Proteolytic Processing of the Aplysia Egg-Laying Hormone Prohormone

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 spectrometr...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1998-03, Vol.95 (7), p.3972-3977
Hauptverfasser: Garden, Rebecca W., Shippy, Scott A., Li, Lingjun, Moroz, Tatiana P., Sweedler, Jonathan V.
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Sprache:eng
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Zusammenfassung: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 AP1-20and 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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.95.7.3972