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Related Experiment Videos

Cell-associated episialin is a complex containing two proteins derived from a common precursor.

M J Ligtenberg1, L Kruijshaar, F Buijs

  • 1Division of Tumor Biology, The Netherlands Cancer Institute (Antoni van Leeuwenhoekhuis), Amsterdam.

The Journal of Biological Chemistry
|March 25, 1992
PubMed
Summary

Epithelial sialomucin episialin undergoes proteolytic cleavage in the endoplasmic reticulum. This cleavage anchors the mucin-like domain to the cell membrane via interaction with the C-terminal subunit.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Episialin, an epithelial sialomucin, is a transmembrane protein with a large extracellular domain.
  • Previous research suggested proteolytic cleavage of episialin within the endoplasmic reticulum.

Purpose of the Study:

  • To confirm and characterize the proteolytic cleavage of episialin.
  • To map the precise cleavage site within the episialin molecule.
  • To investigate the association of cleavage products.

Main Methods:

  • In vitro translation systems using truncated mRNAs.
  • Analysis of a specific episialin mutant lacking the identified cleavage region.

Main Results:

  • Proteolytic cleavage of episialin was confirmed to occur in vitro, mirroring in vivo cleavage.

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  • The cleavage site was mapped to a region 53-71 amino acids upstream of the transmembrane domain.
  • Cleavage products remained associated, not through disulfide bonds, but via interaction between subunits.

    • Conclusions:

    • Episialin undergoes endoplasmic reticulum-associated cleavage.
    • The mucin-like domain remains indirectly anchored to the cell membrane through association with the C-terminal subunit.