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Volumn 17, Issue 8, 1996, Pages 1285-1290

Synthesis and biological activity of adipokinetic hormone analogues modified at the C-terminus

Author keywords

Acetate uptake; Cyclic peptide; Ester; Lipid mobilization; Locust; Locusta migratoria; Structure activity relationships

Indexed keywords

ADIPOKINETIC HORMONE;

EID: 0030445192     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0196-9781(96)00224-0     Document Type: Article
Times cited : (15)

References (45)
  • 1
    • 0026452983 scopus 로고
    • Synthesis and biological activity of analogues of the C-terminal hexapeptide of substance P with modifications at glutaminyl and methioninyl residues
    • 1. Antoniou, M.; Poulos, C.; Tengendis, Th. Synthesis and biological activity of analogues of the C-terminal hexapeptide of substance P with modifications at glutaminyl and methioninyl residues. Structure-activity studies. Int. J. Pept. Protein Res. 40:395-400; 1992.
    • (1992) Structure-activity Studies. Int. J. Pept. Protein Res. , vol.40 , pp. 395-400
    • Antoniou, M.1    Poulos, C.2    Tengendis, T.3
  • 2
    • 0011272668 scopus 로고
    • Inactivation of neurohormone D by Malpighian tubules in an insect, Periplaneta americana
    • 2. Baumann, E.; Penzlin, H. Inactivation of neurohormone D by Malpighian tubules in an insect, Periplaneta americana. J. Comp. Physiol. [B] 157:511-517; 1987.
    • (1987) J. Comp. Physiol. [B] , vol.157 , pp. 511-517
    • Baumann, E.1    Penzlin, H.2
  • 3
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • 3. Chou, P. Y.; Fasman, G. D. Prediction of protein conformation. Biochemistry 13:222-245; 1974.
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 4
    • 0018127648 scopus 로고
    • Structure-function studies on red pigment-concentrating hormone; The significance of the terminal residues
    • 4. Christensen, M.; Carlsen, J.; Josefsson, L. Structure-function studies on red pigment-concentrating hormone; the significance of the terminal residues. Hoppe Seylers Z. Physiol. Chem. 359:813-818; 1978.
    • (1978) Hoppe Seylers Z. Physiol. Chem. , vol.359 , pp. 813-818
    • Christensen, M.1    Carlsen, J.2    Josefsson, L.3
  • 5
    • 0018286667 scopus 로고
    • Structure-function studies on red pigment-concentrating hormone, II. The significance of the C-terminal tryptophan amide
    • 5. Christensen, M.; Carlsen, J.; Josefsson, L. Structure-function studies on red pigment-concentrating hormone, II. The significance of the C-terminal tryptophan amide. Hoppe Seylers Z. Physiol. Chem. 360:1051-1060; 1979.
    • (1979) Hoppe Seylers Z. Physiol. Chem. , vol.360 , pp. 1051-1060
    • Christensen, M.1    Carlsen, J.2    Josefsson, L.3
  • 6
    • 0015506013 scopus 로고
    • Crustacean color-change hormone: Amino acid sequence and chemical synthesis
    • 6. Fernlund, P.; Josefsson, L. Crustacean color-change hormone: Amino acid sequence and chemical synthesis. Science 177:173-175; 1972.
    • (1972) Science , vol.177 , pp. 173-175
    • Fernlund, P.1    Josefsson, L.2
  • 7
    • 0002963972 scopus 로고
    • Structure-activity relationships for insect hypertrehalosemic hormone: The importance of side chains and termini
    • Marshall, G. M., Ed. Leiden, The Netherlands: ESCOM
    • 7. Ford, M. M.; Hayes, T. K.; Keeley, L. L. Structure-activity relationships for insect hypertrehalosemic hormone: The importance of side chains and termini. In: Marshall, G. M., Ed. Peptides: Chemistry and biology. Leiden, The Netherlands: ESCOM; 1988:653-655.
