbell²

2010

Acta Physiologica

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As demonstrated by August Krogh et al. a century ago, the oxygen-binding reaction of vertebrate haemoglobin is cooperative (described by sigmoid O(2) equilibrium curves) and modulated by CO(2) and protons (lowered pH) that - in conjunction with later discovered allosteric effectors (chloride, lactate and organic phosphate anions) - enhance O(2) unloading from blood in relatively acidic and oxygen-poor tissues. Based on the exothermic nature of the oxygenation of the haem groups, haemoglobin-O(2) affinity also decreases with rising temperature. This thermal sensitivity favours oxygen unloading in warm working muscles, but may become detrimental in regionally heterothermic animals, for example in cold-tolerant birds and mammals and warm-bodied fish, where it may perturb the balance between O(2) unloading and O(2) requirement in organs with substantially different temperatures than at the respiratory organs and thus commonly is reduced or obliterated. Given that the oxygenation of haemoglobin is linked with the endothermic release of allosteric effectors, increased effector interaction is an effective strategy that is widely exploited to achieve adaptive reductions in the temperature dependence of blood-O(2) affinity. The molecular mechanisms implicated in heterothermic vertebrates from different taxonomic groups reveal remarkable variability, both as regards the effectors implicated (protons in tunas, organic phosphates in sharks and billfish, chloride ions in ruminants and chloride and phosphate anions in the extinct woolly mammoth, etc.) and binding sites for the same effectors, indicating multiple evolutionary origins, but convergent physiological functionality (reductions in temperature dependence of O(2) -binding affinity that safeguard tissue O(2) supply).

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supporting

confidence: 83%

Temperature dependence of haemoglobin–oxygen affinity in heterothermic vertebrates: mechanisms and biological significance

Weber¹,

Campbell²

2010

Acta Physiologica

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“…These habitats are characterized by fluctuating water temperatures, varying pH and dissolved oxygen levels, high H 2 S levels, high levels of heavy metals and temporal episodes of tectonic activity. Adaptations for survival in these harsh and unpredictable conditions of the hydrothermal vents likely are manifested in biochemical or behavioral adaptations (Geistdoerfer 1996;Weber et al 2003), aspects of the biology of these species much in need of further study.…”

Section: Discussionmentioning

confidence: 99%

A new Western Pacific Tonguefish (Pleuronectiformes: Cynoglossidae): The first Pleuronectiform discovered at active Hydrothermal Vents

Munroe¹,

Hashimoto²

2008

Zootaxa

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Symphurus thermophilus n. sp., described from 16 specimens collected by submersibles, ROV, epibenthic sled and dredge, occurs on a variety of substrata at several active hydrothermal sites located at 239–733 m between 21°N and 35°S in the western Pacific Ocean. Symphurus thermophilus, the only pleuronectiform fish known to inhabit hydrothermal vent areas, is characterized by the combination of a 1–2–2–2–2 pattern of interdigitation of dorsal proximal pterygiophores and neural spines, 14 caudal-fin rays, 5 hypurals, 9 abdominal vertebrae, 47–51 total vertebrae, 88–94 dorsal-fin rays, 74–80 anal-fin rays, 100–112 scales in longitudinal series, ocular-side pigmentation pattern featuring 5–8, black, mostly incomplete crossbands, uniformly white blind side, and black peritoneum. Of specimens examined, seven including the holotype, were collected on Kaikata Seamount off southern Japan; one specimen was collected at the Kasuga-2 hydrothermal vent, Marianas Islands; and six were collected at sites on the Kermadec Ridge. In addition to specimens captured, many other S. thermophilus were observed from submersibles and ROVs at hydrothermal sites in the western Pacific including those in the Marianas Islands, at Nikko Seamount near Minami-Iohjima Island, and at Minami-Ensei Knoll, Mid-Okinawa Trough. Many of the specimens examined have skeletal anomalies including fused bones in the caudal skeleton, and missing or partially developed and/or misshapen fin rays.

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“…These correlations suggest that the O 2 affinities of teleost fish Hbs (like carp isoHbs and anodic and cathodic eel Hbs) that have negatively charged NA2(␤2) Glu residues (47) will not exhibit significant cdB3 sensitivity. Indeed, Hb of the anguillid, Symenchelis parasitica, from deep-sea hydrothermal-vent habitats shows no sensitivity to trout cdB3 at pH 7.0 (49).…”

Section: Hbs a And D [That Show Homology With Turtle Hbs A And D (38)mentioning

confidence: 99%

Modulation of red cell glycolysis: interactions between vertebrate hemoglobins and cytoplasmic domains of band 3 red cell membrane proteins

Weber¹,

Voelter²,

Fago³

et al. 2004

American Journal of Physiology-Regulatory, Integrative and Comp

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Several vital functions/physical characteristics of erythrocytes (including glycolysis, the pentose phosphate pathway, ion fluxes, and cellular deformability) display dependence on the state of hemoglobin oxygenation. The molecular mechanism proposed involves an interaction between deoxyhemoglobin and the cytoplasmic domain of the anion-exchange protein, band 3 (cdB3). Given that band 3 also binds to membrane proteins 4.1 and 4.2, several kinases, hemichromes, and integral membrane proteins, and at least three glycolytic enzymes, it has been suggested that the cdB3-deoxyhemoglobin interaction might modulate the pathways mediated by these associated proteins in an O(2)-dependent manner. We have investigated this mechanism by synthesizing 10-mer peptides corresponding to the NH(2)-terminal fragments of various vertebrate cdB3s, determining their effects on the oxygenation reactions of hemoglobins from the same and different species and examining binding of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase to the erythrocytic membrane of mouse erythrocytes. The cdB3 interaction is strongly dependent on pH and the number of negative and positive charges of the peptide and at the effector binding site, respectively. It lowers the O(2) association equilibrium constant of the deoxygenated (Tense) state of the hemoglobin and is inhibited by magnesium ions, which neutralize cdB3's charge and by 2,3-diphosphoglycerate, which competes for the cdB3-binding site. The interaction is stronger in humans (whose erythrocytes derive energy predominantly from glycolysis and exhibit higher buffering capacity) than in birds and ectothermic vertebrates (whose erythrocytes metabolize aerobically and are poorly buffered) and is insignificant in fish, suggesting that its role in the regulation of red cell glycolysis increased with phylogenetic development in vertebrates.

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Hemoglobin function in deep-sea and hydrothermal-vent endemic fish:Symenchelis parasitica(Anguillidae) andThermarces cerberus(Zoarcidae)

Cited by 36 publications

References 58 publications

Temperature dependence of haemoglobin–oxygen affinity in heterothermic vertebrates: mechanisms and biological significance

Temperature dependence of haemoglobin–oxygen affinity in heterothermic vertebrates: mechanisms and biological significance

A new Western Pacific Tonguefish (Pleuronectiformes: Cynoglossidae): The first Pleuronectiform discovered at active Hydrothermal Vents

Modulation of red cell glycolysis: interactions between vertebrate hemoglobins and cytoplasmic domains of band 3 red cell membrane proteins

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