Pharmacological receptors for substance P and neurokinins |
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| Authors: | D Regoli G Drapeau S Dion P D'Orléans-Juste |
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| Affiliation: | 1. Department of Orthopedic Surgery, Cleveland Clinic, Cleveland, Ohio;2. Houston Methodist Orthopedics & Sports Medicine, Houston Methodist Hospital, Houston, Texas;1. Department of Neuroimmunopharmacology, Beijing Institute of Pharmacology and Toxicology, Beijing, China;2. State Key Laboratory of Toxicology and Medical Countermeasures, Beijing, China;3. Department of Poisoning and the Treatment, Affiliated Hospital to Academy of Military Medical Sciences (the 307 Hospital), Beijing, China;4. Department of Neurobiology, Beijing Institute of Basic Medical Sciences, Beijing, 100850, China;1. Department of Zoology, Banaras Hindu University, Varanasi 221005, India;2. Department of Zoology, Madras Christian College, Chennai 600059, India;3. INRA LPGP UR037, Fish Physiology and Genomics, Campus de Beaulieu, F-35042 Rennes Cedex, France;4. Department of Biotechnology, Cochin University of Science and Technology, Kochi 682022, India |
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| Abstract: | The three neurokinins identified in mammals, substance P, neurokinin A and neurokinin B, as well as their C-terminal biologically active fragments, have been used to characterize the responses of a variety of isolated organs. Three preparations selective either for substance P (the dog carotid artery), or for neurokinin A (the rabbit pulmonary artery) or for neurokinin B (the rat portal vein) are described. A neurokinin receptor classification is attempted using the neurokinins and their fragments to determine the order of potency of agonists. Three receptor subtypes have been identified: the NK-P, on which substance P (SP) is more active than neurokinin A (NKA) and neurokinin B (NKB), and the neurokinins are more active than their respective fragments; the NK-A on which NKA greater than NKB greater than SP, and some NKA fragments are more discriminative than their precursor; the NK-B on which NKB greater than NKA greater than SP, and fragments of NKB are less active than their precursor. Among the peptides studied, some potent compounds have been identified that could provide selective receptor ligands. |
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