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Volumn 151, Issue 1-3, 2008, Pages 80-87

Disulfide-containing peptides from the glandular skin secretions of froglets of the genus Crinia: Structure, activity and evolutionary trends

Author keywords

2D NMR structures; cDNA clones of riparin 1 peptides; Disulfide containing peptides from Crinia signifera, Crinia riparia and Crinia deserticola; Lymphocyte proliferation; Smooth muscle activity

Indexed keywords

CHOLECYSTOKININ B RECEPTOR; DISULFIDE; NITRIC OXIDE SYNTHASE; PEPTIDE; RIPARIN; SIGNIFERIN; UNCLASSIFIED DRUG;

EID: 56249133503     PISSN: 01670115     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.regpep.2008.06.004     Document Type: Article
Times cited : (10)

References (52)
  • 1
    • 0000952847 scopus 로고
    • Bioactive secretions of the amphibian integument
    • Amphibian Biology. Heatwole H., and Barthalmus G.T. (Eds), Surrey Beatty and Sons, Chipping-Norton, NSW, Australia
    • Erspamer V. Bioactive secretions of the amphibian integument. In: Heatwole H., and Barthalmus G.T. (Eds). Amphibian Biology. The Integument Vol. 1 (1994), Surrey Beatty and Sons, Chipping-Norton, NSW, Australia 178-350
    • (1994) The Integument , vol.1 , pp. 178-350
    • Erspamer, V.1
  • 2
    • 0029047938 scopus 로고
    • Amphibian skin: a promising resource of antimicrobial peptides
    • Barra D., and Simmaco M. Amphibian skin: a promising resource of antimicrobial peptides. Trends Biotechnol 13 (1995) 205-209
    • (1995) Trends Biotechnol , vol.13 , pp. 205-209
    • Barra, D.1    Simmaco, M.2
  • 3
    • 33744908288 scopus 로고    scopus 로고
    • Host-defence peptides from the glandular secretions of amphibians: structure and activity
    • Pukala T.L., Bowie J.H., Maselli V.M., Musgrave I.F., and Tyler M.J. Host-defence peptides from the glandular secretions of amphibians: structure and activity. Nat Prod Reps 23 (2006) 368-393
    • (2006) Nat Prod Reps , vol.23 , pp. 368-393
    • Pukala, T.L.1    Bowie, J.H.2    Maselli, V.M.3    Musgrave, I.F.4    Tyler, M.J.5
  • 4
    • 4544386508 scopus 로고    scopus 로고
    • Host-defence peptides of the Australian common froglet Crinia signifera: sequence determination using positive and negative ion electrospray mass spectrometry
    • Maselli V.M., Brinkworth C.S., Bowie J.H., and Tyler M.J. Host-defence peptides of the Australian common froglet Crinia signifera: sequence determination using positive and negative ion electrospray mass spectrometry. Rapid Commun Mass Spectrom 18 (2005) 2155-2161
    • (2005) Rapid Commun Mass Spectrom , vol.18 , pp. 2155-2161
    • Maselli, V.M.1    Brinkworth, C.S.2    Bowie, J.H.3    Tyler, M.J.4
  • 5
    • 33644654421 scopus 로고    scopus 로고
    • Host-defence skin peptides of the Australian steamboat froglet Crinia riparia: isolation and sequence determination by positive and negative ion electrospray mass spectrometry
    • Maselli V.M., Bilusich D., Bowie J.H., and Tyler M.J. Host-defence skin peptides of the Australian steamboat froglet Crinia riparia: isolation and sequence determination by positive and negative ion electrospray mass spectrometry. Rapid Commun Mass Spectrom 20 (2006) 797-803
    • (2006) Rapid Commun Mass Spectrom , vol.20 , pp. 797-803
    • Maselli, V.M.1    Bilusich, D.2    Bowie, J.H.3    Tyler, M.J.4
  • 6
    • 0027069524 scopus 로고
    • A novel method for the release and collection of dermal, glandular secretions from the skin of frogs
    • Tyler M.J., Stone D.J.M., and Bowie J.H. A novel method for the release and collection of dermal, glandular secretions from the skin of frogs. J Pharmacol Toxicol Methods 28 (1992) 199-200
    • (1992) J Pharmacol Toxicol Methods , vol.28 , pp. 199-200
    • Tyler, M.J.1    Stone, D.J.M.2    Bowie, J.H.3
  • 11
    • 0021127534 scopus 로고
    • Comparison of affinities of muscarinic antagonist to pre- and postjunctional receptors in guinea-pig ileum
    • Kilbinger H., Halim S., Lambrecht G., Weiler W., and Wessler I. Comparison of affinities of muscarinic antagonist to pre- and postjunctional receptors in guinea-pig ileum. Eur J Pharmacol 103 (1984) 313-320
    • (1984) Eur J Pharmacol , vol.103 , pp. 313-320
    • Kilbinger, H.1    Halim, S.2    Lambrecht, G.3    Weiler, W.4    Wessler, I.5
  • 12
    • 0032189179 scopus 로고    scopus 로고
    • CCK receptor antagonists
