Advertisement

History of Tachykinin Peptides

  • John E. Maggio
  • Patrick W. Mantyh
Part of the The Receptors book series (REC)

Abstract

A scientific highlight of the first half of the twentieth century was the discovery and characterization of many biologically active molecules. Many large (hormones, neuropeptides) and small (classical transmitters) intercellular messengers were described during this period. Among these was substance P, which claims the longest scientific history and is arguably the most thoroughly characterized of the brain—gut peptides. It is the oldest neuropeptide in the sense that it was the first active compound from neural tissue that was later shown to be a peptide. For 50 years after its discovery, substance P (SP) was generally believed to be the only tachykinin in mammals. The relatively recent discovery of other mammalian tachykinins has raised many important new questions about the physiological role of this peptide family and has reawakened interest in the field.

Keywords

Tachykinin Receptor Amphibian Skin Rabbit Jejunum Mammalian Spinal Cord Tachykinin Peptide 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Amin, A. H., Crawford, T. B. B., and Gaddum, J. H. (1954) The distribution of substance P and 5-hydroxy-tryptamine in the central nervous system of the dog. J. Physiol. Lond. 126 596–618.PubMedGoogle Scholar
  2. Anastasi, A. and Erspamer, V. (1962) Occurrence and some properties of eledoisin in extracts of posterior salivary glands of Eledone. Br. J. Pharmacol. 19 326–336.Google Scholar
  3. Anastasi, A., Erpsamer, V., and Endean, R. (1975) Structure of uperolein a physalaemin-like endecapeptide occuring in the skin of Uperoleia rugosa and Uperoleia marmorata. Experential 31 394–395.Google Scholar
  4. Anastasi, A. and Falconieri-Erspamer, G. (1970) Occurrence of phyllomedusin a physalaemin-like decapeptide in the skin of Phyllomedusa bicolor. Experential 26 866,867.Google Scholar
  5. Anastasi, A., Montecucchi, P., Erspamer, V., and Visser, J. (1977) Amino acid composition and sequence of kassinin, a tachykinin dodecapeptide from the skin of the African frog Kassina senegalensis. Experential 33 857–858.Google Scholar
  6. Beleslin D. and Varagic, V. (1958) The effect of substance Pon the peristaltic reflex of the isolated guinea-pig ileum. Br. J. Pharmacol. 13 321–325.Google Scholar
  7. Bertaccini, G. (1976) Active peptides of nonmammalian origin. Pharmacol. Rev. 28 127–177.PubMedGoogle Scholar
  8. Boissonnas, R. A., Franz, J., and Sturmer, E. (1963) On the chemical characterization of substance P. Ann. NYAcad. Sci. 104 376,377.Google Scholar
  9. Bury, R. W. and Mashford, M. L. (1976) Biological activity of C-terminal partial sequences of substance P. J. Med. Chem. 19 854–856.PubMedCrossRefGoogle Scholar
  10. Chang, M. M. and Leeman, S. E. (1970) Isolation of a sialogogic peptide from bovine hypothalamic tissue and its characterization as substance P. J. Biol. Chem. 245 4784–4790.PubMedGoogle Scholar
  11. Chang, M. M., Leeman, S. E., and Niall, H D. (1971) Amino acid sequence of substance P. Nature New Biol. 232 86,87.PubMedGoogle Scholar
  12. Conlon, J. M., Deacon, C. F., O’Toole, L., and Thim, L. (1986) Scyliorhinin I and 11: Two novel tachykinins from dogfish gut. FEBS Leu. 200 116.CrossRefGoogle Scholar
