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J. Biol. Chem., Vol. 269, Issue 48, 30288-30292, Dec, 1994
KW Li, RM Hoek, F Smith, CR Jimenez, RC van der Schors, PA van Veelen, S Chen, J van der Greef, DC Parish and PR Benjamin
A novel strategy combining peptide fingerprinting of single neurons by
matrix-assisted laser desorption ionization mass spectrometry, molecular
cloning, peptide chemistry, and electrospray ionization mass spectrometry
was used to study the intricate processing pattern of a preprohormone
expressed in identified neurons, the neuroendocrine light yellow cells
(LYCs) of the gastropod mollusc, Lymnaea stagnalis. The cDNA encoding the
precursor, named prepro-LYCP (LYCPs, light yellow cell peptides), predicts
a straightforward processing into three peptides, LYCP I, II, and III, at
conventional dibasic processing sites flanking the peptide domains on the
precursor. However, matrix-assisted laser desorption ionization mass
spectrometry of single LYCs revealed trimmed variant peptides derived from
LYCP I and II. The variants were much more abundant than the intact
peptides, indicating that LYCP I and II serve as intermediates in a
peptide-processing sequence. Using the molecular masses of the peptides as
markers to guide their isolation by well established purification methods,
the structural identities of the peptides could be confirmed by amino acid
sequencing. Furthermore, matrix-assisted laser desorption ionization mass
spectrometry could detect colocalization of a novel peptide with the LYCPs.
Direct peptide profiling by mass spectrometry of single identified neurons reveals complex neuropeptide-processing pattern
Graduate School Neurosciences Amsterdam, Research Institute Neurosciences Vrije Universiteit, Faculty of Biology, The Netherlands.
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