    • Dunlop J. CCK receptor antagonists. Gen Pharmacol (1998) 519-524
    • (1998) Gen Pharmacol , pp. 519-524
    • Dunlop, J.1
  • 13
    • 0037130994 scopus 로고    scopus 로고
    • Diacetylmorphine degradation to 6-monoacetyl-morphine and morphine in cell culture: implications for in vitro studies
    • Hutchinson M.R., and Somogyi A.A. Diacetylmorphine degradation to 6-monoacetyl-morphine and morphine in cell culture: implications for in vitro studies. Eur J Pharmacol 453 (2002) 27-32
    • (2002) Eur J Pharmacol , vol.453 , pp. 27-32
    • Hutchinson, M.R.1    Somogyi, A.A.2
  • 15
    • 13844254284 scopus 로고    scopus 로고
    • The structural organization of aurein cDNAs from the skin secretion of the Australian green and golden bell frog, Litoria aurea
    • Chen T., Scott C., Tang L., Zhou M., and Shaw C. The structural organization of aurein cDNAs from the skin secretion of the Australian green and golden bell frog, Litoria aurea. Regul Pept 128 (2005) 75-83
    • (2005) Regul Pept , vol.128 , pp. 75-83
    • Chen, T.1    Scott, C.2    Tang, L.3    Zhou, M.4    Shaw, C.5
  • 16
    • 0020475314 scopus 로고
    • Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance
    • Wüthrich K., and Wider G. Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance. J Mol Biol 155 (1982) 311-319
    • (1982) J Mol Biol , vol.155 , pp. 311-319
    • Wüthrich, K.1    Wider, G.2
  • 17
    • 0031566434 scopus 로고    scopus 로고
    • Automated NOESY interpretation with ambiguous distance restraints - the refined NMR solution structure of the pleckstrin homology domain from β-spectrin
    • Nilges M., Macias M.J., Odonoghue S.I., and Oschkinat H. Automated NOESY interpretation with ambiguous distance restraints - the refined NMR solution structure of the pleckstrin homology domain from β-spectrin. J Mol Biol 269 (1997) 408-422
    • (1997) J Mol Biol , vol.269 , pp. 408-422
    • Nilges, M.1    Macias, M.J.2    Odonoghue, S.I.3    Oschkinat, H.4
  • 18
    • 0242551269 scopus 로고    scopus 로고
    • The solution structure of frenatin 3, a neuronal nitric oxide synthase inhibitor from the giant tree frog, Litoria infrafrenata
    • Brinkworth C.S., Carver J.A., Wegener K.L., Doyle J., Llewellyn L.E., and Bowie J.H. The solution structure of frenatin 3, a neuronal nitric oxide synthase inhibitor from the giant tree frog, Litoria infrafrenata. Biopolymers 70 (2003) 424-434
    • (2003) Biopolymers , vol.70 , pp. 424-434
    • Brinkworth, C.S.1    Carver, J.A.2    Wegener, K.L.3    Doyle, J.4    Llewellyn, L.E.5    Bowie, J.H.6
  • 19
    • 45249128810 scopus 로고
    • Measurement of vicinal couplings from cross peaks in COSY spectra
    • Kim Y., and Prestegard J.H. Measurement of vicinal couplings from cross peaks in COSY spectra. J Magn Reson 84 (1989) 9-13
    • (1989) J Magn Reson , vol.84 , pp. 9-13
    • Kim, Y.1    Prestegard, J.H.2
  • 20
    • 0037469137 scopus 로고    scopus 로고
    • Solution structure of the RNase H domain of the HIV-1 reverse transcriptase in the presence of magnesium
    • Pari K., Mueller G.A., DeRose E.F., Kirby T.W., and London R.E. Solution structure of the RNase H domain of the HIV-1 reverse transcriptase in the presence of magnesium. Biochemistry 42 (2003) 639-650
    • (2003) Biochemistry , vol.42 , pp. 639-650
    • Pari, K.1    Mueller, G.A.2    DeRose, E.F.3    Kirby, T.W.4    London, R.E.5
  • 21
    • 0014957968 scopus 로고
    • NMR evidence for cis peptide bonds in proline oligomers
    • Deber C.M., Bovey F.A., Carter J.P., and Blout E.R. NMR evidence for cis peptide bonds in proline oligomers. J Am Chem Soc 92 (1970) 6191-6195
    • (1970) J Am Chem Soc , vol.92 , pp. 6191-6195
    • Deber, C.M.1    Bovey, F.A.2    Carter, J.P.3    Blout, E.R.4
  • 22
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graphics 14 (1996) 51-56
    • (1996) J Mol Graphics , vol.14 , pp. 51-56
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 23
    • 0026508095 scopus 로고
    • Functional comparisons of gastrin/cholecystokinin receptors in isolated preparations of gastric mucosa and ileum
    • Patel M., and Spraggs C.P. Functional comparisons of gastrin/cholecystokinin receptors in isolated preparations of gastric mucosa and ileum. Brit J Pharmacol 106 (1992) 275-282
    • (1992) Brit J Pharmacol , vol.106 , pp. 275-282
    • Patel, M.1    Spraggs, C.P.2
