Abstract
In the discovery of most neuropeptides, function has preceded antigen. Each peptide has been identified as the mediator of at least one function, and only later has knowledge of chemical structure led to antibody production, which, in turn, has led to the discovery of peptide distribution (1). Such is not the case for neuropeptide Y (NPY). Originally discovered because of its chemical structure (2), NPY was quickly identified as a member of the pancreatic polypeptide family (2,3), and after specific antiNPY antisera were made, it was localized to neurons throughout the central nervous system (4–6). Yet only very recently have studies of function, from single-cell physiology to animal behavior, begun to determine the role of NPY as a neuroactive substance in the CNS. This process of going from localization to physiology, from antigen to function, is one that is being pursued for many CNS molecules, including proteins that are recognized with select monoclonal antibodies (7–11) or that are phosphorylated by particular kinases (e.g., 12,13). It is a process that has been most successful for NPY.
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Hendry, S.H.C. (1993). Organization of Neuropeptide Y Neurons in the Mammalian Central Nervous System. In: Colmers, W.F., Wahlestedt, C. (eds) The Biology of Neuropeptide Y and Related Peptides. Contemporary Neuroscience. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-59259-465-8_3
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