title: Neuropeptidomic components generated by proteomic functions in secretory vesicles for cell-cell communication.
abstract: Diverse neuropeptides participate in cell-cell communication to coordinate neuronal and endocrine regulation of physiological processes in health and disease. Neuropeptides are short peptides ranging in length from ~3 to 40 amino acid residues that are involved in biological functions of pain, stress, obesity, hypertension, mental disorders, cancer, and numerous health conditions. The unique neuropeptide sequences define their specific biological actions. Significantly, this review article discusses how the neuropeptide field is at the crest of expanding knowledge gained from mass-spectrometry-based neuropeptidomic studies, combined with proteomic analyses for understanding the biosynthesis of neuropeptidomes. The ongoing expansion in neuropeptide diversity lies in the unbiased and global mass-spectrometry-based approaches for identification and quantitation of peptides. Current mass spectrometry technology allows definition of neuropeptide amino acid sequence structures, profiling of multiple neuropeptides in normal and disease conditions, and quantitative peptide measures in biomarker applications to monitor therapeutic drug efficacies. Complementary proteomic studies of neuropeptide secretory vesicles provide valuable insight into the protein processes utilized for neuropeptide production, storage, and secretion. Furthermore, ongoing research in developing new computational tools will facilitate advancements in mass-spectrometry-based identification of small peptides. Knowledge of the entire repertoire of neuropeptides that regulate physiological systems will provide novel insight into regulatory mechanisms in health, disease, and therapeutics.
authors: University of California, San Diego, La Jolla, 92093-0744, USA. vhook@ucsd.edu
authors: Vivian
authors: V
authors: Hook
authors: Steven
authors: S
authors: Bark
authors: Nitin
authors: N
authors: Gupta
authors: Mark
authors: M
authors: Lortie
authors: Weiya D
authors: WD
authors: Lu
authors: Nuno
authors: N
authors: Bandeira
authors: Lydiane
authors: L
authors: Funkelstein
authors: Jill
authors: J
authors: Wegrzyn
authors: Daniel T
authors: DT
authors: O'Connor
authors: Pavel
authors: P
authors: Pevzner
mesh_terms: D000595:Amino Acid Sequence; D002450:Cell Communication; D053379:Chromogranin A / Q000502:physiology; D004745:Enkephalins / Q000502:physiology; D006801:Humans; D006868:Hydrolysis; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000502:physiology*; D011498:Protein Precursors / Q000502:physiology; D011499:Protein Processing, Post-Translational; D040901:Proteomics; D011863:Radioimmunoassay; D053719:Tandem Mass Spectrometry
chemical_list: D053379:Chromogranin A; D004745:Enkephalins; D009479:Neuropeptides; D011498:Protein Precursors; C029992:proenkephalin