Biosynthesis of regulatory peptides — evolutionary aspects

  • J. Michael Conlon

Abstract

Neurohormonal peptides, in common with most peptides/proteins that are designated for export from the cell, are synthesized as higher-molecular-weight precursors which usually have no or reduced biological activity. The conversion to the mature secreted forms of the peptides involves limited proteolysis and frequently post-translational modifications to individual amino acid residues. Determination of a biosynthetic pathway requires a collaboration between the molecular biologist and the protein chemist. The primary structure of the primary gene product (preprohormone) is now determined, almost without exception, indirectly from the nucleotide sequence of cloned DNAs complementary to the mRNA directing synthesis of the hormone or from the nucleotide sequence of a cloned segment of DNA containing the gene isolated from an appropriate genomic library. In order to construct a processing pathway, it is necessary to isolate from a natural source the hormone and the other peptide fragment derived from the precursor and to determine their primary structures. Amino acid sequence analysis is usually carried out using the technique of automated gas-phase Edman degradation. Post-translational modification to individual amino acids may be identified most readily using the technique of fast-atom bombardment mass spectrometry. A comparison of the predicted structure of the preprohormone with the observed structures of the major peptide fragments derived from the precursor enables the identification of the sites of proteolytic cleavage.

Keywords

Pancreatic Polypeptide Coho Salmon Regulatory Peptide Processing Site Fast Atom Bombardment Mass Spectrometry 
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. Andrews, P.C. and Dixon, J.E. (1981) Isolation and structure of a peptide hormone predicted from an mRNA sequence. A second somatostatin from the catfish pancreas. J. Biol. Chem., 256, 8267–70.Google Scholar
  2. Andrews, P.C. and Dixon, J.E. (1986) Isolation and structure of the second of two major peptide products from the precursor to an anglerfish peptide homologous to neuropeptide Y. J. Biol. Chem., 261, 8674–7.Google Scholar
  3. Andrews, P.C., Brayton, K. and Dixon, J.E. (1987a) Precursors to regulatory peptides: their proteolytic processing. Experientia, 43, 784–90.CrossRefGoogle Scholar
  4. Andrews, P.C., Hawke, D.H., Lee, T.D., Legesse, K., Noe, B.D. and Shively, J.E. (1986) Isolation and structure of the principal products of preproglucagon processing, including an amidated glucagon-like peptide. J. Biol. Chem., 261, 8128–33.Google Scholar
  5. Andrews, P.C., Hawke, D., Shively, J.E. and Dixon, J.E. (1984) Anglerfish preprosomatostatin is processed to somatostatin-28 and contains hydroxylysine at residue 23. J. Biol. Chem., 259, 15021–5.Google Scholar
  6. Andrews, P.C., Hawke, D., Shively, J.E. and Dixon, J.E. (1985) A nonamidated peptide homologous to porcine peptide YY and neuropeptide YY. Endocrinology, 116, 2677–81.CrossRefGoogle Scholar
  7. Andrews, P.C., Nichols, R. and Dixon, J.E. (1987b) Post-translational processing of preprosomatostatin-II examined using fast atom bombardment mass spectrometry. J. Biol. Chem., 262, 12692–9.Google Scholar
  8. Andrews, P.C. and Ronner, P. (1985) Isolation and structures of glucagon and glucagon-like peptide from catfish pancreas. J. Biol. Chem., 260, 3910–14.Google Scholar
  9. Argos, P., Taylor, W.L., Minth, C.D. and Dixon, J.E. (1983) Nucleotide and amino acid sequence comparisons of preprosomatostatins. J. Biol. Chem., 258, 8788–93.Google Scholar
