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Biologically Active Fragments of Proteins

  • Theodor Wieland
  • Miklos Bodanszky

Abstract

In the preceding chapter the definition of hormones, compounds which transmit instructions from one organ to another, was not strictly followed, but there are numerous biologically active peptides that do not fit even into a loose hormone-definition. They exhibit great variation in their activities and it is difficult to find a simple way to classify them. Hence we intend to discuss on the following pages compounds containing only proteinogen amino acid constituents, more or less according to the chronology of their discovery. Peptides with unusual building components, generally obtained from microorganisms, will be the subject of a separate discussion (Chap. 9).

Keywords

Angiotensin Converting Enzyme Vasoactive Intestinal Peptide Opioid Peptide Active Peptide Atrial Natriuretic Factor 
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.

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References

  1. 1.
    H. Goldblatt, The renal origin of hypertension. Physiol. Rev. 27:120–165 (1947).PubMedGoogle Scholar
  2. 2.
    L.T. Skeggs, F.E. Dorer, M. Levine, K.E. Lentz, J.R. Kahn, The biochemistry of the angiotensin system. In advances in Exptl. Med. and Biol. Vol. 130 (J.A. Johnson, R.R. Anderson eds., Plenum, New York 1980); L.T. Skeggs, Jr., J.R. Kahn, K. Lentz, N.P. Shumway, Preparation, purification and amino acid sequence of a polypeptide renin substrate. J. Exptl. Med. 106: 439-453 (1957); L.T. Skeggs Jr., K. Lentz, J.R. Kahn, N.P. Shumway, Synthesis of a tetradecapeptide renin substrate. J. Exptl. Med. 108: 283-297 (1958).Google Scholar
  3. 3.
    D.F. Elliott, W.S. Peart, Amino acid sequence in a hypertensin. Nature (Lond.) 177: 527–528 (1956); L.T. Skeggs, Jr., K.E. Lentz, J.R. Kahn, N.P. Shumway, K.R. Woods. The amino acid sequence of hypertensin II. J. Exptl. Med. 104: 193-197 (1956).CrossRefGoogle Scholar
  4. 4.
    H. Schwarz, M. Bumpus, I.H. Page, Synthesis of a biologically active octapeptide similar to natural isoleucine angiotensin octapeptide. J. Amer. Chem. Soc. 79: 5697–5703 (1957).CrossRefGoogle Scholar
  5. 5.
    W. Rittel, B. Iselin, H. Kappeler, B. Riniker, R. Schwyzer, Synthese eines hochwirksamen Hypertensin-II-amids. Helv. Chim. Acta 40: 614–624 (1957).CrossRefGoogle Scholar
  6. 6.
    D.T. Pals, F.D. Masucci, G.S. Denning Jr., F. Sipos, D.C. Fessier, Role of the pressor action of angiotensin II in experimental hypertension. Circulation Research 29: 673–687 (1971).PubMedGoogle Scholar
  7. 7.
    M.A. Ondetti, B. Rubin, D. Cushman, Design of specific inhibitors of angiotensin converting enzyme:New class of orally active antihypertensive agents. Science 196: 441–444 (1977).PubMedCrossRefGoogle Scholar
  8. 8.
    M. Rocha e Silva, W.T. Beraldo, G. Rosenfeld, Bradykinin a hypotensive and smooth muscle stimulating factor released from plasma globulin by snake venoms and by trypsin. Am. J. Physiol. 156: 261–273 (1949).PubMedGoogle Scholar
  9. 9.
    D.F. Elliott, G.P. Lewis, E.W. Horton, The structure of bradykinin — a plasma kinin from ox blood. Biochem. Biophys. Res. Commun. 3: 87–91 (1960).CrossRefGoogle Scholar
  10. 10.
    R.A. Boissonnas, St. Guttmann, P.A. Jaquenoud, Synthèse de la l-arginyl-l-prolyl-l-prolyl-glycyl-l-phenylalanyl-l-seryl-l-prolyl-l-phenylalanyl-l-arginine, un nonapeptide presentant les proprietees de la bradykinine. Helv. Chim. Acta 43: 1349–1358 (1960).CrossRefGoogle Scholar
  11. 11.
    E.D. Nicolaides, H.A. de Wald, Studies on the synthesis of polypeptides. J. Org. Chem. 26: 3872–3876 (1961).CrossRefGoogle Scholar
  12. 12.
