Literature DB >> 20044754

The transition in hemoglobin proton-binding characteristics within the basal actinopterygian fishes.

Matthew Daniel Regan1, Colin J Brauner.   

Abstract

Carbon dioxide (CO(2)) transport in the blood of fishes is aided by the proton-binding properties of hemoglobin (Hb) through either a high-intrinsic buffer value and small oxylabile proton binding (Haldane effect), or a low buffer value and large Haldane effect. Primitive species, such as elasmobranchs and sarcopterygians have been shown to rely on the former, while derived species, such as teleosts rely on the latter. Both strategies are effective in the transport of CO(2) in the blood. However, there is a paucity of information on the nature of the transition between these two strategies that appears to occur within the intermediate group of fishes, the basal actinopterygians. The objective of the present study was to simultaneously assess the intrinsic Hb buffer values and Haldane effects of species within the basal actinopterygian lineage to characterize the transition in Hb-proton-binding strategy seen among the fishes. Expressed in order of most basal to most derived, the species investigated included American paddlefish (Polyodon spathula), white sturgeon (Acipenser transmontanus), spotted gar (Lepisosteus oculatus), alligator gar (Atractosteus spatula), bowfin (Amia calva), and mooneye (Hiodon tergisus). Hemolysates from these species were prepared and Hb titrations (under oxygenated and deoxygenated conditions) were performed in both the presence and absence of saturating levels of organic phosphates (GTP). The findings suggest that the nature of the Hb-proton-binding transition may have been punctuated rather than gradual, with the Hb buffer value decreasing and the Haldane effect increasing significantly in bowfin from fairly steady ancestral levels in the four more basal species. This change is coupled with the initial appearance of the choroid rete, as well as an increase in the magnitude and onset pH of the Root effect in bowfin, suggesting that the change in Hb-proton-binding strategy may be associated with the evolution of enhanced O(2) delivery to the eye and an in vivo operational Root effect.

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Year:  2010        PMID: 20044754     DOI: 10.1007/s00360-009-0438-1

Source DB:  PubMed          Journal:  J Comp Physiol B        ISSN: 0174-1578            Impact factor:   2.200


  20 in total

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Authors:  A L Val
Journal:  Comp Biochem Physiol A Mol Integr Physiol       Date:  2000-04       Impact factor: 2.320

2.  Basal actinopterygian relationships: a mitogenomic perspective on the phylogeny of the "ancient fish".

Authors:  Jun G Inoue; Masaki Miya; Katsumi Tsukamoto; Mutsumi Nishida
Journal:  Mol Phylogenet Evol       Date:  2003-01       Impact factor: 4.286

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Journal:  Biol Bull       Date:  1974-02       Impact factor: 1.818

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Authors:  Michael Berenbrink; Pia Koldkjaer; Oliver Kepp; Andrew R Cossins
Journal:  Science       Date:  2005-03-18       Impact factor: 47.728

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Authors:  F B Jensen
Journal:  Comp Biochem Physiol A Mol Integr Physiol       Date:  2001-06       Impact factor: 2.320

Review 9.  Red blood cell pH, the Bohr effect, and other oxygenation-linked phenomena in blood O2 and CO2 transport.

Authors:  F B Jensen
Journal:  Acta Physiol Scand       Date:  2004-11

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Journal:  Gene       Date:  2004-05-26       Impact factor: 3.688

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  2 in total

1.  The evolution of Root effect hemoglobins in the absence of intracellular pH protection of the red blood cell: insights from primitive fishes.

Authors:  Matthew D Regan; Colin J Brauner
Journal:  J Comp Physiol B       Date:  2010-03-06       Impact factor: 2.200

2.  Osmoregulatory bicarbonate secretion exploits H(+)-sensitive haemoglobins to autoregulate intestinal O2 delivery in euryhaline teleosts.

Authors:  C A Cooper; M D Regan; C J Brauner; E S R De Bastos; R W Wilson
Journal:  J Comp Physiol B       Date:  2014-08-27       Impact factor: 2.200

  2 in total

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