  10. Bataille, D., Coudray, A.M., Carlqvist, M., Rosselin, G. and Mutt, V. (1982) Isolation of glucagon-37 (bioactive enteroglucagon/oxyntomodulin) from porcine jejuno-ileum. FEBS Lett., 146, 73–8.CrossRefGoogle Scholar
  11. Bell, G.I. (1986) The glucagon super family: precursor structure and gene organization. Peptides, 7 (Suppl. 1), 27–36.CrossRefGoogle Scholar
  12. Bell, G.I., Sanchez-Pescador, R., Laybourn, P.J. and Najarian, R.C. (1983a). Exon duplication and divergence in the human preproglucagon gene. Nature, Lond., 304, 368–71.CrossRefGoogle Scholar
  13. Bell, G.I., Santerre, R.F. and Mullenbach, G.T. (1983b) Hamster preproglucagon contains the sequence of glucagon and two related peptides. Nature, Lond., 302, 716–18.CrossRefGoogle Scholar
  14. Bennett, H.P.J., Browne, C.A. and Solomon, S. (1981) Biosynthesis of phosphorylated forms of corticotropin-related peptides. Proc. Natl. Acad. Sci. U.S.A., 78, 4713–17.CrossRefGoogle Scholar
  15. Benoit, R., Böhlen, P., Esch, F. and Ling, N. (1984) Neuropeptides derived from prosomatostatin that do not contain the somatostatin-14 sequence. Brain Res., 311, 23–9.CrossRefGoogle Scholar
  16. Benoit, R., Böhlen, P., Ling, N., Briskin, A., Esch, F., Brazzeau, P., Ying, S.-Y. and Guillemin, R. (1982) Presence of somatostatin-28-(l–12) in hypothalamus and pancreas. Proc. Natl. Acad. Sci. U.S.A., 79, 917–21.CrossRefGoogle Scholar
  17. Blobel, G. and Dobberstein, B. (1975) Transfer of proteins across membranes. J. Cell Biol., 67, 835–51.CrossRefGoogle Scholar
  18. Boel, E., Schwartz, T.W., Norris, K.E. and Fiil, N.P. (1984) A cDNA encoding a small common precursor for human pancreatic polypeptide and pancreatic icosapeptide. EMBO J., 3, 909–12.Google Scholar
  19. Conlon, J.M., Agoston, D.V. and Thim, L. (1985a) An elasmobranchian somatostatin: Primary structure and tissue distribution in Torpedo marmorata. Gen. Comp. Endocrinol., 60, 406–13.CrossRefGoogle Scholar
  20. Conlon, J.M., Askensten, U., Falkmer, S. and Thim, L. (1988) Primary structures of somatostatins from the islet organ of the hagfish suggest an anomalous pathway of post-translational processing of prosomatostatin-1. Endocrinology, 122, 1855–59.CrossRefGoogle Scholar
  21. Cordon, J.M., Ballmann, M. and Lamberts, R. (1985b) Regulatory peptides (glucagon, somatostatin, substance P, and VIP) in the brain and gastrointestinal tract of Ambystoma mexicanum. Gen. Comp. Endocrinol., 58, 150–58.CrossRefGoogle Scholar
  22. Conlon, J.M., Dafgard, E., Falkmer, S. and Thim, L. (1987a) A glucagon-like peptide, structurally related to mammalian oxyntomodulin, from the pancreas of a holocephalan fish, Hydrolagus colliei. Biochem.J., 245, 851–5.Google Scholar
  23. Conlon, J.M., Davis, M.S., Falkmer, S. and Thim, L. (1987b) Structural characterization of peptides derived from prosomatostatins I and II isolated from the pancreatic islets of two species of teleostean: the daddy sculpin and the flounder. Eur. J. Biochem., 168, 647–52.CrossRefGoogle Scholar
  24. Conlon, J.M., Davis, M.S. and Thim, L. (1987c) Primary structure of insulin and glucagon from the flounder (Platichthys flesus). Gen. Comp. Endocrinol., 66, 203–9.CrossRefGoogle Scholar
  25. Conlon, J.M., Eriksson, B., Grimelius, L., Öberg, K. and Thim, L. (1987d) Characterization of three peptides derived from prosomatostatin prosomatostatin-(l–63)-, -(65–76)- and -(79–92)-peptide in a human pancreatic tumour. Biochem.J., 248, 123–7.Google Scholar