    R.B. Merrifield, Solid phase peptide synthesis II. Synthesis of bradykinin. J. Amer. Chem. Soc. 86: 304–305 (1964).CrossRefGoogle Scholar
  13. 13.
    R.J. Vavrek, J.M. Stewart, Competitive antagonists of bradykinin Peptides 6:161–164 (1985).Google Scholar
  14. 14.
    E.G. Erdös, E.M. Sloane, A.G. Renfrew, J.R. Wohler, Enzymatic studies on bradykinin and similar peptides, Ann. N.Y. Acad. Sci. 104: 222–235 (1963).CrossRefGoogle Scholar
  15. 15.
    U.S. von Euler, J.H. Gaddum, An unidentified depressor substance in certain tissue extracts. J. Physiol. 72: 74–87 (1931).Google Scholar
  16. 16.
    J. Franz, R.A. Boissonnas, E. Stürmer, Isolierung von Substanz P aus Pferdedarm und ihre biologische und chemische Abgrenzung gegenüber Bradykinin. Helv. Chim. Acta 44: 881–883 (1961)CrossRefGoogle Scholar
  17. H. Zuber, R. Jaques, The isolation of substance P from bovine brain. Angew. Chem. Int. Ed. 1: 160. (1962)Google Scholar
  18. K. Vogler, W. Haefely, A. Hürliman, R.O. Studer, W. Lergier, R. Strässle, K.H. Berneis, A new purification procedure and biological properties of substance P. Ann. N.Y. Acad. Sci. 104: 378–390 (1963).PubMedCrossRefGoogle Scholar
  19. 17.
    G.W. Tregear, H.D. Niall, J.T. Potts, S.E. Leeman, M.M. Chang, Synthesis of substance P. Nature (Lond.) New Biol. 232: 86–89 (1971)Google Scholar
  20. R.O. Studer, A. Trzeciak, W. Lergier, Isolierung und Aminosäuresquenz von Substanz P aus Pferdedarm. Helv. Chim. Acta 56: 860–866 (1973).CrossRefGoogle Scholar
  21. 18.
    A. Fournier, R. Couture, D. Regoli, M. Gendrau, S. St. Pierre, Synthesis of peptides by the solid phase method 7. Substance P and analogues. J. Med. Chem. 25: 64–68 (1982).PubMedCrossRefGoogle Scholar
  22. 19.
    V. Erspamer, Active constituents of the posterior salivary glands of octopods and of the hypobranchial gland of the purple snail. Arzneimittelforschung 2: 253–258 (1952).PubMedGoogle Scholar
  23. 20.
    V. Erspamer, A. Anastasi, Eledoisin. Experientia 18: 58–59 (1962).PubMedCrossRefGoogle Scholar
  24. 21.
    E. Sandrin, R.A. Boissonnas, Synthesis of Eledoisin. Experientia 18: 59–60 (1962).PubMedCrossRefGoogle Scholar
  25. 22.
    V. Erspamer, A. Anastasi, G. Bertaccini, J.M. Cei, Structure and pharmacological action of physalaemin, the main active polypeptide in the skin of Physalaemus fuscumaculatus. Experientia 20: 489–490 (1964).CrossRefGoogle Scholar
  26. 23.
    L. Bernardi, G. Bosisio, O. Goffredo, R. de Castiglione, Synthesis of physalaemin, Experientia 490-492 (1964).Google Scholar
  27. 24.
    A. Anastasia, V. Erspamer, R. Andean, Structure of uperolein a physalaemin-like undecapeptide occuring in the skin of Uperoleia rugosa and Uperoleia marmorata. Experientia 31:394–395 (1974).CrossRefGoogle Scholar
  28. 25.
    A. Anastasi, V. Erspamer, R. Andean, Amino acid composition and sequence of litorin, a bombesin-like nonapeptide from the skin of the Australian leptodactylid frog Litora aurea. Experientia 31: 510–511 (1975).PubMedCrossRefGoogle Scholar
  29. 26.
    R. de Castiglione, M. Gigli, L. Gozzini, P.C. Montecucchi, G. Perseo, V. Erspamer, Structure, synthesis and preliminary biological results of tryptophyllin-7 and analogues. Peptides 1984, Proceedings of the 18th European Peptide Symposium (Almquist and Wiksell Internat. Stockholm, Sweden) 1984, pp. 533–536.Google Scholar
  30. 27.
    P.C. Montecucchi, A. Anastasi, R. de Castiglione, V. Erspamer, Isolation and amino acid composition of sauvagine. Internatl. J. of Pept. and Prot. Res. 16: 191–199 (1980).CrossRefGoogle Scholar
  31. 28.
    P.C. Montecucchi, R. de Castiglione, S. Piani, L. Gozzini, V. Erspamer, Amino acid composition and sequence of dermorphin, a novel opiate-like peptides from the skin of Phyllomedusa sauvagei. Int. J. Pept. Prot. Res. 17: 275–283 (1981).CrossRefGoogle Scholar
