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Related Experiment Videos

Lungfish prolactin exhibits close tetrapod relationships

T Noso1, C S Nicoll, H Kawauchi

  • 1Laboratory of Molecular Endocrinology, School of Fisheries Sciences, Kitasato University, Iwate, Japan.

Biochimica Et Biophysica Acta
|July 10, 1993
PubMed
Summary

Researchers isolated and sequenced African lungfish prolactin (PRL). Its structure suggests a closer evolutionary link to tetrapod PRLs than to teleost PRLs, offering insights into hormone evolution.

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Area of Science:

  • Comparative endocrinology
  • Evolutionary biology
  • Molecular biology

Background:

  • Prolactin (PRL) is a crucial hormone involved in diverse physiological processes across vertebrates.
  • Understanding PRL evolution requires detailed sequence and structural analysis of PRL from various species.
  • African lungfish (Protopterus aethiopicus) represent a key evolutionary link between fish and terrestrial vertebrates.

Purpose of the Study:

  • To isolate and determine the complete amino acid sequence of prolactin from the African lungfish, Protopterus aethiopicus.
  • To compare the sequence and structural features of lungfish PRL with those of other vertebrate PRLs.
  • To elucidate the evolutionary relationships of lungfish PRL within the vertebrate lineage.

Main Methods:

  • Hormone purification from pituitary gland alkaline extract using a two-step chromatographic procedure.

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  • Detection of specific immunoblot reactivity using rabbit antisera against salmon PRL.
  • Complete amino acid sequencing of the purified lungfish prolactin.

    • Main Results:

    • Isolation and sequencing of lungfish PRL, comprising 200 amino acid residues.
    • Sequence identity: 66% with amphibian, reptilian, and bird PRLs; 57% with mammalian PRLs; 38% with teleost PRLs.
    • Lungfish PRL possesses three disulfide bonds, similar to tetrapod PRLs, and notably includes an amino-terminal disulfide bond absent in teleost PRLs.

    Conclusions:

    • The structural characteristics of African lungfish PRL indicate a closer evolutionary relationship to tetrapod PRLs than to teleost PRLs.
    • The presence of three disulfide bonds, including the amino-terminal one, in lungfish PRL supports its transitional evolutionary position.
    • The 22 common amino acids across all sequenced PRLs may be vital for conserved hormonal functions.