  26. Conlon, J.M., Falkmer, S. and Thim, L. (1987e) Primary structures of three fragments of proglucagon from the pancreatic islets of the daddy sculpin (Cottus scorpius). Eur. J. Biochem., 164, 117–22.CrossRefGoogle Scholar
  27. Conlon, J.M., Hansen, H.F. and Schwartz, T.W. (1985c) Primary structure of glucagon and a partial sequence of oxyntomodulin (glucagon-37) from the guinea pig. Regul. Pept., 11, 309–20.CrossRefGoogle Scholar
  28. Conlon, J.M., Hansen, H.F. and Schwartz, T.W. (1985d) A truncated glucagon-like peptide from Torpedo pancreas. Regul. Pept., 13, 94.CrossRefGoogle Scholar
  29. Conlon, J.M., Hansen, H.F. and Schwartz, T.W. (1985d) A truncated glucagon-like peptide from Torpedo pancreas. Regul. Pept., 13, 94.CrossRefGoogle Scholar
  30. Conlon, J.M. and McCarthy, D.M. (1984) Fragments of prosomatostatin isolated from a human pancreatic tumour. Molec. Cell. Endocrinol., 38, 81–6.CrossRefGoogle Scholar
  31. Conlon, J.M., O’Toole, L. and Thim, L. (1987f) Primary structure of glucagon from the gut of the common dogfish (Scyliorhinus canicula). FEBS Lett., 214, 50–6.CrossRefGoogle Scholar
  32. Conlon, J.M., Schmidt, W.E., Gallwitz, B., Falkmer, S. and Thim, L. (1986) Characterization of an amidated form of pancreatic polypeptide from the daddy sculpin (Cottus scorpius). Regul. Pept., 16, 261–8.CrossRefGoogle Scholar
  33. Conlon, J.M. and Thim, L. (1985) Primary structure of glucagon from an elasmobranchian fish, Torpedo marmorata. Gen. Comp. Endocrinol., 60, 398–405.CrossRefGoogle Scholar
  34. Conlon, J.M., Thim, L., Moody, A.J. and Soling, D. (1984) Cyclic-AMP-dependent phosphorylation of glicentin. Biosci. Rep., 4, 489–96.CrossRefGoogle Scholar
  35. Cutfield, F., Cutfield, S.M., Carne, A., Emdin, S.O. and Falkmer, S. (1986) The isolation, purification and amino-acid squence of insulin from the teleost fish Cottus scorpius (daddy sculpin). Eur. J. Biochem., 158, 117–23.CrossRefGoogle Scholar
  36. Cutfield, S.M., Carne, A. and Cutfield, J.F. (1987) The amino-acid sequences of sculpin islet somatostatin-28 and peptide YY. FEBS Lett., 214, 57–61.CrossRefGoogle Scholar
  37. Davidson, H.W., Peshavaria, M. and Hutton, J.C. (1987) Proteolytic conversion of proinsulin into insulin. Identification of a Ca2+-dependent acidic endopeptidase in isolated insulin-secretory granules. Biochem. J., 246, 279–86.Google Scholar
  38. Dockray, G.J., Varro, A., Desmond, H., Young, J. and Gregory, H. (1987) Post-translational processing of the porcine gastrin precursor by phosphorylation of the COOH-terminal fragment. J. Biol. Chem., 262, 8643–7.Google Scholar
  39. Douglass, J., Civelli, O. and Herbert, E. (1984) Polyprotein gene expression: generation of diversity of neuroendocrine peptides. Annu. Rev. Biochem., 53, 665–715.CrossRefGoogle Scholar
  40. Duve, H., Thorpe, A., Lazarus, N.R. and Lowry, P.J. (1982) A neuropeptide of the blowfly Calliphora vomitoria with an amino acid composition homologous with vertebrate pancreatic polypeptide. Biochem. J., 201, 429–32.Google Scholar
  41. Evans, E.A., Gilmore, R. and Blobel, G. (1986) Purification of microsomal signal peptidase as a complex. Proc. Natl. Acad. Sci. U.S.A., 83, 581–4.CrossRefGoogle Scholar
  42. Falkmer, S. (1985) Comparative morphology of pancreatic islets in animals. In The Diabetic Pancreas, 2nd edn (eds B.W. Volk and E.R. Arquilla), Plenum, New York, pp. 17–52.Google Scholar
  43. Falkmer, S. and Van Noorden, S. (1983) Ontogeny and phylogeny of the glucagon cell. Handb. Exp. Pharmacol., 66(1), 81–119.Google Scholar
