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  • Title: Proteolytic processing of the Aplysia egg-laying hormone prohormone.
    Author: Garden RW, Shippy SA, Li L, Moroz TP, Sweedler JV.
    Journal: Proc Natl Acad Sci U S A; 1998 Mar 31; 95(7):3972-7. PubMed ID: 9520477.
    Abstract:
    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.
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