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Evidence for embryonic haemoglobins from Sparus aurata under normal and hypoxic conditions

  • Manuela Mania
  • Giuseppe Bruschetta
  • Angela Avenoso
  • Angela D’Ascola
  • Michele Scuruchi
  • Adele Campo
  • Giuseppe Acri
  • Salvatore CampoEmail author
Article

Abstract

Teleost haemoglobins vary in polymorphisms and primary structure, although display similar functional properties. Key amino acids for Root effect (a reduction in oxygen-carrying capacity and loss of cooperativity with declining pH) are conserved throughout fish evolution. For the first time, we cloned and characterised Sparus aurata L. embryonic globin chains (eα1, eα2, eβ). We also studied haemoglobins (eHbI, eHbII) behaviour in normal and low-oxygen conditions. Several amino acids in fry globins are different in chemical type (e.g. polar → non-polar and vice versa), compared to adult globins. His55α1, crucial for Root effect, is substituted by Ala in fry, presumably enhancing oxygen capture, transport and reducing the dependence of Root effect from pH. Phylogenetic trees demonstrate that eα1 globin diversified more recently than eα2; moreover, eα1, eα2 and eβ globins evolved earlier than adult α and β globins. In low-oxygen conditions, fry haemoglobins display the same behaviour of the adult haemoglobins (probably, embryonic and adult-type I Hbs display a higher oxygen affinity than type II Hbs, operating through a rapid cycle of heme-Fe auto-oxidation/reduction). Therefore, based on our results and on the comparison with adult haemoglobins, we hypothesise that embryonic haemoglobins have evolved to better adapt fry to variable habitats. We studied Sparus aurata for its economical relevance in Mediterranean aquaculture. The information we provide can help understand Sparus aurata behaviour in the wild and in rearing conditions. Further studies with functional assays will deepen the knowledge on the molecular mechanisms of fry haemoglobin physiology.

Keywords

Teleost Fish culture Haemoglobins Embryonic globin chains Phylogenesis 

Abbreviations

eα1

Embryonic alpha 1

eα2

Embryonic alpha 2

Embryonic beta

HbI

Haemoglobin I

HbII

Haemoglobin II

L.

Linnaeus (1758)

Notes

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

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Copyright information

© Springer Nature B.V. 2019

Authors and Affiliations

  • Manuela Mania
    • 1
  • Giuseppe Bruschetta
    • 2
  • Angela Avenoso
    • 1
  • Angela D’Ascola
    • 1
  • Michele Scuruchi
    • 3
  • Adele Campo
    • 1
  • Giuseppe Acri
    • 1
  • Salvatore Campo
    • 1
    Email author
  1. 1.Department of Biochemical and Dental Sciences and Morphofunctional ImagesUniversity of MessinaMessinaItaly
  2. 2.Department of Veterinary SciencesUniversity of MessinaMessinaItaly
  3. 3.Department of Clinical and Experimental MedicineUniversity of MessinaMessinaItaly

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