  44. Fletcher, D.J., Quigley, J.P., Bauer, G.E. and Noe, B.D. (1981) Characterization of proinsulin- and proglucagon-converting activities in isolated islet secretory granules. J. Cell Biol., 90, 312–22.CrossRefGoogle Scholar
  45. Frandsen, E.K., Gronvald, F.C., Heding, L.G., Johansen, N.L., Lundt, B.F., Moody, A.J., Markussen, J. and Volund, A. (1981) Glucagon: structure-function relationship investigated by sequence deletions. Hoppe-Seyler’s Z. Physiol. Chem., 362, 665–77.Google Scholar
  46. Gafvelin, G., Carlqvist, M. and Mutt, V. (1985) A preform of secretin with high secretin-like bioactivity. FEBS Lett., 184, 347–52.CrossRefGoogle Scholar
  47. Geisow, M.J. (1978) Polypeptide secondary structure may direct the specificity of prohormone conversion. FEBS Lett., 87, 111–14.CrossRefGoogle Scholar
  48. Glembotski, C.C., Eipper, B.A. and Mains, R.E. (1984) Characterization of a peptide a-amidation activity from rat anterior pituitary. J. Biol. Chem., 259, 6385–92.Google Scholar
  49. Gluschankof, P., Morel, A., Gomez, S., Nicolas, P., Fahy, C. and Cohen, P. (1984) Enzymes processing somatostatin-precursors: An Arg-Lys esteropeptidase from rat brain cortex converting somatostatin-28 into somatostatin-14. Proc. Natl. Acad. Sci. U.S.A., 81, 6662–6.CrossRefGoogle Scholar
  50. Goodman, R.H., Aron, D.C. and Roos, B.A. (1983) Rat pre-prosomatostatin. Structure and processing by microsomal membranes. J. Biol. Chem., 258, 5570–73.Google Scholar
  51. Goodman, R.H., Jacobs, J.W., Chin, W.W., Lund, P.K., Dee, P.C. and Habener, J.F. (1980) Nucleotide sequence of a cloned structural gene coding for a precursor of pancreatic somatostatin. Proc. Natl. Acad. Sci. U.S.A., 77, 5869–73.CrossRefGoogle Scholar
  52. Heinrich, G., Gros, P. and Habener, J.F. (1984) Glucagon gene sequence: four of six exons encode separate functional domains of rat pre-proglucagon. J. Biol. Chem., 259, 14082–7.Google Scholar
  53. Hobart, P., Crawford, R., Shen, L.P., Pictet, R. and Rutter, W.J. (1980) Cloning and sequence analysis of cDNAs encoding two distinct somatostatin precursors found in the endocrine pancreas of anglerfish. Nature, Lond., 288, 137–41.CrossRefGoogle Scholar
  54. Hoist, J.J., Orskov, C., Vagn Nielsen, O. and Schwartz, T.W. (1987) Truncated glucagon-like peptide I, an insulin-releasing hormone from the distal gut. FEBS Lett., 211, 169–74.CrossRefGoogle Scholar
  55. Hook, V. Y.H. and La Gamma, E. (1987) Product inhibition of carboxypeptidase H. J. Biol. Chem., 262, 12583–8.Google Scholar
  56. Hook, V.Y.H. and Loh, Y.P. (1984) Carboxypeptidase B-like converting enzyme activity in secretory granules of rat pituitary. Proc. Natl. Acad. Sci. U.S.A., 81, 2776–80.CrossRefGoogle Scholar
  57. Hoosein, N.M., Mahrenholz, A.M., Andrews, P.C. and Gurd, R.S. (1987) Biological activities of catfish glucagon and glucagon-like peptide. Biochem. Biophys. Res. Commun., 143, 87–92.CrossRefGoogle Scholar
  58. Inouye, S., Soberon, X., Franceschini, T., Nakamura, K., Itakura, K. and Inouye, M. (1982) Role of positive change on the ammo-terminal region of the signal peptide in protein secretion across the membrane. Proc. Natl. Acad. Sci. U.S.A., 79, 3438–42.CrossRefGoogle Scholar
  59. Julius, D., Brake, A., Blair, L., Kunisawa, R. and Thorner, J. (1984) Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-α-factor. Cell, 37, 1075–89.CrossRefGoogle Scholar
  60. Kimmel, J.R., Plisetskaya, E.M., Pollock, H.G., Hamilton, J.W., Rouse, J.B., Ebner, K.E. and Rawitch, A.B. (1986) Structure of a peptide from salmon endocrine pancreas with homology to neuropeptide Y. Biochem. Biophys. Res. Commun., 141, 1084–91.CrossRefGoogle Scholar