    • (1988) Peptides: Chemistry and Biology , pp. 653-655
    • Ford, M.M.1    Hayes, T.K.2    Keeley, L.L.3
  • 8
    • 84990441912 scopus 로고
    • Structure-function studies on hypertrehalosemic and adipokinetic hormones: Activity of naturally occurring analogues and some N-and C-terminally modified analogues
    • 8. Gäde, G. Structure-function studies on hypertrehalosemic and adipokinetic hormones: Activity of naturally occurring analogues and some N-and C-terminally modified analogues. Physiol. Entomol. 15:299-316; 1990.
    • (1990) Physiol. Entomol. , vol.15 , pp. 299-316
    • Gäde, G.1
  • 9
    • 0025903413 scopus 로고
    • A unique charged tyrosine-containing member of the adipokinetic hormone/red-pigment-concentrating hormone peptide family isolated from two beetle species
    • 9. Gäde, G. A unique charged tyrosine-containing member of the adipokinetic hormone/red-pigment-concentrating hormone peptide family isolated from two beetle species. Biochem. J. 275:671-677; 1991.
    • (1991) Biochem. J. , vol.275 , pp. 671-677
    • Gäde, G.1
  • 10
    • 0028894898 scopus 로고
    • Structure-activity relationships for Periplaneta americana hypertrehalosemic hormone I: The importance of side chains and termini
    • 10. Gäde, G.; Hayes, T. K. Structure-activity relationships for Periplaneta americana hypertrehalosemic hormone I: The importance of side chains and termini. Peptides 16:1173-1180; 1995.
    • (1995) Peptides , vol.16 , pp. 1173-1180
    • Gäde, G.1    Hayes, T.K.2
  • 11
    • 0011273837 scopus 로고
    • Insect hypertrehalosemic hormone: Structure-activity studies in Periplaneta americana
    • Borkovec, A. B.; Masler, E. P., Eds. Clifton, NJ: The Humana Press
    • 11. Gäde, G.; Hayes, T. K. Insect hypertrehalosemic hormone: Structure-activity studies in Periplaneta americana. In: Borkovec, A. B.; Masler, E. P., Eds. Insect neurochemistry and neurophysiology: 1989. Clifton, NJ: The Humana Press: 1990:243-246.
    • (1990) Insect Neurochemistry and Neurophysiology: 1989 , pp. 243-246
    • Gäde, G.1    Hayes, T.K.2
  • 12
    • 0002536455 scopus 로고
    • Molecular evolution of peptides of the AKH-RPCH family
    • Davey, K. G.; Peter, R. E.; Tobe, S. S., Eds. Canada: National Research Council
    • 12. Gäde, G.; Reynolds, S. E.; Beeching, J. R. Molecular evolution of peptides of the AKH-RPCH family. In: Davey, K. G.; Peter, R. E.; Tobe, S. S., Eds. Perspectives in comparative endocrinology. Canada: National Research Council; 1994:119-128.
    • (1994) Perspectives in Comparative Endocrinology , pp. 119-128
    • Gäde, G.1    Reynolds, S.E.2    Beeching, J.R.3
  • 13
    • 0002150231 scopus 로고
    • The inhibition of lipid synthesis in vitro in the locust, Schistocerca gregaria, by factors from the corpora cardiaca
    • 13. Gokuldas, M.; Hunt, P. A.; Candy, D. J. The inhibition of lipid synthesis in vitro in the locust, Schistocerca gregaria, by factors from the corpora cardiaca. Physiol. Entomol. 13:43-48; 1988.
    • (1988) Physiol. Entomol. , vol.13 , pp. 43-48
    • Gokuldas, M.1    Hunt, P.A.2    Candy, D.J.3
  • 14
    • 38249042381 scopus 로고
    • Relative adipokinetic activities of members of the adipokinetic hormone/red pigment concentrating hormone family
    • 14. Goldsworthy, G. J.; Mallison K.; Wheeler, C. H.; Gäde, G. Relative adipokinetic activities of members of the adipokinetic hormone/red pigment concentrating hormone family. J. Insect Physiol. 32:433-438; 1986.
