Proteolytic processing of the Aplysia egg-laying hormone prohormone

Rebecca W. Garden, Scott A. Shippy, Lingjun Li, Tatiana P. Moroz, Jonathan V. Sweedler

Research output: Contribution to journalArticlepeer-review


By using matrix-assisted laser desorption/ionization time-of-flight MS, individual peptidergic neurons from Aplysia are assayed. A semiquantitative method is developed for comparing single-cell profiles by using spectral normalization, and peptides are localized to specific cells by mass spectrometric cell mapping. In addition to all previously identified products of the egg-laying hormone (ELH) gene, other peptides are formed from proteolytic hydrolysis of Leu-Leu residues within ELH and acidic peptide (AP). AP exhibits further processing to yield AP1-20 and AP9-27. These peptides appear to be colocalized in vesicles with ELH, transported to specific neuronal targets, and released in a Ca2+-dependent manner. A differential peptide distribution is observed at a specific target cell, and a low-frequency variation of AP, [Thr21]AP, is detected in a single animal.

Original languageEnglish (US)
Pages (from-to)3972-3977
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number7
StatePublished - Mar 31 1998

ASJC Scopus subject areas

  • General


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