  13. Conlon, J. M. and Thim, L. (1988) Isolation of the tachykinin des[SerlPro2] scyliorhinin 11 from the intestine of the ray, Torpedo marmorata. Gen. Comp. Endocrinol. 71 383–388.CrossRefGoogle Scholar
  14. Conlon, J. M., Katsoulis, S., Schmidt, W. E., and Thim, L. (1988a) [Arg3]substance P and neurokinin A from chicken small intestine. Regul. Pept. 20 171–180.CrossRefGoogle Scholar
  15. Conlon, J. M., O’Harte, F., Peter, R. E., and Kah, O. (1991) Carassin: A tachykinin that is structurally related to neuropeptide-gamma of the goldfish. J. Neurochem. 56 1432–1436.PubMedCrossRefGoogle Scholar
  16. Couture, R., Fournier, A., Magnan, J., St.-Pierre, S., and Regoli, D. (1979) Structure-activity studies on substance P. Can. J. Physiol. Pharmacol. 57 1427–1436.CrossRefGoogle Scholar
  17. Deacon, C. F., Agoston, D. V., Nau, R., and Conlon, J. M. (1987) Conversion of neuropeptide K to neurokinin A and vesicular colocalization of neurokinin A and substance P in the guinea-pig small intestine. J. Neurochem. 48 141–146.PubMedCrossRefGoogle Scholar
  18. Douglas, W. W., Feldberg, W., Paton, W. D. M., and Schachter, M. S. (1951) Distribution of histamine and substance P in the wall of dogs digestive tract. J. Physiol. Lond. 115 163–176.PubMedGoogle Scholar
  19. Eliasson, R., Lie, L., and Pernow, B. (1956) A comparative study of substance P from intestine and brain. Br. J. Pharmacol. 11, 137–140.Google Scholar
  20. Erspamer, V. (1949) Ricerche preliminaria sulla moschatina. Experential 5 79–81.CrossRefGoogle Scholar
  21. Erspamer, V. (1971) Biogenic amines and active polypeptides of the amphibian skin. Annu. Rev. Pharmacol. 11, 327–350.PubMedCrossRefGoogle Scholar
  22. Erspamer, V. (1981) The tachykinin peptide family. Trends Neurosci. 4 267–269.CrossRefGoogle Scholar
  23. Erspamer, V. and Anastasi, A. (1962) Structure and pharmacological actions ofeledoisin, the active endecapeptide of the posterior salivary glands of Eledone.Experiential 18 58,59.Google Scholar
  24. Erspamer, V. and Anastasi, A. (1966) Polypeptides active on plain muscle in the amphibian skin, in Hypotensive Peptides (Erdos, E. G., Back, N., Sicuteri, F., and Wilde, A. F., eds.), Springer-Verlag, New York, pp. 63–75.CrossRefGoogle Scholar
  25. Erspamer, V., Anastasi, A., Bertaccini, G., and Cei, J. M. (1964) Structure and pharmacological actions of physalaemin, the main active polypeptide of the skin of Physalaemus fuscumaculatus. Experiential 20 489,490.Google Scholar
  26. Erspamer, V. and Falconieri-Erspamer, G. (1962) Pharmacological actions of eledoi-sin on extravascular smooth muscle. Br. J. Pharmacol. 19 337–354.Google Scholar
  27. Erspamer, V. and Melchiorri, P. (1973) Active peptides of the amphibian skin andtheir synthetic analogs. Pure Appl. Chem. 35 463–494.CrossRefGoogle Scholar
  28. Gaddum, J. H. (1953) Tryptamine receptors. J. Physiol. Lond. 119 363–368.PubMedGoogle Scholar
  29. Gaddum, J. H. and Schild, H. (1934) Depressor substances in extracts of intestine. J. Physiol. Lond. 83 1–14.PubMedGoogle Scholar
  30. Gaddum, J. H. and Szerb, J. C. (1961) Assay of substance P on goldfish intestine in a microbath. Br. J. Pharmacol. 17 451–463.Google Scholar
  31. Garfield, E. (1980) ABCs of cluster mapping. Part 1. Most active fields in the life sciences 1978. Curr. Contents 40 5–12.Google Scholar
