Substance P and Somatostatin Regulate Sympathetic Noradrenergic Function

• Published in: Science (American Association for the Advancement of Science) Vol. 221; no. 4615; pp. 1059 - 1061
• Main Authors: Kessler, John A., Adler, Joshua E., Black, Ira B.
• Format: Journal Article
• Language: English
• Published: Washington, DC The American Association for the Advancement of Science 09.09.1983; American Association for the Advancement of Science
• Subjects: Agonists; Animals; Apud cells. Peptide and protein hormones. Growth factors; Autonomic ganglia; Autonomic nervous system; Bacitracin - pharmacology; Biochemistry; Biological and medical sciences; Captopril - pharmacology; Cell culture techniques; Cells, Cultured; Culture Techniques; Dose-Response Relationship, Drug; Enzymes; Fundamental and applied biological sciences. Psychology; Ganglia; Ganglia, Autonomic; Ganglia, Sympathetic - enzymology; Nervous system, Autonomic; Neurology; Neurons; Neurotransmitters; Physiological regulation; Rats; Receptors; Somatostatin - pharmacology; Substance P - pharmacology; Sympathetic ganglia; Transmitters; Tyrosine 3-Monooxygenase - metabolism; Vertebrates: endocrinology; Rat; Substance P; Rodentia; Superior cervical ganglion; Peptide hormone; Catecholamine; Tyrosine 3-monooxygenase; Neuropeptide; Biological activity; Vertebrata; Regulation(control); Mammalia; Neurotransmitter; Norepinephrine; Somatostatin; Sympathic nervous system
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.6192502

Peptidergic-noradrenergic interactions were examined in explants of rat sympathetic superior cervical ganglia and in cultures of dissociated cells. The putative peptide transmitters substance P and somatostatin each increased the activity of the catecholamine-synthesizing enzyme tyrosine hydroxylase after 1 week of exposure in culture. Maximal increases occurred at 10$^{-7}$ molar for each peptide, and either increasing or decreasing the concentration reduced the effects. Similar increases in tyrosine hydroxylase were produced by a metabolically stable agonist of substance P, while a substance P antagonist prevented the effects of the agonist. The data suggest that the increased tyrosine hydroxylase activity was mediated by peptide interaction with specific substance P receptors and that peptides may modulate sympathetic catecholaminergic function.