Peptidomics analysis of dromedary camel supraoptic nucleus by tandem mass spectrometry

ABSTRACT: Peptides were qualitatively characterized in supraoptic nuclei (SON)of dromedary camels by liquid chromatography-mass spectrometry/mass spectrometry. Samples collected in winter and summer were analyzed separately. Qualitative seasonal differences were noted. The presence of the PMCH hormone by detection of a single peptide, Neuropeptide-glutamic acid-isoleucine (EIGDEENSAKFPI-amide), only in winter SON. SCG1- and SCG2- derived peptides were detected in both seasons, but more peptides identified in winter than summer for either of the proteins. Peptides from SCG3 were detected only in winter SON samples. We found evidence of alternative splicing of the tachykinin precursor 1 in dromedary between seasons. In summer, we detected neurokinin A (isoforms 2,4, and 6) as well as peptide DADSSVEKQVALLKALYGLGQISHKMAYE confirming prohormone variant without neurokinin A (dromedary isoforms 3 and 7), while in winter SON we detected peptides supporting prohormone variants with neurokinin A (isoforms 2, 4, 6). Substance P was detected only in winter samples. The MS data supported some of our transcriptomics results.

INSTRUMENT(S):

ORGANISM(S): Camelus Dromedarius (dromedary) (arabian Camel)

TISSUE(S): Brain

SUBMITTER: Elena Romanova  

LAB HEAD: Jonathan Sweedler

PROVIDER: PXD013869 | Pride | 2019-11-11

REPOSITORIES: Pride