  61. Kimmel, J.R., Pollock, H.G., Chance, R.E., Johnson, M.G., Reeve, J.R., Taylor, L., Miller, C. and Shively, J.E. (1984) Pancreatic polypeptide from rat pancreas. Endocrinology, 114, 1725–31.CrossRefGoogle Scholar
  62. Leiter, A.B., Montminy, M.R., Jamieson, E. and Goddman, R.H. (1985) Exons of the human pancreatic polypeptide gene define functional domains in the precursor. J. Biol. Chem., 260, 13013–17.Google Scholar
  63. Loh, Y.P., Brownstein, M.J. and Gainer, H. (1984) Proteolysis in neuropeptide processing and other neural functions. Annu. Rev. Neurosci., 7, 189–222.CrossRefGoogle Scholar
  64. Lopez, L.C., Frazier, M.L., Su, C.-J., Kumar, A. and Saunders, G.F. (1983) Mammalian pancreatic preproglucagon contains three glucagon-related peptides. Proc. Natl. Acad. Sci. U.S.A., 80, 5485–9.CrossRefGoogle Scholar
  65. Lopez, L.C., Li, W.-H., Frazier, M.L., Luo, C.-C. and Saunders, G.F. (1984) Evolution of glucagon genes. Molec. Biol. Evol., 1, 335–44.Google Scholar
  66. Lund, P.K., Goodman, R.H., Dee, P.C. and Habener, J.F. (1982) Pancreatic preproglucagon cDNA contains two glucagon-related coding sequences arranged in tandem. Proc. Natl. Acad. Sci. U.S.A., 79, 3345–9.CrossRefGoogle Scholar
  67. Lund, P.K., Goodman, R.H., Montminy, M.R., Dee, P.C. and Habener, J.F. (1983) Anglerfish islet pre-proglucagon II. Nucleotide and corresponding amino acid sequence of the cDNA. J. Biol. Chem., 258, 3280–84.Google Scholar
  68. Magazin, M., Minth, C.D., Funckes, C.L., Deschenes, R., Tavianini, M. and Dixon, J.E. (1982) Sequence of a cDNA encoding pancreatic pre-prosomatostatin-22. Proc. Natl. Acad. Sci. U.S.A., 79, 5152–6.CrossRefGoogle Scholar
  69. Minth, C.D., Taylor, W.L., Magazin, M., Tavianini, M.A., Collier, K., Weith, H.L. and Dixon, J.E. (1982) The structure of cloned DNA complementary to catfish pancreatic somatostatin-14 messenger RNA. J. Biol. Chem., 257, 10372–7.Google Scholar
  70. Mizuno, K. and Matsuo, H. (1984) A novel protease from yeast with specificity towards paired basic residues. Nature, Lond., 309, 558–60.CrossRefGoogle Scholar
  71. Mojsov, S., Heinrich, G., Wilson, I.B., Ravazzola, M., Orci, L. and Habener, J.F. (1986) Preproglucagon gene expression in pancreas and intestine diversifies at the level of post-translational processing. J. Biol. Chem., 261, 11880–89.Google Scholar
  72. Mommsen, T.P., Andrews, P.C. and Plisetskaya, E.M. (1987) Glucagon-like peptides activate hepatic gluconeogenesis. FEBS Lett., 219, 227–32.CrossRefGoogle Scholar
  73. Morel, A., Chang, J.-Y. and Cohen, P. (1984) The complete amino-acid sequence of anglerfish somatostatin-28. II. A new octacosapeptide containing the (Tyr7 Gly10; derivative of somatostatin-14. FEBS Lett., 175, 21–4.CrossRefGoogle Scholar
  74. Munck, A., Kervran, A., Marie, J.-C., Bataille, D. and Rosselin, G. (1984) Glucagon-37 (oxyntomodulin) and glucagon-29 (pancreatic glucagon) in human bowel: Analysis by HPLC and radioreceptor assay. Peptides, 5, 553–61.CrossRefGoogle Scholar
  75. Nielsen, H.V., Gether, U. and Schwartz, T.W. (1986) Cat pancreatic eicosapeptide and its biosynthetic intermediate. Conversion of a monobasic processing site. Biochem. J., 240, 69–74.Google Scholar
  76. Noe, B.D., Andrews, P.C., Dixon, J.E. and Spiess, J. (1986) Cotranslational and posttranslational proteolytic processing of preprosomatostatin-I in intact islet tissue. J. Cell Biol., 103, 1205–11.CrossRefGoogle Scholar
  77. Noe, B.D., Debo, G. and Spiess, J. (1984) Comparison of prohormone-processing activities in islet microsomes and secretory granules: evidence for distinct converting enzymes for separate islet prosomatostatins. J. Cell Biol., 19, 578–87.CrossRefGoogle Scholar
