Formation of N-pyroglutamyl peptides from N-Glu and N-Gln precursors in Aplysia neurons

Rebecca W. Garden, Tatiana P. Moroz, Juliann M. Gleeson, Philip D. Floyd, Lingjun Li, Stanislav Rubakhin, Jonathan V Sweedler

Research output: Contribution to journalArticlepeer-review

Abstract

Matrix-assisted laser desorption/ionization with time-of-flight mass spectrometry is used to examine the formation of N-pyroglutamate (pGlu) in single, identified neurons from Aplysia. Six pGlu peptides are identified in the R3-14 and the R15 neurons that result from in vivo processing of peptides containing either Glu or Gln at their respective N-termini. Moreover, we show that Glu-derived pGlu is not a sample collection or measurement artifact. The pGlu peptides are detected in isolated cell bodies, regenerated neurites in culture, interganglionic connective nerves, cell homogenates, and collected releasates. We also demonstrate that R3-14 cells readily convert a synthetic N-Glu peptide to its pGlu analogue, indicating the presence of novel enzymatic activity.

Original languageEnglish (US)
Pages (from-to)676-681
Number of pages6
JournalJournal of Neurochemistry
Volume72
Issue number2
DOIs
StatePublished - 1999

Keywords

  • Abdominal ganglion
  • Aplysia
  • Matrix-assisted laser desorption/ionization mass spectrometry
  • Neuropeptide
  • Pyroglutamate
  • Single cell

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

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