    • (1986) J. Insect Physiol. , vol.32 , pp. 433-438
    • Goldsworthy, G.J.1    Mallison, K.2    Wheeler, C.H.3    Gäde, G.4
  • 15
    • 0002624274 scopus 로고
    • Adipokinetic hormones: Interassay variations in potencies as clues to hormone-receptor interactions in the locust
    • Konopinska, D., Ed. Poland: University of Wroclaw
    • 15. Goldsworthy, G. J.; Lee, M. J.; Luswata, R. Adipokinetic hormones: Interassay variations in potencies as clues to hormone-receptor interactions in the locust. In: Konopinska, D., Ed. Insects: Chemical, physiological and environmental aspects 1994. Poland: University of Wroclaw; 1995:17-27.
    • (1995) Insects: Chemical, Physiological and Environmental Aspects 1994 , pp. 17-27
    • Goldsworthy, G.J.1    Lee, M.J.2    Luswata, R.3
  • 17
    • 0011276473 scopus 로고
    • Probing the steric tolerance of the insect hypertrehalosemic hormone receptor to develop an effective photoaffinity probe
    • Hodges, R.; Smith, J., Eds. Leiden, The Netherlands: ESCOM
    • 17. Hayes, T. K.; Nails, F. L.; Ford, M. M. Probing the steric tolerance of the insect hypertrehalosemic hormone receptor to develop an effective photoaffinity probe. In: Hodges, R.; Smith, J., Eds. Peptides: Chemistry, structure and biology. Leiden, The Netherlands: ESCOM; 1994:666-668.
    • (1994) Peptides: Chemistry, Structure and Biology , pp. 666-668
    • Hayes, T.K.1    Nails, F.L.2    Ford, M.M.3
  • 18
    • 0029109802 scopus 로고
    • Inhibition of RNA synthesis by adipokinetic hormones and brain factor(s) in adult fat body of Locusta migratoria
    • 18. Kodrík, D.; Goldsworthy, G. J. Inhibition of RNA synthesis by adipokinetic hormones and brain factor(s) in adult fat body of Locusta migratoria. J. Insect Physiol. 41:127-133; 1995.
    • (1995) J. Insect Physiol. , vol.41 , pp. 127-133
    • Kodrík, D.1    Goldsworthy, G.J.2
  • 19
    • 0027685748 scopus 로고
    • Metabolism of insect neuropeptides: Properties of a membrane-bound endopeptidase from heads of Musca domesticus
    • 19. Lamango, N. S.; Isaac, R. E. Metabolism of insect neuropeptides: Properties of a membrane-bound endopeptidase from heads of Musca domesticus. Insect Biochem. Mol. Biol. 23:801-808; 1993.
    • (1993) Insect Biochem. Mol. Biol. , vol.23 , pp. 801-808
    • Lamango, N.S.1    Isaac, R.E.2
  • 20
    • 0029169545 scopus 로고
    • Acetate uptake assay; The basis of a rapid method for determining potencies of adipokinetic peptides for structure-activity studies
    • 20. Lee, M. J.; Goldsworthy, G. J. Acetate uptake assay; the basis of a rapid method for determining potencies of adipokinetic peptides for structure-activity studies. J. Insect Physiol. 41:163-170; 1995.
    • (1995) J. Insect Physiol. , vol.41 , pp. 163-170
    • Lee, M.J.1    Goldsworthy, G.J.2
  • 21
    • 0029076420 scopus 로고
    • The preparation and use of dispersed cells from fat body of Locusta migratoria in a filtration plate assay for adipokinetic peptides
    • 21. Lee, M. J.; Goldsworthy, G. J. The preparation and use of dispersed cells from fat body of Locusta migratoria in a filtration plate assay for adipokinetic peptides. Anal. Biochem. 228:155-161; 1995.