  78. Parish, D.C., Tuteja, R., Altstein, M., Gainer, H. and Loh, Y.P. (1986) Purification and characterization of paired basic residue-specific prohormone-converting enzyme from bovine pituitary neural lobe secretory vesicles. J. Biol. Chem., 261, 14392–6.Google Scholar
  79. Patzelt, C. and Schiltz, E. (1984) Conversion of proglucagon in pancreatic alpha cells: The major end products are glucagon and a single peptide, the major proglucagon fragment, that contains two glucagon-like sequences. Proc. Natl. Acad. Sci. U.S.A., 81, 5007–11.CrossRefGoogle Scholar
  80. Plisetskaya, E.M., Pollock, H.G., Rouse, J.B., Hamilton, J.W., Kimmel, J.R., Andrews, P.C. and Gorbman, A. (1986a) Characterization of coho salmon (Oncorhynchuskisutch) islet somatostatins. Gen. Comp. Endocrinol., 63, 252–63.CrossRefGoogle Scholar
  81. Plisetskaya, E.M., Pollock, H.G., Rouse, J.B., Hamilton, J.W., Kimmel, J.R. and Gorbman, A. (1986b) Isolation and structures of coho salmon (Oncorhynchus kisutch) glucagon and glucagon-like peptide. Regul. Pept., 14, 57–67.CrossRefGoogle Scholar
  82. Pollock, H.G., Kimmel, J.R., Hamilton, J.W., Rouse, J.B., Ebner, K.E., Lance, V. and Rawitch, A.B. (1987) Isolation and structure of Alligator Gar (Lepisosteus spatula) insulin and pancreatic polypeptide. Gen. Comp. Endocrinol., 67, 375–82.CrossRefGoogle Scholar
  83. Pradayrol, L., Jömvall, H., Mutt, V. and Ribet, A. (1980) N-terminally extended somatostatin: the primary structure of somatostatin-28. FEBS Lett., 109, 55–8.CrossRefGoogle Scholar
  84. Rholam, M., Nicolas, P. and Cohen, P. (1986) Precursors for peptide hormones share common secondary structures forming features at the proteolytic processing sites. FEBS Lett., 207, 1–6.CrossRefGoogle Scholar
  85. Schaefer, M., Picciotto, M.R., Kreiner, T., Kaldany, R.-R., Taussig, R. and Scheller, R.H. (1985) Aplysia neurons express a gene encoding multiple FMRF amide neuropeptides. Cell, 41, 457–67.CrossRefGoogle Scholar
  86. Schmidt, W.E., Mutt, V., Kratzin, H., Carlquist, M., Conlon, J.M. and Creutzfeldt, W. (1985) Isolation and characterization of proSSt1–32’ a peptide derived from the N- terminal region of porcine preprosomatostatin. FEBS Lett., 192, 141–6.CrossRefGoogle Scholar
  87. Schwartz, T.W. (1986) The processing of peptide precursors: ‘Proline-directed arginyl cleavage’ and other monobasic processing mechanisms. FEBS Lett., 200, 1–10.CrossRefGoogle Scholar
  88. Schwartz, T.W. and Hansen, H.F. (1984) Isolation of ovine pancreatic icosapeptide: a peptide product containing one cysteine residue. FEBS Lett., 168, 293–8.CrossRefGoogle Scholar
  89. Schwartz, T.W., Hånsen, H.F., Hakanson, R., Sundler, F. and Tager, H.S. (1984) Human pancreatic icosapeptide: isolation, sequence and immuno-histochemical localization of the COOH-terminal fragment of the pancreatic polypeptide precursor. Proc. Natl. Acad. Sci. U.S.A., 81, 708–12.CrossRefGoogle Scholar
  90. Schwartz, T.W. and Tager, H.S. (1981) Isolation and biogenesis of a new peptide from pancreatic islets. Nature, Lond., 294, 589–91.CrossRefGoogle Scholar
  91. Seino, S., Welsh, M., Bell, G.I., Chan, S.J. and Steiner, D.F. (1986) Mutations in the guinea pig preproglucagon gene are restricted to a specific portion of the prohormone sequence. FEBS Lett., 203, 25–30.CrossRefGoogle Scholar
  92. Shen, L.-P., Pictet, R.L. and Rutter, W.J. (1982) Human somatostatin I: sequence of the cDNA. Proc. Natl. Acad. Sci. U.S.A., 79, 4575–9.CrossRefGoogle Scholar