  32. Gater, P. R., Jordon, C. C., and Owen, D. G. (1982) Relative activities of substance P related peptides in the guinea-pig ileum and rat parotid gland, in vitro. Br. J. Pharmacol. 75 341–348.PubMedCrossRefGoogle Scholar
  33. Gernandt B. (1942) Untersuchung über die biologische Wirkung der Substanz P. Acta Physiol. Scand. 3 270–274.CrossRefGoogle Scholar
  34. Grabner, K., Lembeck, F., and Neuhold, K. (1959) Substanz P im Gehirn verschiedener Species. Naunyn Schmiedeberg’s Arch. Exp. Pathol. Pharmacol. 236 331–334.Google Scholar
  35. Henry, J. L., Couture, R., Cuello, A. C., Pelletier, G. Quirion, R., and Regoli, D. eds.(1987) Substance P and Neurokinins. Springer-Verlag, New York.Google Scholar
  36. Hunter, J. C. and Maggio, J. E. (1984) Pharmacological characterization of a novel tachykinin isolated from mammalian spinal cord. Eur. J. Pharmacol. 97 159,160.Google Scholar
  37. Jensen, J. and Conlon, J. M. (1992) Substance-P-related and neurokinin-A-relatedpeptides from the brain of the cod and trout. Eur. J. Biochem. 206 659–664.PubMedCrossRefGoogle Scholar
  38. Jessell, T. M. (1983) Substance P in the nervous system, in Handbook of Psychopharmacology. Neuropeptides, vol. 16 (Iversen, L. L., Iversen, S. D., and Snyder, S. H., eds.), Plenum, New York, pp. 1–105.Google Scholar
  39. Jordan, C. C. and Oehme, P., eds. (1985) Substance P, Metabolism and Biological Actions. Taylor & Francis, London.Google Scholar
  40. Kage, R., McGregor, G. P., Thim, L., and Conlon, J. M. (1988) Neuropeptidegamma: A peptide isolated from rabbit intestine that is derived from gammapreprotachykinin. J. Neurochem. 50 1412–1417.PubMedCrossRefGoogle Scholar
  41. Kangawa, K., Minamino, N., Fukuda, A., and Matsuo, H. (1983) Neuromedin K: A novel mammalian tachykinin identified in porcine spinal cord. Biochem. Biophys. Res. Commun. 114 533–540.PubMedCrossRefGoogle Scholar
  42. Kimura, S., Ogawa, T., Goto, K., Sugita, Y., Munekata, E., and Kanazawa, I. (1985) Endogenous ligands for tachykinin receptors in mammals, in Substance P: Metabolism and Biological Actions (Jordan, C.C. and Oehme, P., eds.), Taylor & Francis, London, pp. 33–43.Google Scholar
  43. Kimura, S., Okada, M., Sugita, Y., Kanazawa, I., and Munekata, E. (1983) Novel neuropeptides, neurokinins a and 13, isolated from porcine spinal cord. Proc. Jpn. Acad. Ser. B. Phys. Biol. Sci. 59 101–104.CrossRefGoogle Scholar
  44. Kozowa, H., Hino, J., Minamino, N., Kangawa, K., and Matsuo, H. (1991) Isolation of four novel tachykinins from frog (Rana catesbeiana) brain and intestine. Biochem. Biophys. Res. Comm. 177 588–595.CrossRefGoogle Scholar
  45. Lee, C.-M., Iversen, L., Hanley, M. R., and Sandberg, B. E. B. (1982) The possible existence of multiple receptors for substance P. Naunyn Schmiedeberg’s Arch. Pharmacol. 318 281–287.CrossRefGoogle Scholar
  46. Leeman, S. E. and Hammerschlag, R. (1967) Stimulation of salivary secretion by a factor from hypothalamic tissue. Endocrinology 81 803–810.PubMedCrossRefGoogle Scholar
  47. Lembeck, F. (1953) Zur Frage der zentralen Ubertragung afferenter Impulse. Ill. Das Vorkommen und die Bedeutung der Substanz P in den dorsalen Wurzeln des Ruckenmarks. Naunyn Schmiedeberg’s Arch. Exp. Pathol. Pharmacol . 219 197–213.Google Scholar
  48. Lembeck, F. and Starke, K. (1968) Substanz P und Speichelsekrection. Naunyn Schmeideberg’s Arch. Exp. Pathol. Pharmacol. 259 375–385.CrossRefGoogle Scholar
