Differential glycosylation and proteolytical processing of LeechCAM in central and peripheral leech neurons

Chunfa Jie, Birgit Zipser, John Jellies, Kristen M. Johansen, Jørgen Johansen

Research output: Contribution to journalArticlepeer-review

Abstract

LeechCAM is a recently described member of the Ig-superfamily which has five Ig-domains, two FNIII-domains, a transmembrane domain, and a cytoplasmic domain. Phylogenetic analysis indicated that LeechCAM is the leech homolog of apCAM, FasII, and vertebrate NCAM. Using a leechCAM-specific monoclonal antibody we show by immunoblot analysis and by Triton X-114 phase separation experiments that in addition to existing in a transmembrane version LeechCAM is likely to be proteolytically cleaved into a secreted form without the transmembrane domain and the intracellular tail. Furthermore, by immunoprecipitation we demonstrate that LeechCAM is glycosylated with the Laz2-369 glycoepitope, an epitope that has been specifically implicated in regulation of axonal outgrowth and synapse formation.

Original languageEnglish (US)
Pages (from-to)161-171
Number of pages11
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Volume1452
Issue number2
DOIs
StatePublished - Nov 11 1999

Keywords

  • (Leech)
  • Differential glycosylation
  • LeechCAM
  • Neuron
  • Proteolytic processing

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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