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Isolation, Primary Structure, and Effects on -Melanocyte-Stimulating Hormone Release of Frog Neurotensin¹

European Institute for Peptide Research (IFRMP 23), Laboratory of Cellular and Molecular Neuroendocrinology, INSERM U-413, Unité Affiliée au Centre National de la Recherche Scientifique, University of Rouen (L.D., M.-C.T., J.L., H.V.), 76821 Mont-Saint-Aignan, France; and Regulatory Peptide Center, Department of Biomedical Sciences, Creighton University School of Medicine (J.M.C.), Omaha, Nebraska 68178-0405

Address all correspondence and requests for reprints to: Dr. J. M. Conlon, Department of Biomedical Sciences, Creighton University Medical School, Omaha, Nebraska 68178-0405.

Neurotensin (NT) was isolated in pure form from the small intestine of the European green frog, Rana ridibunda, and its primary structure was established as pGlu-Ala-His-Ile-Ser-Lys-Ala-Arg-Arg-Pro-Tyr-Ile-Leu. This sequence contains five amino acid substitutions (Leu²Ala, Tyr³His, Glu⁴Ile, Asn⁵Ser, and Pro⁷Ala) compared with human NT. A peptide with identical chromatographic properties was identified in an extract of frog brain. Synthetic frog NT produced a concentration-dependent increase in MSH release from perifused frog pars intermedia cells, with an ED₅₀ of 5 x 10^-9 M. A maximum response (276.3 ± 45.5% above basal release) was produced by a 10^-8-M concentration. Repeated administration of NT to melanotrope cells revealed the occurrence of a rapid and pronounced desensitization mechanism. The data are consistent with a possible role for the peptide as a hypophysiotropic factor in amphibians.

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