Pro-GnRH processing

Progress in Brain Research

Volumn 141, Issue , 2002, Pages 221-241

  Wetsel, William C ^a   Srinivasan, Sudha ^a  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYPEPTIDASE; ENZYME; FURIN; GLUTAMINYL CYCLASE; GONADORELIN; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

ADENOHYPOPHYSIS; AMINO ACID SEQUENCE; CONFERENCE PAPER; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; PLEIOTROPY; PRIORITY JOURNAL; PROTEIN PROCESSING; TISSUE DISTRIBUTION;

EID: 0036458082     PISSN: 00796123     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0079-6123(02)41096-5     Document Type: Conference Paper

References (189)

1. Ackland, J.F., Nikolics, K., Seeburg, P.H. et al. (1988) Molecular forms of gonadotropin-releasing hormone associated peptide (GAP): Changes within the rat hypothalamus and release from hypothalamic cells in vitro. Neuroendocrinology, 48: 376-386.
2. Adelman, J.P., Mason, A.J., Hayflick, J.S. et al. (1986) Isolation of the gene and hypothalamic cDNA for the common precursor of gonadotropin-releasing hormone and prolactin release-inhibiting factor in human and rat. Proc. Natl. Acad. Sci. USA, 83: 179-183.
3. Allen, R.G., Peng, B., Pellegrino, M.J. et al. (2001) Altered processing of pro-orphanin FQ/nociceptin and proopiomelanocortin-derived peptides in the brains of mice expressing defective prohormone convertase 2. J. Neurosci., 21: 5864-5870.
4. Aloy, P., Companys, V., Vendrell, J. et al. (2001) The crystal structure of the inhibitor-complexed carboxypeptidase D domain II and the modeling of regulatory carboxypeptidases. J. Biol. Chem., 276: 16177-16184.
5. Amico, J.A. and Hempel, J. (1990) An oxytocin precursor intermediate circulates in the plasma of humans and rhesus monkeys administered estrogen. Neuroendocrinology, 51: 437-443.
6. Aschner, B. (1912) Ueber die fuktion der hypophyse. Pfluegers Arch. Ges. Physiol., 146: 1-7.
7. Bergeron, F., Leduc, R. and Day, R. (2000) Subtilase-like proprotein convertases: From molecular specificity to therapeutic applications. J. Mol. Endocrinol., 24: 1-22.
8. Berman, Y., Mzhavia, N., Polonskaia, A. et al. (2000) Defective prodynorphin processing in mice lacking prohormone convertase PC2. J. Neurochem., 75: 1763-1770.
9. Bogerd, J., Zandbergen, T., Andersson, E. et al. (1994) Isolation, characterization and expression of cDNAs encoding the catfish-type and chicken-II-type gonadotropin-releasing hormone precursors in the African catfish. Eur. J. Biochem., 222: 541-549.
10. Bourguignon, J.P., Alvarez Gonzalez, M.L. et al. (1994) Gonadotropin releasing hormone inhibitory autofeedback by subproducts antagonist at N-methyl-D-aspartate receptors: A model of autocrine regulation of peptide secretion. Endocrinology, 134: 1589-1592.
11. Bradbury, A.F., Finnie, D.A. and Smyth, D.G. (1982) Mechanism of C-terminal amide formation by pituitary enzymes. Nature, 298: 686-688.
12. Braks, J.A. and Martens, G.J. (1994) 7B2 is a neuroendocrine chaperone that transiently interacts with prohormone convertase PC2 in the secretory pathway. Cell, 78: 263-273.
13. Bruder, J.M., Krebs, W.D., Nett, T.M. et al. (1992) Phorbol ester activation of the protein kinase C pathways inhibits gonadotropin-releasing hormone gene expression. Endocrinology, 131: 2552-2558.
14. Bruzzaniti, A., Goodge, K., Jay, P. et al. (1996) PC8, a new member of the convertase family. Biochem. J., 314: 727-731.
15. Burgus, R., Butcher, M., Amoss, M. et al. (1972) Primary structure of ovine luteinizing hormone-releasing factor (LRF). Proc. Natl. Acad. Sci. USA, 69: 278-282.
16. Busby, W.H. Jr., Quackenbush, G.E., Humm, J. et al. (1987) An enzyme(s) that converts glutaminyl-peptides into pyroglutamyl-peptides. Presence in pituitary, brain, adrenal medulla, and lymphocytes. J. Biol. Chem., 262: 8532-8536.
17. Campbell, H.J., Feuer, G. and Harris, G.W. (1964) The effect of intrapituitary infusion of median eminence and other brain extracts on anterior pituitary gonadotropic secretion. J. Physiol. (Lond.), 170: 474-486.
18. Carolsfeld, J., Powell, J.F.F., Park, M. et al. (2000) A novel form of gonadotropin-releasing hormone (GnRH) in herring sheds light on evolutionary pressures. Endocrinology, 141: 505-512.
19. Cattanach, B.M., Iddon, C.A., Charlton, H.M. et al. (1977) Gonadotropin-releasing hormone deficiency in a mutant mouse with hypogonadism. Nature, 269: 338-340.
20. Chandrashekar, V., Bartke, A. and Browning, R.A. (1988) Assessment of the effects of a synthetic gonadotropin-releasing hormone associated peptide on hormone release from the in situ and ectopic pituitaries in adult male rats. Brain Res. Bull., 21: 95-99.
