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Related Experiment Videos

Isolation and characterisation of arthropod gap junctions.

M E Finbow1, T E Buultjens, N J Lane

  • 1The Beatson Institute for Cancer Research, Garscube Estate, Bearsden, Glasgow G61 1BD, UK.

The EMBO Journal
|October 1, 1984
PubMed
Summary

Researchers isolated gap junction proteins from Norway lobster hepatopancreas. These proteins exist in interconvertible monomeric and dimeric forms, showing some shared antigens with vertebrate gap junction proteins.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Crustacean Research

Background:

  • Gap junctions are crucial for intercellular communication in multicellular organisms.
  • Understanding the molecular composition of gap junctions in invertebrates provides insights into their evolution and function.

Purpose of the Study:

  • To isolate and characterize gap junction proteins from the hepatopancreas of Nephrops norvegicus (Norway lobster).
  • To investigate the molecular forms, aggregation states, and antigenic properties of these proteins.

Main Methods:

  • Isolation of gap junctions from crustacean hepatopancreas.
  • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for protein analysis.
  • Two-dimensional tryptic and chymotryptic peptide mapping.

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  • Buoyant density centrifugation.
  • Immunological cross-reactivity assays using antibodies.

    • Main Results:

    • Two major protein bands (18 kDa and 28 kDa) were identified, likely representing monomeric and dimeric forms of the same protein.
    • The protein can form higher multimers (38 kDa and 52 kDa).
    • Isolated gap junctions have a buoyant density of 1.260 g/cm³.
    • The 18 kDa protein shares antigenic determinants with vertebrate 16 kDa gap junction proteins, but peptide mapping revealed no sequence similarity.

    Conclusions:

    • The gap junction protein from Nephrops norvegicus hepatopancreas exhibits distinct monomeric and dimeric forms and can aggregate into larger structures.
    • While sharing some antigenic similarities, the primary structure of the crustacean gap junction protein differs from its vertebrate counterpart, suggesting evolutionary divergence.