    • (1995) Anal. Biochem. , vol.228 , pp. 155-161
    • Lee, M.J.1    Goldsworthy, G.J.2
  • 22
    • 0030066504 scopus 로고    scopus 로고
    • Modified AKH peptides containing two tryptophan residues and their activities in vitro and in vivo in
    • 22. Lee, M. J.; Goldsworthy, G. J. Modified AKH peptides containing two tryptophan residues and their activities in vitro and in vivo in Locusta. J. Comp. Physiol. [B] 166:61-67; 1996.
    • (1996) Locusta. J. Comp. Physiol. [B] , vol.166 , pp. 61-67
    • Lee, M.J.1    Goldsworthy, G.J.2
  • 23
    • 0011352940 scopus 로고    scopus 로고
    • New perspectives on the structures, assays and actions of locust adipokinetic hormones
    • in press
    • 23. Lee, M. J.; Goldsworthy, G. J. New perspectives on the structures, assays and actions of locust adipokinetic hormones. Soc. Exp. Biol. Symp. Ser. (in press).
    • Soc. Exp. Biol. Symp. Ser.
    • Lee, M.J.1    Goldsworthy, G.J.2
  • 24
    • 0029878295 scopus 로고    scopus 로고
    • In vitro metabolism of an insect neuropeptide by neural membrane preparations from Lymantria dispar
    • 24. Masler, E. P.; Wagner, R. M.; Kovaleva, E. S. In vitro metabolism of an insect neuropeptide by neural membrane preparations from Lymantria dispar. Peptides 17:321-326; 1996.
    • (1996) Peptides , vol.17 , pp. 321-326
    • Masler, E.P.1    Wagner, R.M.2    Kovaleva, E.S.3
  • 25
    • 0029102944 scopus 로고
    • Diuretic activity of C-terminal group analogues of the insect kinins in Acheta domesticus
    • 25. Nachman, R. J.; Coast, G. M.; Holman, G. M.; Beier, R. C. Diuretic activity of C-terminal group analogues of the insect kinins in Acheta domesticus. Peptides 16:809-813; 1995.
    • (1995) Peptides , vol.16 , pp. 809-813
    • Nachman, R.J.1    Coast, G.M.2    Holman, G.M.3    Beier, R.C.4
  • 26
    • 0022533517 scopus 로고
    • Active fragments and analogs of the insect neuropeptide leucopyrokinin: Structure-function studies
    • 26. Nachman, R. J.; Holman G. M.; Cook, B. J. Active fragments and analogs of the insect neuropeptide leucopyrokinin: Structure-function studies. Biochem. Biophys. Res. Commun. 137:936-942; 1986.
    • (1986) Biochem. Biophys. Res. Commun. , vol.137 , pp. 936-942
    • Nachman, R.J.1    Holman, G.M.2    Cook, B.J.3
  • 28
    • 0027265411 scopus 로고
    • Active conformation of the pyrokinin/PBAN neuropeptide family for pheromone biosynthesis in the silkworm
    • 28. Nachman, R. J.; Kuniyoshi, H.; Roberts, V. A.; Holman G. M.; Suzuki A. Active conformation of the pyrokinin/PBAN neuropeptide family for pheromone biosynthesis in the silkworm. Biochem. Biophys. Res. Commun. 193:661-666; 1993.
    • (1993) Biochem. Biophys. Res. Commun. , vol.193 , pp. 661-666
    • Nachman, R.J.1    Kuniyoshi, H.2    Roberts, V.A.3    Holman, G.M.4    Suzuki, A.5
  • 30
    • 0024987258 scopus 로고
    • Consensus chemistry and conformation of an insect neuropeptide family analogous to tachykinins
    • Epple, A.; Scanes, C. G.; Stetson, M. H., Eds. New York: Wiley-Liss, Inc.
    • 30. Nachman, R. J.; Roberts, V. A.; Holman, G. M.; Trainer, J. A. Consensus chemistry and conformation of an insect neuropeptide family analogous to tachykinins. In: Epple, A.; Scanes, C. G.; Stetson, M. H., Eds. Progress in comparative endocrinology. New York: Wiley-Liss, Inc.; 1990:60-66.