  32. 29.
    P.C. Montecucchi, R. de Castiglione, V. Erspamer, Identification of dermorphin and Hyp6-dermorphin in skin extracts of the Brazilian frog Phyllomedusa rhodeii. Int. J. Pept. Protein Res. 17: 316–321 (1981); R. de Castiglione, F. Faoro, G. Perseo, S. Piani, Synthesis of dermorphins, a new class of opiate like peptides. Int. J. Pept. Protein Res. 17: 263-272 (1981).PubMedCrossRefGoogle Scholar
  33. 30.
    A. Anastasi, V. Erspamer, M. Bucci, Isolation and amino acid sequences of alytesin and bombesin, two analogous active tetradecapeptides from the skin of the European dicoglossid frog. Arch. Biochem. Biophys. 148: 443–446 (1972).PubMedCrossRefGoogle Scholar
  34. 31.
    V. Erspamer, Peptides of amphibian skin active on the gut. II. Bombesin like peptides: isolation, structure and basic functions. In Gastrointestinal Hormones (G.B. Jerzy Glass ed.) Raven, New York, 1980, pp. 344–361.Google Scholar
  35. 32.
    E. Habermann, J. Jentsch, Sequential analysis of melittin from tryptic and peptic fragments. Hoppe Seyler’s Z. Physiol. Chem 348: 37–50 (1967).PubMedCrossRefGoogle Scholar
  36. 33.
    M.A. Ondetti, N.J. Williams, E.F. Sabo, J. Pluscec, E.R. Weaver, O. Kocy, Angiotensin-converting enzyme inhibitor from the venom of Bothrops jararaca. Isolation, elucidation of structure and synthesis. Biochemistry 10: 4033–4039 (1971).PubMedCrossRefGoogle Scholar
  37. 34.
    A. Bodanszky, M.A. Ondetti, C.A. Ralofsky, M. Bodanszky, Optical rotatory dispersion of prolin-rich peptides from the venom of Bothrops jararaca. Experientia 27:1269–1270 (1971).PubMedCrossRefGoogle Scholar
  38. 35.
    D.S. Parker, J.P. Raufman, T.L. O’Donohue, M. Bledsoe, H. Yoshida, J.J. Pisano, Amino acid sequence of helospectin, new member of the glucagon superfamily found in Gila monster venom. J. Biol. Chem. 259:11751–11755 (1984).PubMedGoogle Scholar
  39. 36.
    J. Hughes, T.W. Smith, H.W. Kosterlitz, L.A. Fotherhill, B.A. Morgan, H.R. Morris, Identification of two related peptides from the brain with potent opiate agonist activity. Nature (Lond.) 258: 577–579 (1975).CrossRefGoogle Scholar
  40. 37.
    C.H. Li, D. Chung, Isolation and structure of an untriakontapeptide with opiate activity from camel pituitary glands. Proc. Natl. Acad. Sci. U.S. 73:1145–1148 (1976); N. Ling, R. Burgus, R. Guillemin, Isolation, primary structure and synthesis of α-endorphin and γ-endorphin, two peptides of hypothalamic-hypophysial origin with morphinomimetic activity. Proc. Natl. Acad. Sci. U.S. 73: 3942-3946 (1976); M. Robintsen, S. Stein, S. Udenfriend, Isolation, characterization of the opioid peptide from rat pituitary: β-endorphin. Proc. Natl. Acad. Sci. U.S. 74: 4969-4972 (1977).CrossRefGoogle Scholar
  41. 38.
    A. Goldstein, S. Tachibana, L.I. Lowney, M. Hunkapiller, L. Hood, Dynorphin (1–13) an extraordinarily potent opioid peptide. Proc. Natl. Acad. Sci. U.S. 76: 6666-6670; A. Goldstein, W. Fischli, L.I. Lowney, M. Hunkapiller, L. Hood, Porcine pituitary dynorphin:complete amino acid sequence of the biologically active heptadecapeptide. ibid. 78:7219-7223 (1981).Google Scholar
  42. 39.
    S. Kimura, R.V. Lewis, L.D. Gerber, L. Brink, M. Rubinstein, S. Stein, S. Udenfriend, Purification to homogeneity of camel pituitary pro-opiocortin, the common precursor of opioid peptides and corticotropin. Proc. Natl. Acad. Sci. U.S. 76:1756–1759 (1979).CrossRefGoogle Scholar
  43. 40.
    C.D. Unsworth, J. Hughes, J.S. Morley, O-sulfated Leu-enkephalin in brain. Nature (Lond.) 295: 519–522 (1982).CrossRefGoogle Scholar
  44. 41.
    S. Cohen, G. Carpenter, Human epidermal growth factor. Isolation and chemical and biological properties. Proc. Natl. Acad. Sci. U.S. 72: 1317–1321 (1975).CrossRefGoogle Scholar
  45. 42.