21. Chen, A., Yahalom, D., Ben-Aroya, N. et al. (1998) A second isoform of gonadotropin-releasing hormone is present in the brain of human and rodents. FEBS Lett., 435: 199-203.
22. Chen, H., Jawahar, S., Qian, Y. et al. (2001) Missense polymorphism in the human carboxypeptidase E gene alters enzymatic activity. Human Mutat., 18: 120-131.
23. Chen, Y., Wong, M. and Moss, R.L. (1993) Effects of a biologically active LHRH fragment on CA1 hippocampal neurons. Peptides, 14: 1079-1081.
24. Chertow, B.S. (1981) The role of lysosomes and proteases in hormone secretion and degradation. Endocr. Rev., 2:137-173.
25. Clarke, I.J., Cummins, J.T., Karsch, F.J. et al. (1987) GnRH-associated peptide (GAP) is cosecreted with GnRH into the hypophyseal portal blood of ovariectomized sheep. Biochem. Biophys. Res. Commun., 143: 665-671.
26. Coleman, D.L. and Eichler, E.M. (1990) Fat (fat) and tubby (tub): Two autosomal recessive mutations causing obesity syndromes in mice. J. Hered., 81: 424-427.
27. Constam, D.B. and Robertson, E.J. (2000) SPC4/PACE4 regulates a TGF-beta signaling network during axis formation. Genes Dev., 14: 1146-1155.
28. Cravatt, B.F., Prospero-Garcia, O., Siuzdak, G. et al. (1995) Chemical characterization of a family of brain lipids that induce sleep. Science, 268: 1506-1509.
29. Culler, M.D., Culler, M.D., Wetsel, W.C. et al. (1987) Orchidectomy induces temporal and regional changes in the synthesis and processing of the LHRH prohormone in the rat brain. In: V.B. Mahesh, D.S. Dhindsa, E. Anderson and S.P. Kalra (Eds.), Regulation of Ovarian and Testicular Function. Plenum Press, New York, pp. 623-628.
30. Dellovade, T.L., King, J.A., Millar, R.P. et al. (1993) Presence and differential distribution of distinct forms of immunoreactive gonadotropin-releasing hormone in the musk shrew brain. Neuroendocrinology, 58: 166-177.
31. Dockray, G.J., Varro, A. and Dimaline, R. (1996) Gastric endocrine cells: Gene expression, processing, and targeting of active products. Physiol. Rev., 76: 767-798.
32. Dong, W., Marcinkiewicz, M., Vieau, D. et al. (1995) Distinct mRNA expression of the highly homologous convertases PC5 and PACE4 in the rat brain and pituitary. J. Neurosci., 15: 1778-1796.
33. Dong, W., Fricker, L.D. and Day, R. (1999) Carboxypeptidase D is a potential candidate to carry out redundant processing functions of carboxypeptidase E is based on comparative distribution studies in the rat central nervous system. Neuroscience, 89: 1301-1317.
34. Douglass, J., Civelli, O. and Herbert, E. (1984) Polyprotein gene expression: Generation of diversity of neuroendocrine peptides. Ann. Rev. Biochem., 53: 665-704.
35. Dunn, I.C., Chen, Y., Hook, C. et al. (1993) Characterization of the chicken preprogonadotropin-releasing hormone-I gene. J. Mol. Endocrinol., 11: 19-29.
36. Eipper, B.A., Mains, R.E. and Glembotski, C.C. (1983) Identification in pituitary tissue of a peptide α-amidation activity that acts on glycine-extended peptides and requires molecular oxygen, copper, and ascorbic acid. Proc. Natl. Acad. Sci. USA, 80: 5144-5148.
37. Eipper, B.A., Park, L.P., Dickerson, I.M. et al. (1987) Structure of the precursor to an enzyme mediating COOH-terminal amidation in peptide biosynthesis. Mol. Endocrinol., 1: 777-790.
38. Eipper, B.A., Stoffers, D.A. and Mains, R.E. (1992a) The biosynthesis of neuropeptides: Peptide α-amidation. Ann. Rev. Neurosci., 15: 57-85.
39. Eipper, B.A., Green, C.B.-R., Campbell, T.A. et al. (1992b) Alternative splicing and endoproteolytic processing generate tissue-specific forms of pituitary peptidylglycine α-amidating monooxygenase (PAM). J. Biol. Chem., 267: 4008-4015.
40. Erdheim, J. and Stumme, E. (1909) Ueber die schwangerschaftsveranderung der hypophyse. Beitr. Pathol. Anat. Allgem. Pathol., 46: 1-4.
41. Feng, Y., Reznik, S.E. and Fricker, L.D. (2001) Distribution of proSAAS-derived peptides in rat neuroendocrine tissues. Neuroscience, 105: 469-478
42. Fernald, R.D. and White, R.B. (1999) Gonadotropin-releasing hormone genes: Phylogeny, structure, and function. Front. Neuroendocrinology, 20: 224-240.
43. Fischer, W.H. and Spiess, J. (1987) Identification of a mammalian glutaminyl cyclase converting glutaminyl into pyroglutamyl peptides. Proc. Natl. Acad. Sci. USA, 84: 3628-3632.
44. Fricker, L.D. (1991) Peptide processing exopeptidases: Amino and carboxypeptidases involved with peptide biosynthesis. In: L.D. Fricker (Ed.), Peptide Biosynthesis and Processing. CRC Press, Boca Raton, pp. 199-229.