  49. Lembeck, F. and Zetler, G. (1962) Substance P. A polypeptide of possible physiological significance especially within the nervous system. Int. Rev. Neurobiol. 4 159–215.CrossRefGoogle Scholar
  50. Lembeck, F. and Zetler, G. (1971) Substance P, in Pharmacology of Naturally Occurring Polypeptides and Lipid-Soluble Acids (Walker, J. M., ed.), Pergamon, Oxford, UK, p. 2972.Google Scholar
  51. Maggio, J. E. (1988) Tachykinins. Annu. Rev. Neurosci. 11 13–28.PubMedCrossRefGoogle Scholar
  52. Maggio, J. E. (1985) Kassinin in mammals: the newest tachykinins. Peptides 6 (Suppl. 3) 237–243.PubMedCrossRefGoogle Scholar
  53. Maggio, J. E. and Hunter, J. C. (1984) Regional distribution of kassinin-like immunoreactivity in rat central and peripheral tissues and the effect of capsaicin. Brain Res. 307 370–373.PubMedCrossRefGoogle Scholar
  54. Maggio, J. E. and Mantyh, P. W. (1989) Gut tachykinins, in Handbook of Physiology (Makhlouf, G., ed.), American Physiological Society, Bethesda, MD, pp. 661–690.Google Scholar
  55. Maggio, J. E., Sandberg, B. E. B., Bradley, C. V., Iversen, L. L., Santikarn, S., Williams, D. H., Hunter, J. C., and Hanley, M.R. (1983) Substance K: A novel tachykinin in mammalian spinal cord, in Substance P—Dublin, 1983 (Skrabanek, P. and Powell, D., eds.), Boole, Dublin, Ireland, pp. 20,21.Google Scholar
  56. Meinardi, H. and Craig, L. C. (1966) Studies of substance P, in Hypotensive Peptides (Erdos, E. G., Back, N., Sicuteri, F., and Wilde, A. F., eds.), Springer-Verlag, New York, pp. 594–606.Google Scholar
  57. Melchiorri, P. and Negri, L. (1984) Evolutionary aspects of amphibian peptides, in Evolution and Tumour Pathology of the Neuroendocrine System (Falkmer, S., Hâkanson, R., and Sundler, F., eds.), Elsevier, New York, pp. 231–244.Google Scholar
  58. Minamino, N., Kangawa, K., Fukuda, A., and Matsuo, H. (1984) Neuromedin L: A novel mammalian tachykinin identified in porcine spinal cord. Neuropeptides 4 157–166.PubMedCrossRefGoogle Scholar
  59. Nakajima, T., Yasuhara, T., Erspamer, V., Falconieri-Erspamer, G., Negri, L., and Endean, R. (1980) Physalaemin-and bombesin-like peptides in the skin of the Australian leptodactylid frog Uperoleia rugosa. Chem. Pharm. Bull. 28 689–695.PubMedCrossRefGoogle Scholar
  60. Nawa, H. Hirose, T., Takashima, H., Inayama, S., and Nakanishi, S. (1983) Nucleotide sequences of cloned cDNAs for two types of bovine substance P precursor. Nature 306 32–36.PubMedCrossRefGoogle Scholar
  61. Nicoll, R. A., Schenker, C., and Leeman, S. E. (1980) Substance P as a neurotransmitter candidate. Annu. Rev. Neurosci. 3 227–268.PubMedCrossRefGoogle Scholar
  62. Oehme, P., Bienert, M., Hecht, K., and Bergmann, J. (1981) Substanz P. Ausgewählte Probleme der Chemie, Biochemie, Pharmacologie, Physiologie und Pathophysiologie. Beitr. Wirkstofforsch. 12 1–185.Google Scholar
  63. O’Harte, F., Burcher, E., Lovas, S., Smith, D. D., Vaudry, H., and Conlon, J. M. (1991) Ranakinin: A novel NK1 tachykinin receptor agonist isolated with neurokinin B from the brain of the frog Rana ridibunda. J. Neurochem. 57 2086–2091.PubMedCrossRefGoogle Scholar
  64. Otsuka, M. S., Konishi, S., and Takahashi, T. (1972a) A further study of motoneuron depolarizing peptide extracted from dorsal roots of bovine spinal nerves. Proc. Jpn. Acad. 48 747–752.Google Scholar
  65. Otsuka, M. S., Konishi, S., and Takahashi, T. (1972b) The presence of a motoneuron depolarizing peptide in bovine dorsal roots of spinal nerves. Proc. Jpn. Acad. 48 342–346.Google Scholar