    H. Gregory, Isolation and structure of urogastrone and its relationship to epidermal growth factor. Nature 257: 325–327 (1975).PubMedCrossRefGoogle Scholar
  46. 43.
    G.A. Schoenenberger, M. Monnier, Characterization of a deltaelectroeneephalogram (-sleep)-inducing peptide. Proc. Natl. Acad. Sci. U.S. 74: 1282–1286 (1977).CrossRefGoogle Scholar
  47. 44.
    J.R. Slemmon, R. Blacher, W. Danho, J.L. Hemstead, J.I. Morgan, Isolation and sequence of two cerebellum-specific peptides. Proc. Natl. Acad. Sci. U.S. 81: 6866–6870 (1984).CrossRefGoogle Scholar
  48. 45.
    V. Mutt, Questions answered and raised by work on the chemistry of gastrointestinal and cerebrogastrointestinal hormonal polypeptides. Chemical Scripta 26B: 191–207 (1986).Google Scholar
  49. 46.
    A.J. de Bold, H.B. Borenstein, A.T. Veress, H.A. Sonnenberg, A rapid and potent natriuretic response to intravenous injection of atrial miocardial extracts in rats. Life Sci. 28: 89–94 (1981); A.J. de Bold, Atrial natriuretic factor of the rat heart. Studies on isolation and properties. Proc. Soc. Exptl. Biol. Med. 1982: 133-138.PubMedCrossRefGoogle Scholar
  50. 47.
    T.G. Flynn, M.L. de Bold, A.J. de Bold, The amino acid sequence of an atrial peptide with potent diuretic and natriuretic properties. Biochem. Biophys. Res. Commun. 117: 859–865 (1983); M.G. Currie, D.M. Geller, B.R. Cole, N.R. Siegel, K.F. Fok, S.P. Adams, S.R. Eubanks, C.R. Galluppi, P. Needleman, Purification and sequence analysis of bioactive atrial peptides (atriopeptines). Science 223: 67-69 (1984).PubMedCrossRefGoogle Scholar
  51. 48.
    K. Nakayama, H. Ohkubo, T. Hirose, S. Inayama, S. Nakanishi, mRNA sequence for human cardiodilatin-atrial natriuretic factor and regulation of precursor mRNA in rat atria. Nature (Lond.) 310: 699–701 (1984); S. Oikawa, M. Imai, A. Ueno, S. Tanaka, T. Noguchi, H. Nakazato, K. Kangawa, A. Fukuda, H. Matsuo, Cloning and-sequence analysis of cDNA encoding a precursor for human atrial natriuretic polypeptides. ibid. 309: 724-726 (1984).CrossRefGoogle Scholar
  52. 49.
    S.A. Atlas, H.D. Kleinert, M.J. Camargo, A. Januszewicz, J.E. Sealy, J.H. Laragh, J.W. Schilling, J.A. Lewicki, L.K. Johnson, T. Maack, Purification, sequencing and synthesis of a natriuretic and vasoactive rat atrial peptide. Nature (Lond.) 309: 717–719 (1984); M. Yamanaka, B. Greenberg, T. Friedmann, J. Miller, S. Atlas, L. Laragh, J. Lewicki, J. Fiddes, Cloning and sequence analysis of the c DNA for the rat atrial natriuretic factor precursor, ibid. 309: 719-722 (1984); M. Maki, R. Takayanagi, K.S. Misono, K.N. Pandey, C. Tibbets, T. Inagami, Structure of rat atrial factor precursor deduced from c DNA sequence, ibid. 309: 722-724 (1984); R.A. Zivin, J.H. Condra, R.A.F. Dixon, N.G. Seidah, M. Chretien, M. Nemer, Molecular cloning and characterization of DNA sequences encoding rat and human atrial natriuretic factors. Proc. Natl. Acad. Sci. U.S. 81: 6325-6329 (1984); N.G. Seidah, C. Lazure, M. Chretien, G. Thibault, R. Garcia, M. Cautin, J. Genest, R.F. Nutt, S.T. Brady, T.A. Lyle, W.J. Paleveda, C.D. Colton, T.M. Cicerone, D.F. Veber, Amino acid sequence of homologous rat atrial peptides: natriuretic activity of native and synthetic forms, ibid. 81: 2640-2644 (1984); C.E. Seidman, A.D. Duby, E. Choi, R.M. Graham, E. Haber, C. Honey, J.G. Seidman, The structure of rat preproatrial natriuretic factor as defined by a complementary DNA sequence. Science 225: 324-326 (1984).CrossRefGoogle Scholar

Copyright information

© Spinger-Verlag Berlin Heidelberg 1991

Authors and Affiliations

  • Theodor Wieland
    • 1
  • Miklos Bodanszky
    • 2
  1. 1.Max-Planck-Institut für Medizinische ForschungHeidelbergGermany
  2. 2.PrincetonUSA

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