45. Fricker, L.D. (1998) Carboxypeptidase E/H. In: A.J. Barrett, N.D. Rawlings, J.F. Woessner (Eds.), Handbook of Proteolytic Enzymes. Academic Press, London, pp. 1341-1344.
46. Fricker, L.D. and Snyder, S.H. (1972) Enkephalin convertase: Purification and characterization of a specific enkephalin-synthesizing carboxypeptidase localized to adrenal chromaffin granules. Proc. Natl. Acad. Sci. USA, 79: 3886-3890.
47. Fricker, L.D., Evans, C.J., Esch, F.S. et al. (1986) Cloning and sequence analysis of cDNA for bovine carboxypeptidase E. Nature, 323: 461-464.
48. Fricker, L.D., Das, B. and Angeletti, R.H. (1990) Identification of the pH-dependent membrane anchor of carboxypeptidase E (EC 3.4.17.10). J. Biol. Chem., 265: 2476-2482.
49. Fricker, L.D., McKinzie, A.A., Sun, J. et al. (2000) Identification and characterization of proSAAS, a granin-like neuroendocrine peptide precursor that inhibits prohormone processing. J. Neurosci., 20: 639-648.
50. Furuta, M., Yano, H., Zhou, A. et al. (1997) Defective prohormone processing and altered pancreatic islet morphology in mice lacking active SPC2. Proc. Natl. Acad. Sci. USA, 94: 6646-6651.
51. Furuta, M., Zhou, A., Webb, G. et al. (2001) Severe defect in proglucagon processing in islet A-cells of prohormone convertase 2 null mice. J. Biol. Chem., 276: 27197-27202.
52. 9]luteinizing hormone-releasing hormone and its smallest precursor forms in immortalized luteinizing hormone-releasing hormone-secreting neurons (GT1-7), and evaluation of their mode of action on pituitary cells. Mol. Cell. Endocrinol., 110: 161-173.
53. Gomis-Rüth, F.X., Companys, V., Qian, Y. et al. (1999) Crystal structure of avian carboxypeptidase D domain II: A prototype for the regulatory metallocarboxypeptidase subfamily. EMBO J., 18: 5817-5826.
54. Gore, A.C. and Roberts, J.L. (1997) Regulation of gonadotropin- releasing hormone gene expression in vivo and in vitro. Front. Neuroendocrinol., 18: 209-245.
55. Gothilf, Y., Elizur, A., Chow, M. et al. (1995) Molecular cloning and characterization of a novel gonadotropin-releasing hormone from the gilthead seabream (Sparus aurata). Mol. Marine Biol. Biotechnol., 4: 27-35.
56. Halasz, B., Pupp, L. and Uhlarik, S. (1962) Hypophysiotrophic area in the hypothalamus. J. Endocrinol., 25: 147-154.
57. Harris, G.W. and Jacobsohn, D. (1952) Functional grafts of anterior pituitary gland. Proc. Roy. Soc. Ser. B, 139: 263-276.
58. Ishibashi, M., Yamaji, T., Takaku, F. et al. (1987) Effect of GnRH-associated peptide on prolactin secretion from human lactotrope adenoma cells in culture. Acta Endocrinol. (Cophen.), 116: 81-84.
59. Jackson, R.S., Creemers, J.W., Ohagi, S. et al. (1997) Obesity and impaired prohormone processing associated with mutations in the human prohormone convertase 1 gene. Nat. Genet., 16: 303-306.
60. Jimenez-Liñan, M., Rubin, B. and King, J.C. (1997) Examination of guinea pig luteinizing hormone-releasing hormone gene reveals a unique decapeptide and existence of two transcripts in the brain. Endocrinology, 138: 4123-4137.
61. Johanning, K., Juliano, M.A., Juliano, L. et al. (1998) Specificity of prohormone convertase 2 on proenkephalin and proenkephalin-related substrates. J. Biol. Chem., 273: 22672- 22680.
62. Julius, D., Brake, A., Blair, L. et al. (1984) Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-alpha-factor. Cell, 37: 1075-1089.
63. +,K(+)-ATPase alpha-subunit gene expression through a novel receptor. J. Biol. Chem., 270: 11155-11160.
64. Kalra, P.S. and Kalra, S.P. (1985) Control of gonadotropin secretion. In: H. Imura (Ed.), The Pituitary Gland. Raven Press: New York, pp. 189-220.
65. Karten, M.J. and Rivier, J.E. (1986) Gonadotropin-releasing hormone analog design. Structure-function studies toward the development of agonists and antagonists: Rationale and perspectives. Endocrine Rev., 7: 44-66.
66. Kasten, T.L., White, S.A., Norton, T.T. et al. (1996) Characterization of two new preproGnRH mRNAs in the tree shrew: First direct evidence for mesencephalic GnRH gene expression in a placental mammal. Gen. Comp. Endocrinol., 104: 7-19.
67. Kato, I., Yonekura, H., Tajima, M., et al. (1990) Two enzymes concerned in peptide hormone alpha-amidation are synthesized from a single mRNA. Biochem. Biophys. Res. Commun., 172: 197-203.
68. Katopodis, A.G. and May, S.W. (1990) Novel substrates and inhibitors of peptidylglycine alpha-amidating monooxygenase. Biochemistry, 29: 4541-4548.
69. Katopodis, A.G., Ping, D. and May, S.W. (1990) A novel enzyme from bovine neurointermediate pituitary catalyzes dealkylation of alpha-hydroxyglycine derivatives, thereby functioning sequentially with peptidylglycine alpha-amidating monooxygenase in peptide amidation. Biochemistry, 29: 6115-6120.
