Haemoglobin properties and polymerization in the marine teleost Lophius americanus (Goosefish)

Borgese, Thomas A.; Harrington, John P.; Ganjian, Iraj; Durán, Carlos M.G.

doi:10.1016/0305-0491(88)90189-7

Cited by 6 publications

(3 citation statements)

References 10 publications

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“…It is tempting to speculate that one or both of the above two histidine substitutions, which are likely to change surface charge, are responsible for the pH-dependent polymerisation of at least some Hb isoforms in codfishes. Alternatively, or in addition, the globins of codfishes are also unusually rich in cysteine, which has been implicated in the in vitro formation of Hb polymers in some other teleosts (Borgese et al, 1988;Borgese et al, 1992;Fago et al, 1993). Clearly, the elucidation of the mechanism behind Hb polymerisation awaits detailed molecular structure-function analyses, ideally on otherwise similar, polymerising and non-polymerising Hbs.…”

Section: Discussionmentioning

confidence: 99%

In vivored blood cell sickling and mechanism of recovery in whiting,Merlangius merlangus

Koldkjær

Berenbrink

2007

Journal of Experimental Biology

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hormones, which are released under capture stress, activate a powerful endogenous Na/H exchanger in these fish red blood cells, which is known to elevate intracellular pH. ␤-adrenergic treatment further leads to a marked reduction of acid-induced in vitro sickling, which is impaired when Na/H exchange is inhibited by amiloride. We propose that this mechanism protects red blood cells of some fishes against the problem of haemoglobin aggregation and red blood cell sickling, except under most severe acidosis. This system offers a unique example of how, over evolutionary time, nature may have overcome what is still a deadly disease in humans.Key words: Merlangius merlangus, sickle cell disease, Na/H exchanger, red blood cell, haemoglobin, Hb polymerisation, fish. ; N=18] were caught on hook and line from the Mersey estuary, Merseyside, UK, at incoming tide. 5-8 fish were kept in a 50-litre plastic container with ice-cooled, aerated artificial seawater (33·p.p.m.; Instant Ocean, Aquarium Systems, www.aquariumsystems.com) for up to 2·h while fishing and during transport, which took no more than 10-15·min. Fish were kept at the University of Liverpool in a 1200-litre tank with a biological filter and aerated, recirculated, artificial seawater at 13-16°C for more than one week before blood sampling (exceptions see below). Fish were exposed to a 10·h:14·h light:dark regime and fed five times weekly on frozen sand eel, squid and octopus. To ensure that the possible seasonality of RBC ion transport function would not affect the results, the experiments were carried out during the winter months Summary

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Section: Discussionmentioning

confidence: 99%

In vivored blood cell sickling and mechanism of recovery in whiting,Merlangius merlangus

Koldkjær

Berenbrink

2007

Journal of Experimental Biology

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“…Hb polymerization commonly involves Cys residues, as evident from the correlation between disulfide bridge formation and polymerization in ectotherm Hbs (13,25,67,69,85). In human Hb mutants Mississippi (␤9Ser¡Cys) and Hb Ta-li (␤83Gly¡Cys), polymerization is induced by the incorporation of a single Cys residue (6).…”

Section: Polymerization and Its Effect On Hb-o 2 Bindingmentioning

confidence: 98%

Lack of conventional oxygen-linked proton and anion binding sites does not impair allosteric regulation of oxygen binding in dwarf caiman hemoglobin

Weber

Fago

Malte

et al. 2013

American Journal of Physiology-Regulatory, Integrative and Comp

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In contrast to other vertebrate hemoglobins (Hbs) whose high intrinsic O2 affinities are reduced by red cell allosteric effectors (mainly protons, CO2, organic phosphates, and chloride ions), crocodilian Hbs exhibit low sensitivity to organic phosphates and high sensitivity to bicarbonate (HCO3(-)), which is believed to augment Hb-O2 unloading during diving and postprandial alkaline tides when blood HCO3(-) levels and metabolic rates increase. Examination of α- and β-globin amino acid sequences of dwarf caiman (Paleosuchus palpebrosus) revealed a unique combination of substitutions at key effector binding sites compared with other vertebrate and crocodilian Hbs: β82Lys→Gln, β143His→Val, and β146His→Tyr. These substitutions delete positive charges and, along with other distinctive changes in residue charge and polarity, may be expected to disrupt allosteric regulation of Hb-O2 affinity. Strikingly, however, P. palpebrosus Hb shows a strong Bohr effect, and marked deoxygenation-linked binding of organic phosphates (ATP and DPG) and CO2 as carbamate (contrasting with HCO3(-) binding in other crocodilians). Unlike other Hbs, it polymerizes to large complexes in the oxygenated state. The highly unusual properties of P. palpebrosus Hb align with a high content of His residues (potential sites for oxygenation-linked proton binding) and distinctive surface Cys residues that may form intermolecular disulfide bridges upon polymerization. On the basis of its singular properties, P. palpebrosus Hb provides a unique opportunity for studies on structure-function coupling and the evolution of compensatory mechanisms for maintaining tissue O2 delivery in Hbs that lack conventional effector-binding residues.

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“…This behavior is similar to that of the human variant Hb Rainier (30), and of C. kumu Hb (23), where Cys b49 CD8 replaces His, commonly found in other fish Hbs. Hb polymerization has also been recorded in other teleosts (33).…”

Section: Discussionmentioning

confidence: 92%

Polymerization of hemoglobins in Arctic fish: Lycodes reticulatus and Gadus morhua

et al. 2011

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SummaryIn vitro, and possibly in vivo, hemoglobin polymerization and red blood cell sickling appear to be widespread in codfish. In this article, we show that the hemoglobins of the two Arctic fish Lycodes reticulatus and Gadus morhua also have the tendency to polymerize, as monitored by dynamic light scattering experiments. The elucidation of the primary structure of the single hemoglobin of the zoarcid L. reticulatus shows the presence of a large number of cysteyl residues in a and b chains. Their role in eliciting the ability to produce polymers was also addressed by MALDI-TOF and TOF-TOF mass spectrometry. The G. morhua globins are also rich in Cys, but unlike in L. reticulatus, polymerization does not seem to be disulfide driven. The widespread occurrence of the polymerization phenomenon displayed by hemoglobins of Arctic fish supports the hypothesis that this feature may be a response to stressful environmental conditions.

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Haemoglobin properties and polymerization in the marine teleost Lophius americanus (Goosefish)

Cited by 6 publications

References 10 publications

In vivored blood cell sickling and mechanism of recovery in whiting,Merlangius merlangus

In vivored blood cell sickling and mechanism of recovery in whiting,Merlangius merlangus

Lack of conventional oxygen-linked proton and anion binding sites does not impair allosteric regulation of oxygen binding in dwarf caiman hemoglobin

Polymerization of hemoglobins in Arctic fish: Lycodes reticulatus and Gadus morhua

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