α-MSH immunoreactive peptides were fractionated and characterized in rat and human brain and rat pituitary by reversed phase high pressure liquid chromatographic techniques. α-MSH and deacetylated α-MSH were two major naturally existing peptides in both brain and pituitary gland. Subsequent experiments examined the roles of these two peptides in neuronal function. The α-MSH was clearly more effective than deacetylated α-MSH in improving performance on a visual discrimination task after intraperitoneal administration and in inducing excessive grooming after intraventricular administration. The difference in behavioral potency may be explained by the fact that α-MSH was much more resistant to peptidase degradation than was deacetylated α-MSH. N-acetylation of α-MSH may be an effective regulatory process for modulating the behavioral potency of the secretory product of α-MSH-containing pituitary cells and neurons.
| Identifer | oai:union.ndltd.org:ETSU/oai:dc.etsu.edu:etsu-works-14193 |
| Date | 01 January 1981 |
| Creators | O'Donohue, Thomas L., Handelmann, Gail E., Chaconas, Ted, Miller, Russell L., Jacobowitz, David M. |
| Publisher | Digital Commons @ East Tennessee State University |
| Source Sets | East Tennessee State University |
| Detected Language | English |
| Type | text |
| Source | ETSU Faculty Works |
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