70. Katopodis, A.G., Ping, D.S., Smith, C.E. et al. (1991) Functional and structural characterization of peptidylamidoglycolate lyase, the enzyme catalyzing the second step in peptide amidation. Biochemistry, 30: 6189-6194.
71. Kiefer, M.C., Tucker, J.E., Joh, R. et al. (1991) Identification of a second human subtilisin-like protease gene in the fes/fps region of chromosome 15. DNA Cell Biol., 10: 757-769.
72. King, J.A. and Millar, R.P. (1982) Structure of chicken hypothalamic luteinizing hormone-releasing hormone I. Structural determination on partially purified material. J. Biol. Chem., 257: 10772-10732.
73. Kitamura, K., Kato, J., Kawamoto, M. et al. (1998) The intermediate form of glycine-extended adrenomedullin is the major circulating molecular form in human plasma. Biochem. Biophys. Res. Commun., 244: 551-555.
74. Klungland, H., Lorens, J.B., Andersen, O. et al. (1992) The Atlantic salmon prepro-gonadotropin releasing hormone gene and mRNA. Mol. Cell. Endocrinol., 84: 167-174.
75. Knigge, K.M. (1962) Gonadotropic activity of neonatal pituitary glands implanted in the rat brain. Am. J. Physiol., 202: 387- 391.
76. Koch, Y., Baram, T., Chobsieng, P. et al. (1974) Enzymatic degradation of luteinizing hormone-releasing hormone (LH-RH) by hypothalamic tissue. Biochem. Biophys. Res. Commun., 61: 95-103.
77. Kolhekar, A.S., Roberts, M.S., Jiang, N. et al. (1997) Neuropeptide amidation in Drosophila: Separate genes encode the two enzymes catalyzing amidation. J. Neurosci., 17: 1363-1376.
78. Kumar, A.M., Agarwal, R.K., Thompson, M.L. et al. (1994) Effect of chronic DDC treatment on LHRH and substance P amidation processes in the rat. Brain Res. Bull., 33: 337-344.
79. Kuroki, K., Cheung, R., Marion, P. et al. (1994) A cell surface protein that binds avian hepatitis B virus particles. J. Virol., 68: 2091-2096.
80. Kuroki, K., Eng, F., Ishikawa, T. et al. (1995) gp180, a host cell glycoprotein that binds duck hepatitis B virus particles, is encoded by a member of the carboxypeptidase gene family. J. Biol. Chem., 270: 15022-15028.
81. Lanoue, E. and Day, R. (2001) Coexpression of proprotein convertase SPC3 and the neuroendocrine precursor proSAAS. Endocrinology, 142: 4141-4149.
82. Leiter, E.H. and Herberg, L. (1997) The polygenetics of diabetes in mice. Diabetes Rev., 5: 131-148.
83. Lescheid, D.W., Teresawa, E., Abler, L.A. et al. (1997) A second form of gonadotropin-releasing hormone (GnRH) with characteristics if chicken GnRH-II is present in primate brain. Endocrinology, 138: 5618-5629.
84. Lew, R.A., Tetaz, T.J., Glucksman, M.J. et al. (1994) Evidence for a two-step mechanism of gonadotropin-releasing hormone metabolism by proylyl endopeptidase and metalloendopeptidase EC 3.4.24.15 in ovine hypothalamic extracts. J. Biol. Chem., 269: 12626-12632.
85. Lewin, B. (1996) Genes V. Oxford University Press, Oxford, pp. 168.
86. Lindberg, I., Van den Hurk, W.H., Bui, C. et al. (1995) Enzymatic characterization of immunopurified convertase 2. Potent inhibition by a 7B2 peptide fragment. Biochemistry, 34: 5486-5493.
87. Lovejoy, D.A., Fischer, W.H., Ngamvongchon, S. et al. (1992) Distinct sequence of gonadotropin-releasing hormone (GnRH) in dogfish brain provides insight into GnRH evolution. Proc. Natl. Acad. Sci. USA, 89: 6373-6377.
88. Lusson, J., Vieau, D., Hamelin, J. et al. (1993) cDNA structure of the mouse and rat subtilisin/kexin-like PC5: A candidate proprotein convertase expressed in endocrine and neuroendocrine cells. Proc. Natl. Acad. Sci. USA, 90: 6691-6695.
89. Mason, A.J., Hayflick, J.S., Zoeller, R.T. et al. (1986a) A deletion truncating the gonadotropin-releasing hormone gene is responsible for hypogonadism in the hpg mouse. Science, 234: 1366-1371.
90. Mason, A.J., Pitts, S.L., Nikolics, K. et al. (1986b) The hypogonadal mouse: Reproductive functions restored by gene therapy. Science, 234: 1372-1378.
91. Matsuo, H., Baba, Y., Nair, R.M.G. et al. (1971) Structure of the porcine LH- and FSH-releasing hormone. I. The proposed amino acid sequence. Biochem. Biophys. Res. Commun., 43: 1334-1339.
92. Mbikay, M., Tadros, H., Ishida, N. et al. (1997) Impaired fertility in mice deficient for the testicular germ-cell protease PC4. Proc. Natl. Acad. Sci. USA, 94: 6842-6846.
93. McCann, S.M., Taleisnik, S. and Friedman, H.M. (1960) LH-releasing activity in hypothalamic extracts. Proc. Soc. Exp. Biol. Med., 104: 432-434.