  66. Pernow, B. (1951) Substance P distribution in the digestive tract. Acta Physiol. Scand. 24 97–102.PubMedCrossRefGoogle Scholar
  67. Pernow, B. (1953) Studies on substance P: Purification, occurrence and biological actions. Acta Physiol. Scand. Suppl. 105 1–90.Google Scholar
  68. Pernow, B. (1963) Pharmacology of substance P. Ann. NY Acad. Sci. 104 393–402.CrossRefGoogle Scholar
  69. Pernow, B. (1983) Substance P. Pharmacol. Rev. 35,85–141PubMedGoogle Scholar
  70. Piercey, M. F., Dobry, P. J. K., Einspahr, F. J., Schroeder, L. A., and Masiques, N. (1982) Use of substance P fragments to differentiate substance P receptors of different tissue. Regul. Pept. 3 337–349.PubMedCrossRefGoogle Scholar
  71. Porter, R. and O’Connor, M., eds. (1982) Substance Pin the Nervous System. Pitman, London (Ciba Found. Symp. 91).CrossRefGoogle Scholar
  72. Sandberg, B. E. B. (1985) Structure-activity relationships for substance P: A review, in Substance P: Metabolism and Biological Actions (Jordan, C. C. and Oehme, P., eds.), Taylor & Francis, London, pp. 65–81.Google Scholar
  73. Sandberg, B. E. B. and Iversen, L. L. (1982) Substance P. J. Med. Chem. 25 1090–1095.CrossRefGoogle Scholar
  74. Schoofs, L., Holman, G. M., Hayes, T. K., Nachman, R. J., and De Loof, A. (1990a) Locustatachykinin I and II, two novel insect neuropeptides with homology to peptides of the vertebrate tachykinin family. FEBS Lett. 261 397–401.CrossRefGoogle Scholar
  75. Schoofs, L., Holman, G. M., Hayes, T. K., Kochansky, J. P., Nachman, R. J., and De Loof, A. (1990b) Locustatachykinin Ill and IV: Two novel insect neuropeptides with homology to peptides of the vertebrate tachykinin family. Regul. Pept. 31 199–212.CrossRefGoogle Scholar
  76. Segawa, T., Nakata, Y., and Inoue, A. (1985) Precursors for substance P, in Substance P: Metabolism and Biological Actions (Jordan, C. C. and Oehme, P., eds.), Taylor & Francis, London, pp. 1–12.Google Scholar
  77. Simmaco, M., Severini, C., De Biase, D., Barra, D. Bossa, F., Roberts, J. D., Melchiorri, P., and Erspamer, V. (1990) Six novel tachykinin-and bombesinrelated peptides from the skin of the Austrialian frog Pseudophryne guntheri. Peptides 11, 299–304.PubMedCrossRefGoogle Scholar
  78. Skrabanek, P. (1984) Eye of newt and toe of frog: substance P and the charmed pot of neuropeptides. Ir. J. Med. Sci. 153 47–59.PubMedCrossRefGoogle Scholar
  79. Skrabanek, P. and Powell, D. (1977) Substance P. Vol. 1. Eden, Montreal, Canada.Google Scholar
  80. Skrabanek, P. and Powell, D. (1980) Substance P. Vol. 2. Eden, Montreal, Canada.Google Scholar
  81. Skrabanek, P. and Powell, D. (1983a) Substance P. Vol. 3. Eden, Montreal, Canada.Google Scholar
  82. Skrabanek, P. and Powell, D. (1983b) Substance P—Dublin 1983. Boole, Dublin,Ireland.Google Scholar
  83. Studer, R.O., Trzeciak, H. and Lergier, W. (1973) Isolierung und Aminosauresequenz Von Substanz P aus Pferdedarm. Heiv. Chim. Acta 56 860–866.CrossRefGoogle Scholar
  84. Tatemoto, K., Lundberg, J. M., Jornvall, H., and Mutt, V. (1985) Neuropeptide K: Isolation, structure and biological activities of a novel brain tachykinin. Biochem. Biophys. Res. Commun. 128 947–953.PubMedCrossRefGoogle Scholar
