Mass spectrometric survey of interganglionically transported peptides in aplysia

• Published in: Peptides (New York, N.Y. : 1980) Vol. 19; no. 8; pp. 1425 - 1433
• Main Authors: Li, Lingjun, Moroz, Tatiana P, Garden, Rebecca W, Floyd, Philip D, Weiss, Klaudiusz R, Sweedler, Jonathan V
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 1998
• Subjects: Animals; Aplysia; Aplysia - chemistry; Aplysia - metabolism; Aplysia - physiology; Aplysia californica; Biological Transport, Active - physiology; Central Nervous System - chemistry; Cerebral peptide 1 (CP1); Freshwater; Ganglia, Invertebrate - chemistry; Ganglia, Invertebrate - metabolism; Ganglia, Invertebrate - physiology; Interganglionic transport; LUQIN; Mass spectrometry (MS); Matrix-assisted laser desorption/ionization (MALDI); Neuropeptide; Neuropeptides - analysis; Neuropeptides - metabolism; Peptide processing; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods; Interganglionic transport; Matrix-assisted laser desorption/ionization (MALDI); Aplysia californica; Peptide processing; Mass spectrometry (MS); LUQIN; Neuropeptide; Cerebral peptide 1 (CP1)
• ISSN: 0196-9781; 1873-5169
• DOI: 10.1016/S0196-9781(98)00094-1

The major ganglionic connectives in
Aplysia are assayed to determine putative neuropeptides. Matrix-assisted laser desorption/ionization mass spectrometry allows direct measurement of peptides in a nerve. Many previously characterized peptides are observed, including APGWamide, buccalins, small cardioactive peptides, and egg-laying hormone. Several unreported peptides are detected in specific nerves, suggesting they may have important physiological roles. Furthermore, novel processing products of the L5–67 precursor peptide and the APGWamide/cerebral peptide 1 prohormone are strongly suggested, and their interganglionic transport demonstrated.