94. Merkler, D.J., Glufke, U., Ritenour-Rodgers, K.J. et al. (1999) Formation of nicotinamide from nicotinuric acid by peptidylglycine alpha-amidating monooxygenase (PAM): A possible alternative route from nicotinic acid (niacin) to NADP in mammals. J. Amer. Chem. Soc., 121: 4904-4905.
95. Milton, R.C.deL., Wormald, P.J., Brandt, W. et al. (1986) The delineation of a decapeptide gonadotropin-releasing sequence in the carboxy-terminal extension of the human gonadotropin-releasing hormone precursor. J. Biol. Chem., 261: 16990-16997.
96. Miyamoto, K., Hasegawa, Y., Nomura, M. et al. (1984) Identification of the second gonadotropin-releasing hormone in chicken hypothalamus: Evidence that gonadotropin secretion is probably controlled by two distinct gonadotropin-releasing hormones in avian species. Proc. Natl. Acad. Sci. USA, 81: 3874-3878.
97. Mizuno, K., Ohsuye, K., Wada, Y. et al. (1987) Cloning and sequence of cDNA encoding a peptide C-terminal α-amidating enzyme from Xenopus laevis. Biochem. Biophys. Res. Commun., 148: 546-552.
98. Montaner, A.D., Park, M.K., Fischer, W.H. et al. (2001) Primary structure of a novel gonadotropin-releasing hormone in the brain of a teleost, pejerry. Endocrinology, 142: 1453-1460.
99. Naggert, J.K., Fricker, L.D., Varlamov, O. et al. (1995) Hyperproinsulinaemia in obese fat/fat mice associated with a carboxypeptidase E mutation which reduces enzyme activity. Nat. Genet., 10: 135-142.
100. Nakagawa, T., Murakami, K. and Nakayama, K. (1993a) Identification of an isoform with an extremely large Cys-rich region of PC6, a Kex2-like processing endoprotease. FEBS Lett., 327: 165-171.
101. Nakagawa, T., Hosaka, M., Torii, S. et al. (1993b) Identification and functional expression of a new member of the mammalian Kex2-like processing endoprotease family: Its striking structural similarity to PACE4. J. Biochem. (Tokyo), 113: 132-135.
102. Nakayama, K., Kim, W.S., Torii, S. et al. (1992) Identification of the fourth member of the mammalian endoprotease family homologous to the yeast Kex2 protease. Its testis-specific expression. J. Biol. Chem., 267: 5897-5900.
103. Ngamvongchon, S., Lovejoy, D.A., Fischer, W.H. et al. (1992) Primary structures of two forms of gonadotropin-releasing hormone, one distinct and one conserved, from catfish brain. Mol. Cell. Neurosci., 3: 17-22.
104. Nikitovitch-Winer, M. and Everett, J.W. (1958) Functional reconstitution of pituitary grafts re-transplanted from kidney to median eminence. Endocrinology, 63: 916-930.
105. Nikolics, K., Mason, A.J., Szõnyi, E. et al. (1985) A prolactin-inhibiting factor within the precursor form human gonadotropin-releasing hormone. Nature, 316: 511-517.
106. Novikova, E.G., Eng, F.J., Yan, L. et al. (1999) Characterization of the enzymatic properties of the first and second domains of metallocarboxypeptidase D. J. Biol. Chem., 274: 28887-28892.
107. O'Cuinn, G., O'Connor, B. and Elmore, M. (1990) Degradation of thyrotropin-releasing hormone and luteinizing hormone-releasing hormone by enzymes in brain tissue. J. Neurochem., 4: 1-13.
108. Okada, T., Kitamura, K., Baba, Y. et al. (1973) Luteinizing hormone-releasing hormone analogs lacking N-terminal pGLU ring structure. Biochem. Biophys. Res. Commun., 53: 1180-1186.
109. Okubo, K., Amano, M., Yoshiura, Y. et al. (2000) A novel form of gonadotropin-releasing hormone in the madaka, oryzias latipes. Biochem. Biophys. Res. Commun., 276: 298-303.
110. O'Rahilly, S., Gray, H., Humphreys, P.J. et al. (1995) Brief report: Impaired processing of prohormones associated with abnormalities of glucose homeostasis and adrenal function. New Engl. J. Med., 333: 1386-1390.
111. Ouafik, L.H., Stoffers, D.A., Campbell, T.A. et al. (1992) The multifunctional peptidylglycine α-amidating monooxygenase gene: Exon/intron organization of catalytic, processing, and routing domains. Mol. Endocrinol., 6: 1571-1584.
112. 2-terminal sequences. J. Biol. Chem., 265: 17101-17105.
113. Perkins, S.N., Husten, E.J. and Eipper, B.A. (1990) The 108-kDA peptidylglycine alpha-amidating monooxygenase precursor contains two separable enzymatic activities involved in peptide amidation. Biochem. Biophys. Res. Commun., 171: 926-932.
114. Pitts, G.R., Nunemaker, C.S. and Moenter, S.M. (2001) Cycles of transcription and translation do not comprise the gonadotropin-releasing hormone pulse generator in GT1 cells. Endocrinology, 142: 1858-1864.
115. Planas, J., Bern, H.A. and Millar, R.P. (1990) Effects of GnRH- associated peptide and its component peptides on prolactin secretion from the tilapia pituitary in vitro, Gen. Comp. Endocrinol., 77: 386-396.
116. Pohl, T., Zimmer, M., Mugele, K. et al. (1991) Primary structure and functional expression of a glutaminyl cyclase. Proc. Natl. Acad. Sci. USA, 88: 10059-10063.