    • (1990) Progress in Comparative Endocrinology , pp. 60-66
    • Nachman, R.J.1    Roberts, V.A.2    Holman, G.M.3    Trainer, J.A.4
  • 31
    • 0021153599 scopus 로고
    • Isolation and characterization of two myoactive neuropeptides: Further evidence of an invertebrate peptide family
    • 31. O Shea, M.; Witten, J. L.; Schaffer, M. Isolation and characterization of two myoactive neuropeptides: Further evidence of an invertebrate peptide family. J. Neurosci. 4:521-529; 1984.
    • (1984) J. Neurosci. , vol.4 , pp. 521-529
    • O Shea, M.1    Witten, J.L.2    Schaffer, M.3
  • 32
    • 0029738627 scopus 로고    scopus 로고
    • Locust adipokinetic hormones: Carrier-independent transport and differential inactivation at physiological concentrations during rest and flight
    • 32. Oudejans, R. C. H. M.; Vroemen, S. F.; Jansen, R. F. R.; Van der Horst, D. J. Locust adipokinetic hormones: Carrier-independent transport and differential inactivation at physiological concentrations during rest and flight. Proc. Natl. Acad. Sci. USA 93:8654-8659; 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8654-8659
    • Oudejans, R.C.H.M.1    Vroemen, S.F.2    Jansen, R.F.R.3    Van Der Horst, D.J.4
  • 33
    • 0028020491 scopus 로고
    • Synthesis and biological activity of locust AKH-I and its analogues with modifications at the threonine residues
    • 33. Poulos, C.; Karagiannis, K.; Lee, M.; Goldsworthy, G. Synthesis and biological activity of locust AKH-I and its analogues with modifications at the threonine residues. Int. J. Pept. Protein Res. 44:589-593; 1994.
    • (1994) Int. J. Pept. Protein Res. , vol.44 , pp. 589-593
    • Poulos, C.1    Karagiannis, K.2    Lee, M.3    Goldsworthy, G.4
  • 34
    • 0001988167 scopus 로고
    • Inactivation of neuropeptide hormones (AKH I and AKHII) studied in vivo and in vitro
    • 34. Rayne, R. C.; O Shea, M. Inactivation of neuropeptide hormones (AKH I and AKHII) studied in vivo and in vitro. Insect Biochem. Mol. Biol. 22:25-34; 1992.
    • (1992) Insect Biochem. Mol. Biol. , vol.22 , pp. 25-34
    • Rayne, R.C.1    O Shea, M.2
  • 35
    • 0011273842 scopus 로고    scopus 로고
    • Consensus chemistry and conformation of the active core of the myotropic/diuretic insect kinin neuropeptide family from experimental data and molecular dynamics
    • in press
    • 35. Roberts, V. A.; Nachman, R. J.; Coast, G. M.; Chung, J. S.; Holman, G. M.; Hariharan, M.; Tainer, J. A. Consensus chemistry and conformation of the active core of the myotropic/diuretic insect kinin neuropeptide family from experimental data and molecular dynamics. Biol. Chem. (in press).
    • Biol. Chem.
    • Roberts, V.A.1    Nachman, R.J.2    Coast, G.M.3    Chung, J.S.4    Holman, G.M.5    Hariharan, M.6    Tainer, J.A.7
  • 36
    • 1842390410 scopus 로고
    • Isolation and primary structure of two peptides with cardioacceleratory and hyperglycaemic activity from the corpora cardiaca of Periplaneta americana
    • 36. Scarborough, R. M.; Jamieson G. C.; Kalish, F.; Kramer, S. J.; McEnroe, G. A.; Miller, C. A.; Schooley, D. A. Isolation and primary structure of two peptides with cardioacceleratory and hyperglycaemic activity from the corpora cardiaca of Periplaneta americana. Proc. Natl. Acad. Sci. USA 81:5575-5579; 1984.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 5575-5579
    • Scarborough, R.M.1    Jamieson, G.C.2    Kalish, F.3    Kramer, S.J.4    McEnroe, G.A.5    Miller, C.A.6    Schooley, D.A.7
  • 37
    • 0011318093 scopus 로고
    • Breakdown of locust adipokinetic hormone I by Malpighian tubules of Schistocerca gregaria
    • 37. Siegert, K. J.; Mordue, W. Breakdown of locust adipokinetic hormone I by Malpighian tubules of Schistocerca gregaria. Insect Biochem. 17:705-710; 1987.
