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Related Experiment Videos

Production, in vitro characterisation, in vivo clearance, and tissue localisation of recombinant barramundi (Lates

B Degger1, N Richardson, C Collet

  • 1Cooperative Research Centre for Tissue Growth and Repair, School of Biological Sciences, Flinders University of South Australia, Adelaide. brian@automatic.com.au

General and Comparative Endocrinology
|September 12, 2001
PubMed
Summary

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Recombinant barramundi insulin-like growth-factor-II (bIGF-II) showed lower potency than bIGF-I. bIGF-II was degraded faster in vivo, likely due to lower binding affinity for fish insulin-like growth factor-binding proteins (IGFBPs).

Area of Science:

  • Comparative endocrinology
  • Molecular biology
  • Fish physiology

Background:

  • Insulin-like growth factors (IGFs) are crucial for growth and development.
  • Understanding fish IGF systems is vital for aquaculture and evolutionary studies.
  • Barramundi insulin-like growth factor-II (bIGF-II) function and interaction with binding proteins are not well characterized.

Purpose of the Study:

  • To produce recombinant barramundi insulin-like growth-factor-II (bIGF-II) in Escherichia coli.
  • To compare the in vitro potency and in vivo behavior of bIGF-II with barramundi insulin-like growth factor-I (bIGF-I).
  • To investigate the potential role of IGF-binding proteins (IGFBPs) in bIGF-II degradation.

Main Methods:

  • Recombinant bIGF-II production using a modified expression plasmid and bacterial inclusion body processing.

Related Experiment Videos

  • Protein purification via cleavage with subtilisin BPN' and High-Performance Liquid Chromatography (HPLC).
  • In vitro protein synthesis assays and in vivo studies using radiolabeled bIGF-II and bIGF-I in juvenile barramundi, followed by radioactivity analysis and neutral gel chromatography.

    • Main Results:

    • Recombinant bIGF-II exhibited decreased potency in stimulating protein synthesis compared to bIGF-I.
    • In vivo, radiolabeled bIGF-II was degraded more rapidly than bIGF-I in juvenile barramundi.
    • Neutral gel chromatography suggested that bIGF-II has a lower affinity for barramundi IGF-binding proteins (IGFBPs) compared to bIGF-I.

    Conclusions:

    • While key IGF functional elements are conserved across vertebrates, fish IGF systems require further characterization.
    • The faster degradation of bIGF-II in vivo may be attributed to its reduced interaction with circulating IGFBPs.
    • Further research on fish IGFBPs is necessary to fully understand the biological actions of native IGFs in fish.