117. Powell, J.F.F., Zohar, Y., Elizur, A. et al. (1994) Three forms of gonadotropin-releasing hormone characterized from brains of one species. Proc. Natl. Acad. Sci. USA, 91: 12081-12085.
118. Powell, J.F.F., Reska-Skinner, S.M., Om Prakash, M. et al. (1996) Two new forms of gonadotropin-releasing hormone in a protochordate and the evolutionary implications. Proc. Natl. Acad. Sci. USA, 93: 10461-10464.
119. Prigge, S.T., Mains, R.E., Eipper, B.A. et al. (2000) New insights into copper monooxygenases and peptide amidation: Structure, mechanism and function. Cell. Mol. Life Sci., 57: 1236-1259.
120. Prochazka, M., Gold, D.P., Castano, L. et al. (1991) Mapping of secretogranin 1 (Scg-1) to Chr 2, and carboxypeptidase H (Cph-1) to Chr 8. Mouse Genome, 89: 280.
121. Qian, Y., Devi, L.A., Mzhavia, N. et al. (2000) The C-terminal region of proSAAS is a potent inhibitor of prohormone convertase 1. J. Biol. Chem., 275: 23596-23601.
122. th Edition. Saunders, Philadelphia, pp. 341-388.
123. Reznik, S.E. and Fricker, L.D. (2001) Carboxypeptidases from A to Z: Implications in embryonic development and Wnt binding. Cell. Mol. Life Sci., 58: 1790-1804.
124. Rodriguez, C., Brayton, K.A., Brownstein, M. et al. (1989) Rat preprocarboxypeptidase H: Cloning, characterization, and sequence of the cDNA and regulation of the mRNA by corticotropin-releasing factor. J. Biol. Chem., 264: 5988-5995.
125. Roebroek, A.J., Schalken, J.A., Leunissen, J.A. et al. (1986) Evolutionary conserved close linkage of the c-fes/fps proto-oncogene and genetic sequences encoding a receptor-like protein. EMBO J., 5: 2197-2202.
126. Roebroek, A.J., Umans, L., Pauli, I.G. et al. (1998) Failure of ventral closure and axial rotation in embryos lacking the proprotein convertase Furin. Development, 125: 4863-4876.
127. Sakuma, Y. and Pfaff, D.W. (1983) Modulation of the lordosis reflex of female rats by LHRH, its antiserum and analogs in the mesencephalic central gray. Neuroendocrinology, 36: 218-224.
128. Sayah, M., Fortenberry, Y., Cameron, A. et al. (2001) Tissue distribution and processing of proSAAS by proprotein convertases. J. Neurochem., 76: 1833-1841.
129. Schäfer, M.K.-H., Day, R., Cullinan, W.E. et al. (1993) Gene expression of pro-hormone and proprotein convertases in the rat CNS: A comparative in situ hybridization analysis. J. Neurosci., 13: 1258-1279.
130. Schalken, J.A., Roebroek, A.J.M., Oomen, P.P.C.A. et al. (1987) fur Gene expression as a discriminating marker for small cell and nonsmall cell lung carcinoma. J. Clin. Invest., 80: 1545-1549.
131. Schally, A.V., Arimura, A. and Kastin, A.J. (1973) Hypothalamic regulatory hormones. Science, 179: 341-350.
132. Sealfon, S.C., Weinstein, H. and Millar, R.P. (1997) Molecular mechanisms of ligand interaction with the gonadotropin-releasing hormone receptor. Endocrine Rev., 18: 180-205.
133. Seeburg, P.H. and Adelman, J.P. (1984) Characterization of the cDNA for precursor of human luteinizing hormone releasing hormone. Nature, 311: 666-668.
134. Seidah, N.G. and Chrétien, M. (1999) Proprotein and prohormone convertases: A family of subtilases generating diverse bioactive polypeptides. Brain Res., 848: 45-62.
135. Seidah, N.G., Gaspar, L., Mion, P. et al. (1990) cDNA sequence of two distinct pituitary proteins homologous to Kex2 and furin gene products: Tissue-specific mRNAs encoding candidates for pro-hormone processing proteinases. DNA Cell Biol., 9: 415-424.
136. Seidah, N.G., Marcinkiewicz, M., Benjannet, S. et al. (1991) Cloning and primary sequence of a mouse candidate prohormone convertase PC1 homologous to PC2, Furin, and Kex2: Distinct chromosomal localization and messenger RNA distribution in brain and pituitary compared to PC2. Mol. Endocrinol., 5: 111-122.
137. Seidah, N.G., Day, R., Hamelin, J. et al. (1992) Testicular expression of PC4 in the rat: Molecular diversity of a novel germ cell-specific Kex2/subtilisin-like proprotein convertase. Mol. Endocrinol., 6: 1559-1570.
138. Seidah, N.G., Hamelin, J., Mamarbachi, M. et al. (1996) cDNA structure, tissue distribution, and chromosomal localization of rat PC7, a novel mammalian proprotein convertase closest to yeast kexin-like proteinases. Proc. Natl. Acad. Sci. USA, 93: 3388-3393.
139. Seidah, N.G., Mowla, S.J., Hamelin, J. et al. (1999a) Mammalian subtilisin/kexin isozyme SKI-1: A widely expressed proprotein convertase with a unique cleavage specificity and cellular localization. Proc. Natl. Acad. Sci. USA, 96: 1321-1326.