    • (1987) Insect Biochem. , vol.17 , pp. 705-710
    • Siegert, K.J.1    Mordue, W.2
  • 38
    • 0001355422 scopus 로고
    • Occurrence of a hyperglycaemic factor in the corpus cardiacum of an insect
    • 38. Steele, J. E. Occurrence of a hyperglycaemic factor in the corpus cardiacum of an insect. Nature 192:680-681; 1961.
    • (1961) Nature , vol.192 , pp. 680-681
    • Steele, J.E.1
  • 39
    • 0002489331 scopus 로고
    • The site of action of insect hyperglycaemic hormone
    • 39. Steele, J. E. The site of action of insect hyperglycaemic hormone. Gen. Comp. Endocrinol. 3:46-52; 1963.
    • (1963) Gen. Comp. Endocrinol. , vol.3 , pp. 46-52
    • Steele, J.E.1
  • 40
    • 0017173049 scopus 로고
    • Structure of locust adipokinetic hormone, a neurohormone that regulates lipid utilisation during flight
    • 40. Stone, J. V.; Mordue, W.; Batley, K. E.; Morris, H. R. Structure of locust adipokinetic hormone, a neurohormone that regulates lipid utilisation during flight. Nature 263:207-211; 1976.
    • (1976) Nature , vol.263 , pp. 207-211
    • Stone, J.V.1    Mordue, W.2    Batley, K.E.3    Morris, H.R.4
  • 41
    • 0018170879 scopus 로고
    • Structure-activity relationships for the lipid-mobilising action of locust adipokinetic hormone
    • 41. Stone, J. V.; Mordue, W.; Broomfield, C. E.; Hardy, P. M. Structure-activity relationships for the lipid-mobilising action of locust adipokinetic hormone. Eur. J. Biochem. 89:195-202; 1978.
    • (1978) Eur. J. Biochem. , vol.89 , pp. 195-202
    • Stone, J.V.1    Mordue, W.2    Broomfield, C.E.3    Hardy, P.M.4
  • 42
    • 0018687075 scopus 로고
    • Hyperglycaemic factor from the corpora cardiaca of Manduca sexta. (L.) (Lepidoptera: Sphingidae)
    • 42. Ziegler, R. Hyperglycaemic factor from the corpora cardiaca of Manduca sexta. (L.) (Lepidoptera: Sphingidae). Gen. Comp. Endocrinol. 39:350-357; 1979.
    • (1979) Gen. Comp. Endocrinol. , vol.39 , pp. 350-357
    • Ziegler, R.1
  • 44
    • 3042863884 scopus 로고
    • Synthesis and back bone cyclization studies of hexapeptides using the reagents TBTU, HBTU, DPPA and PPA
    • Schneider, C. H.; Eberle, A. N., Eds. Leiden: ESCOM
    • 44. Zimmer, S.; Hoffman, E.; Jung, G.; Kessler, H. Synthesis and back bone cyclization studies of hexapeptides using the reagents TBTU, HBTU, DPPA and PPA. In: Schneider, C. H.; Eberle, A. N., Eds. Peptides 1992 (Proceedings of 22nd European Peptide Symposium). Leiden: ESCOM; 1993:393-394.
    • (1993) Peptides 1992 (Proceedings of 22nd European Peptide Symposium) , pp. 393-394
    • Zimmer, S.1    Hoffman, E.2    Jung, G.3    Kessler, H.4


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