  85. Teichberg, V. I. Cohen, S., and Blumberg, S. (1981) Distinct classes of substance P receptors revealed by a comparison of the activities of substance P and some of its segments. Regul. Pept. 1 323–333.CrossRefGoogle Scholar
  86. Theodorsson-Norheim, E., Brodin, E., Norheim, I, and Rosell, N. (1985) Antisera raised against elodoisin and kassinin detect immunoreactive material in rat tissue extracts: Tissue distribution and chromotographic characterization. Regul. Pept. 9 229–244.CrossRefGoogle Scholar
  87. Theodorsson-Norheim, E., Norheim, I., Oberg, K., Brodin, E., Lundberg, J. M., Tatemoto, K., and Lindgrenn, P. G. (1985) Neuropeptide K: A major tachykinin in plasma and tumor tissues from carcinoid patients. Biochem. Biophys. Res. Commun. 131 77–83.PubMedCrossRefGoogle Scholar
  88. Too, H. P., Cordova, J. L., and Maggio, J. E. (1989) Heterogeneity of tachykinin peptides in the rat spinal cord and dorsal root ganglia. Peptides 10 25–30.PubMedCrossRefGoogle Scholar
  89. Vogler, K., Haefely, W., Hurlimann, A., Studer, R. O., Lergier, W., Strassle, R., and Berneis, K. H. (1963) A new purification procedure and biological properties of substance P. Ann. NYAcad. Sci. 104 378–389.CrossRefGoogle Scholar
  90. Von Euler, U. S. (1936) Untersuchungen uber Substanz P, die atropinfester, darmerregende und gefbasserweiternde Substanz aus Darm und Gehirn. Naunyn Schmiedeberg’s Arch. Exp. Pathol. Pharmacol. 181 181–197.CrossRefGoogle Scholar
  91. Von Euler, U. S. (1942) Herstellung und Eigenschaften Von Substanz P Acta Physiol. Scand. 4 373–375.CrossRefGoogle Scholar
  92. Von Euler, U. S. and Gaddum, J. H. (1931) An unidentified depressor substance in certain tissue extracts. J. Physiol. Lond. 72 74–87.Google Scholar
  93. Von Euler, U.S. and Ostlund, E. (1956) Occurrence of a substance P-like polypeptide in fish intestine and brain. Br. J. Pharmacol. 11, 323–325.Google Scholar
  94. Von Euler, U. S. and Pernow, B. (1977) Substance P. Raven, New York (Nobel Symp Ser., no. 37).Google Scholar
  95. Wang, Y., O’Harte, F., and Conlon, J. M. (1992a) Structural characterization of tachykinins (neuropeptide gamma, neurokinin A and substance P) from a reptile, Alligator mississipiensis. Gen. Comp. Endocrinol. 88 277–286.CrossRefGoogle Scholar
  96. Wang, Y., Badgery-Parker, T., Lovas, S., Chartrel, N., Vaudry, H., Burcher, E., and Conlon, J. M. (1992b) Primary structure and receptor-binding properties of a neurokinin A-related peptide from frog gut. Biochem. J. 287 827–832.Google Scholar
  97. Watson, S. P., Sandberg, B. E. B., Hanley, M. R., and Iversen, L. L. (1983) Tissue selectivity of substance P alkyl esters suggesting multiple receptors. Eur. J. Pharmacol. 87 77–84.PubMedCrossRefGoogle Scholar
  98. Waugh, D., Hazon, N., Balment, R. J. and Conlon, J. M. (1993) Structures and biological activities of novel tachykinins from fish brain. Thirteenth Am. Peptide Symp., in press.Google Scholar
  99. Yasuhara, T., Nakjima, T., Falconieri-Erspamer, G., and Erspamer, V. (1981) New tachykinins Glu2 ProS-kassinin (Hylambates-kassinin) and hylambatin in the skin of the African rhacophorid frog Hylambates maculatus. Biomed. Res. 2 613–617.Google Scholar
  100. Zuber, H. (1963) Isolation of substance P from bovine brain. Ann. NYAcad. Sci. 104 391–392.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1994

Authors and Affiliations

  • John E. Maggio
  • Patrick W. Mantyh

There are no affiliations available

Personalised recommendations