140. Seidah, N.G., Benjannet, S., Hamelin, J. et al. (1999b) The subtilisin/kexin family of precursor convertases. Emphasis on PC1, PC2/7B2, POMC and the novel enzyme SKI-1. Ann. N.Y. Acad. Sci., 885: 57-74.
141. Seong, J.Y., Park, S. and Kim, K. (1999) Enhanced splicing of the first intron from the gonadotropin-releasing hormone (GnRH) primary transcript is a prerequisite for mature GnRH messenger RNA: Presence of GnRH neuron-specific splicing factors. Mol. Endocrinol., 13: 1882-1895.
142. Seong, J.Y., Kim, B.W., Park, S. et al. (2001) First intron excision of GnRH pre-mRNA during postnatal development of normal mice and adult hypogonadal mice. Endocrinology, 142: 4454-4461.
143. Sherwood, N., Eiden, L., Brownstein, M. et al. (1983) Characterization of a teleost gonadotropin-releasing hormone. Proc. Natl. Acad. Sci. USA, 80: 2794-2798.
144. Sherwood, N.M., Sower, S.A., Marshak, D.R. et al. (1986) Primary structure of gonadotropin-releasing hormone from lamprey brain. J. Biol. Chem., 261: 4812-4819.
145. Smeekens, S.P. and Steiner, D.F. (1990) Identification of a human insulinoma cDNA encoding a novel mammalian protein structurally related to the yeast dibasic processing protease Kex2. J. Biol. Chem., 265: 2997-3000.
146. Smyth, D.G., Maruthainar, K., Darby, N.J. et al. (1989) Catalysis of slow C-terminal processing reactions by carboxypeptidase H. J. Neurochem., 53: 489-493.
147. Song, L. and Fricker, L. (1995a) Processing of procarboxypeptidase E into carboxypeptidase E occurs in secretory vesicles. J. Neurochem., 65: 444-453.
148. Song, L. and Fricker, L.D. (1995b) Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary. J. Biol. Chem., 270: 25007-25013.
149. Song, L. and Fricker, L.D. (1996) Tissue distribution and characterization of soluble and membrane-bound forms of metallocarboxypeptidase D. J. Biol. Chem., 271: 28884-28889.
150. Sower, S.A., Chiang, Y.A., Lova, S. et al. (1993) Primary structure and biological activity of a third gonadotropin-releasing hormone from lamprey brain. Endocrinology, 132: 1125-1131.
151. Steiner, D.F. (1998) The proprotein convertases. Curr. Opin. Chem. Biol., 2:31-39.
152. Stoffers, D.A., Green, C.B.-R. and Eipper, B.A. (1989) Alternative mRNA splicing generates multiple forms of peptidylglycine α-amidating monooxygenase in rat atrium. Proc. Natl. Acad. Sci. USA, 86: 735-739.
153. Stoffers, D.A., Ouafik, L.H. and Eipper, B.A. (1991) Characterization of novel mRNAs encoding enzymes involved in peptide α-amidation. J. Biol. Chem., 266: 1701-1707.
154. Suzuki, K., Gamble, R.K. and Sower, S.A. (2000) Multiple transcripts encoding lamprey gonadotropin-releasing hormone-I precursors. J. Mol. Endocrinol., 24: 365-376.
155. Sykes, P.A., Watson, S.J., Temple, J.S. et al. (1999) Evidence for tissue-specific forms of glutaminyl cyclase. FEBS Lett., 455: 159-161.
156. Tadros, H., Chretien, M. and Mbikay, M. (2001) The testicular germ-cell protease PC4 is also expressed in macrophage-like cells of the ovary. Reprod. Immunol., 49: 133-152.
157. Takahashi, K., Okamoto, H., Seino, H. et al. (1990) Peptidylglycine α-amidating reaction: Evidence for a two-step mechanism involving a stable intermediate at neutral pH. Biochem. Biophys. Res. Commun., 169: 524-530.
158. Tan, F., Rehli, M., Krause, S.W. et al. (1997) Sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem active site domains. Biochem. J., 327: 81-87.
159. Thim, L., Hansen, M.T., Norris, K. et al. (1986) Secretion and processing of insulin precursors in yeast. Proc. Natl. Acad. Sci. USA, 83: 6766-6770.
160. Thomas, G.B., Cummins, J.T., Doughton, B.W. et al. (1988a) Gonadotropin-releasing hormone associated peptide (GAP) and putative processed GAP peptides do not release luteinizing hormone or follicle-stimulating hormone or inhibit prolactin secretion in sheep. Neuroendocrinology, 48: 342-350.
161. Thomas, G., Thorne, B.A., Thomas, L. et al. (1988b) Yeast KEX2 endopeptidase correctly cleaves a neuroendocrine prohormone in mammalian cells. Science, 241: 226-230.
162. th Edition. Saunders, Philadelphia, pp. 249-340.
163. Vacher, P., Mariot, P., Dufy-Barbe, L. et al. (1991) The gonadotropin-releasing hormone associated peptide reduces calcium entry in prolactin-secreting cells. Endocrinology, 128: 285-294.
164. Valença, M.M., Johnston, C.A., Ching, M. et al. (1987) Evidence for a negative ultrashort feedback mechanism operating on the luteinizing hormone-releasing hormone neuronal system. Endocrinology, 121: 2256-2259.
165. +], prostaglandin E2, and C kinase activation. Mol. Cell. Endocrinol., 55: 95-100.
