Subcellular peptide localization in single identified neurons by capillary microsampling mass spectrometry

Zhang, Linwen, Khattar, Nikkita, Kemenes, Ildiko, Kemenes, Gyorgy, Zrinyi, Zita, Pirger, Zsolt, Vertes, Akos and Unset (2018) Subcellular peptide localization in single identified neurons by capillary microsampling mass spectrometry. Scientific Reports, 8. p. 1227. ISSN 2045-2322

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Single cell mass spectrometry (MS) is uniquely positioned for the sequencing and identification of peptides in rare cells. Small peptides can take on different roles in subcellular compartments. Whereas some peptides serve as neurotransmitters in the cytoplasm, they can also function as transcription factors in the nucleus. Thus, there is a need to analyze the subcellular peptide compositions in identified single cells. Here, we apply capillary microsampling MS with ion mobility separation for the sequencing of peptides in single neurons of the mollusk Lymnaea stagnalis, and the analysis of peptide distributions between the cytoplasm and nucleus of identified single neurons that are known to express cardioactive Phe-Met-Arg-Phe amide-like (FMRFamide-like) neuropeptides. Nuclei and cytoplasm of Type 1 and Type 2 F group (Fgp) neurons were analyzed for neuropeptides cleaved from the protein precursors encoded by alternative splicing products of the FMRFamide gene. Relative abundances of nine neuropeptides were determined in the cytoplasm. The nuclei contained six of these peptides at different abundances. Enabled by its relative enrichment in Fgp neurons, a new 28-residue neuropeptide was sequenced by tandem MS.

Item Type: Article
Keywords: Single cell mass spectrometry, identified neuron, subcellular peptide localization, Lymnaea stagnalis
Schools and Departments: School of Life Sciences > Neuroscience
Subjects: Q Science
Depositing User: Ildiko Kemenes
Date Deposited: 23 Aug 2018 13:46
Last Modified: 29 Aug 2018 12:58

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