  93. Shen, L.-P. and Rutter, W.J. (1984) Sequence of the human somatostatin gene. Science, 244, 168–71.CrossRefGoogle Scholar
  94. Spiess, J. and Noe, B.D. (1985) Processing of an anglerfish somatostatin precursor to a hydroxylysine-containing somatostatin-28. Proc. Natl. Acad. Sci. U.S.A., 82, 277–81.CrossRefGoogle Scholar
  95. Stefan, Y., Ravazzola, M. and Orci, L. (1981) Primitive islets contain two populations of cells with differing glucagon immunoreactivity. Diabetes, 30, 192–5.CrossRefGoogle Scholar
  96. Steiner, D.F., Kemmler, W., Tager, H.S. and Peterson, J.P. (1974) Proteolytic processing in the biosynthesis of insulin and other proteins. Fed. Proc., 33, 2105–15.Google Scholar
  97. Stensiö, E. (1968) The cyclostome with special reference to the diphyletic origin of the Petromyzontida and Myxinoidea. 4th Nobel Symp., 13–71.Google Scholar
  98. Sundby, F. (1976) Species variations in the primary structure of glucagon. Metabolism (Suppl. 1), 25, 1319–21.CrossRefGoogle Scholar
  99. Tager, H.S. and Steiner, D.F. (1973) Isolation of a glucagon-containing peptide: Primary structure of a possible fragment of proglucagon. Proc. Natl. Acad. Sci. U.S.A., 70, 2321–5.CrossRefGoogle Scholar
  100. Takeuchi, T. and Yamada, T. (1985) Isolation of a cDNA clone encoding pancreatic polypeptide. Proc. Natl. Acad. Sci. U.S.A., 82, 1536–9.CrossRefGoogle Scholar
  101. Tavianini, M.A., Hayes, T.E., Magazin, M.D., Minth, C.D. and Dixon, J.E. (1984) Isolation, characterization and DNA sequence of the rat somatostatin gene. J. Biol. Chem., 259, 11798–803.Google Scholar
  102. Tatemoto, K. (1982) Isolation and characterization of peptide YY (PYY), a candidate gut hormone that inhibits pancreatic exocrine secretion. Proc. Natl. Acad. Sci. U.S.A., 79, 2514–18.CrossRefGoogle Scholar
  103. Tatemoto, K., Carlquist, M. and Mutt, V. (1982) Neuropeptide Y- a novel brain peptide with structural similarities to peptide YY and pancreatic polypeptide. Nature, Lond., 296, 659–60.CrossRefGoogle Scholar
  104. Thim, L., Hansen, M.T., Norris, K., Hoegh, I., Boel, E., Forstrom, J., Ammerer, G. and Fiil, N. (1986) Secretion and processing of insulin precursors in yeast. Proc. Natl. Acad. Sci. U.S.A., 83, 6766–70.CrossRefGoogle Scholar
  105. Thim, L. and Moody, A.J. (1982) Purification and chemical characterization of a glicentin-related pancreatic peptide (proglucagon fragment) from porcine pancreas. Biochim. Biophys. Acta., 703, 134–41.CrossRefGoogle Scholar
  106. Uy, R. and Wold, F. (1977) Posttranslational covalent modification of protein. Science, 198, 890–96.CrossRefGoogle Scholar
  107. von Heijne, G. (1983) Patterns of amino acids near signal-sequence cleavage sites. Eur. J. Biochem., 133, 17–21.CrossRefGoogle Scholar
  108. Wallace, E.F., Weber, E., Barchas, J.D. and Evans, C.J. (1984) A putative processing enzyme from Aplysia that cleaves dynorphin A at the single arginine residue. Biochem. Biophys. Res. Commun., 119, 415–22.CrossRefGoogle Scholar
  109. Wold, F.A. (1981) In vivo chemical modification of proteins (post-translational modification). Annu. Rev. Biochem., 50, 783–814.CrossRefGoogle Scholar
  110. Wolfe, P.B. and Wickner, W. (1984) Bacterial leader peptidase, a membrane protein without a leader peptide, uses the same export pathway as pre-secretory proteins. Cell, 36, 1067–72.CrossRefGoogle Scholar
  111. Yamamoto, H., Nata, K. and Okamoto, H. (1986) Mosaic evolution of prepropancreatic polypeptide. J. Biol. Chem., 261, 6156–9Google Scholar

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  • J. Michael Conlon

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