166. van Chuoi, M.T., Vacher, P. and Dufy, B. (1993) GnRH-associated peptide decreases cyclic AMP accumulation in the GH3 pituitary cell line. Neuroendocrinology, 58: 251-257.
167. 202 of carboxypeptidase E. J. Biol. Chem., 271: 13981-13986.
168. Varlamov, O., Eng, F.J., Novikova, E.G. et al. (1999) Localization of metallocarboxypeptidase D in AtT-20 cells: Potential role in prohormone processing. J. Biol. Chem., 274: 14759-14767.
169. Vishnuvardhan, D., Connolly, K., Cain, B. et al. (2000) PC2 and 7B2 null mice demonstrate that PC2 is essential for normal pro-CCK processing. Biochem. Biophys. Res. Commun., 273: 188-191.
170. Voigt, P., Ma, Y.J., Gonzalez, D. et al. (1996) Neural and glial-mediated effects of growth factors acting via tyrosine kinase receptors on luteinizing hormone-releasing hormone neurons. Endocrinology, 137: 2593-2605.
171. Utsunomiya, N., Ohagi, S., Sanke, T. et al. (1998) Organization of the human carboxypeptidase E gene and molecular scanning for mutations in Japanese subjects with NIDDM or obesity. Diabetologia, 41: 701-705.
172. Westphal, C.H., Muller, L., Zhou, A. et al. (1999) The neuroendocrine protein 7B2 is required for peptide hormone processing in vivo and provides a novel mechanism for pituitary Cushing's disease. Cell, 96: 689-700.
173. Wetsel, W.C. (1995) Immortalized hypothalamic luteinizing hormone-releasing hormone (LHRH) neurons: A new tool for dissecting the molecular and cellular basis of LHRH physiology. Cell. Mol. Neurobiol., 15: 43-78.
174. Wetsel, W.C. and Negro-Vilar, A. (1989) Testosterone selectively influences protein kinase C-coupled secretion of proluteinizing hormone-releasing hormone-derived peptides. Endocrinology, 125: 538-547.
175. Wetsel, W.C., Culler, M.D., Johnston, C.A. et al. (1988) Processing of the luteinizing hormone-releasing hormone precursor in the preoptic area and hypothalamus of the rat. Mol. Endocrinol., 2: 22-31.
176. Wetsel, W.C., Mellon, P.L., Weiner, R.I. et al. (1991) Metabolism of pro-luteinizing hormone-releasing hormone in immortalized hypothalamic neurons. Endocrinology, 129: 1584-1595.
177. Wetsel, W.C., Eraly, S.A., Whyte, D.B. et al. (1993) Regulation of gonadotropin-releasing hormone by protein kinase-A and -C in immortalized hypothalamic neurons. Endocrinology, 132: 2360-2370.
178. Wetsel, W.C., Liposits, Z., Seidah, N.G. et al. (1995) Expression of candidate pro-GnRH processing enzymes in rat hypothalamus and an immortalized hypothalamic neuronal cell line. Neuroendocrinology, 62: 166-177.
179. Wetsel, W.C., Hill, D.F. and Ojeda, S.R. (1996) Basic fibroblast growth factor regulates the conversion of pro-luteinizing hormone-releasing hormone (Pro-LHRH) to LHRH in immortalized hypothalamic neurons. Endocrinology, 137: 2606-2616.
180. White, R.B., Eisen, J.A., Kasten, T.L. et al. (1998a) Second gene for gonadotropin-releasing hormone in humans. Proc. Natl. Acad. Sci. USA, 95: 305-309.
181. White, R.B., Urbanski, H.F. and Fernald, R.D. (1998b) A second gene for gonadotropin-releasing hormone is expressed in the rhesus macaque. Soc. Neurosci., 24: 1609 (abstract).
182. Wormald, P.J., Abrahamson, M.J., Seeburg, P.H. et al. (1989) Prolactin-inhibiting activity of GnRH associated peptide in cultured human pituitary cells. Clin. Endocrinol., 30: 149-155.
183. Xin, X., Varlamov, O., Day, R. et al. (1997) Cloning and sequence analysis of cDNA encoding rat carboxypeptidase D. DNA Cell Biol., 16: 897-909.
184. Yahalom, D., Chen, A., Ben-Aroya, N. et al. (1999) The gonadotropin-releasing hormone family of neuropeptides in the brain of human, bovine, and rat: Identification of a third isoform. Febs Lett., 463: 289-294.
185. 8] GnRH) in frog brain. Mol. Cell. Endocrinol., 164: 197-204.
186. Yu, W.H., Seeburg, P.H., Nikolics, K. et al. (1988) Gonadotropin-releasing hormone associated peptide exerts a prolactin-inhibiting and weak gonadotropin-releasing activity in vivo. Endocrinology, 123: 390-395.
187. Yu, W.H., Arisawa, M., Millar, R.P. et al. (1989) Effects of gonadotropin-releasing hormone associated peptides (GAP) on the release of luteinizing hormone (LH), follicle-stimulating hormone (FSH) and prolactin (PRL) in vivo. Peptides, 10: 1133-1138.
188. Zheng, M., Streck, R.D., Scott, R.E. et al. (1994) The developmental expression in rat of proteases furin, PC1, PC2, and carboxypeptidase E: Implications for early maturation of proteolytic processig capacity. J. Neurosci., 14: 4656-4673.
189. Zhu, X. and Lindberg, I. (1995) 7B2 facilitates the maturation of proPC2 in neuroendocrine cells and is required for the expression of enzymatic activity. J. Cell Biol., 129: 1641-1650.