  • 24
    • 0028958147 scopus 로고
    • Gastrin CCKB type receptors on human T lymphobastoid Jurgat cells
    • Dornand J., Roche S., Michel F., Bali J.P., and Magous R. Gastrin CCKB type receptors on human T lymphobastoid Jurgat cells. Am J Physiol 268 (1995) G522-G529
    • (1995) Am J Physiol , vol.268
    • Dornand, J.1    Roche, S.2    Michel, F.3    Bali, J.P.4    Magous, R.5
  • 26
    • 0030612754 scopus 로고    scopus 로고
    • mRNAs encoding CCKB but not CCKA receptors are expressed in human T lymphocytes and Jurgat lymphoblastoid cells
    • Cuq P., Gross A., Terraza A., Fourmy D., Clerk P., Dornand J., and Magnous P. mRNAs encoding CCKB but not CCKA receptors are expressed in human T lymphocytes and Jurgat lymphoblastoid cells. Life Sci 61 (1997) 543-555
    • (1997) Life Sci , vol.61 , pp. 543-555
    • Cuq, P.1    Gross, A.2    Terraza, A.3    Fourmy, D.4    Clerk, P.5    Dornand, J.6    Magnous, P.7
  • 27
    • 0033121026 scopus 로고    scopus 로고
    • Age related changes in the modulatory action of gastrin-releasing peptide, neuropeptide Y and sulfated CCK-8 in the proliferation of murine lymphocytes
    • Medina S., Rio M.D., Cuadra B.D., Guayerbas N., and Fuents M.D. Age related changes in the modulatory action of gastrin-releasing peptide, neuropeptide Y and sulfated CCK-8 in the proliferation of murine lymphocytes. Neuropeptides 33 (1999) 173-179
    • (1999) Neuropeptides , vol.33 , pp. 173-179
    • Medina, S.1    Rio, M.D.2    Cuadra, B.D.3    Guayerbas, N.4    Fuents, M.D.5
  • 29
    • 0026726004 scopus 로고
    • Effect of TFE on protein secondary structure - an NMR and CD study using a synthetic actin peptide
    • Sonnichsen F.D., Vaneyk J.E., Hodges R.S., and Sykes B.D. Effect of TFE on protein secondary structure - an NMR and CD study using a synthetic actin peptide. Biochemistry 31 (1992) 8790-8798
    • (1992) Biochemistry , vol.31 , pp. 8790-8798
    • Sonnichsen, F.D.1    Vaneyk, J.E.2    Hodges, R.S.3    Sykes, B.D.4
  • 30
    • 0028174643 scopus 로고
    • Qualitative determination of helical propensities from TFE titration curves
    • Jasanoff A., and Fersht A.R. Qualitative determination of helical propensities from TFE titration curves. Biochemistry 33 (1994) 2129-2135
    • (1994) Biochemistry , vol.33 , pp. 2129-2135
    • Jasanoff, A.1    Fersht, A.R.2
  • 31
    • 0033548058 scopus 로고    scopus 로고
    • Non-proline cis peptide bonds in proteins
    • Jabs A., Weiss M.S., and Hilgenfeld R. Non-proline cis peptide bonds in proteins. J Mol Biol 286 (1999) 291-304
    • (1999) J Mol Biol , vol.286 , pp. 291-304
    • Jabs, A.1    Weiss, M.S.2    Hilgenfeld, R.3
  • 32
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • MacArthur M.W., and Thornton J.M. Influence of proline residues on protein conformation. J Mol Biol 218 (1991) 397-412
    • (1991) J Mol Biol , vol.218 , pp. 397-412
    • MacArthur, M.W.1    Thornton, J.M.2
  • 33
    • 0029181728 scopus 로고
    • H-1, C-13 and N-15 random coil NMR chemical shifts of the common amino acids. 1. Investigations of nearest-neighbor effects
    • Wishart D.S., Bigam C.G., Holm A., Hodges R.S., and Sykes B.D. H-1, C-13 and N-15 random coil NMR chemical shifts of the common amino acids. 1. Investigations of nearest-neighbor effects. J Biomol NMR 5 (1995) 67-81
    • (1995) J Biomol NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 34
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart D.S., Sykes B.D., and Richards F.M. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J Mol Biol. 222 (1991) 311-333
    • (1991) J Mol Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 35
    • 0001202015 scopus 로고
    • The relationship between chemical shift and secondary structure in proteins
    • Pastore A., and Saudek V. The relationship between chemical shift and secondary structure in proteins. J Magn Res 90 (1990) 165-176
    • (1990) J Magn Res , vol.90 , pp. 165-176
    • Pastore, A.1    Saudek, V.2
  • 37
    • 0021764802 scopus 로고
    • Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances
    • Wüthrich K., Billeter M., and Braun W. Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances. J Mol Biol. 180 (1984) 715-740
    • (1984) J Mol Biol. , vol.180 , pp. 715-740
    • Wüthrich, K.1    Billeter, M.2    Braun, W.3
  • 38
    • 0027379001 scopus 로고
    • 3-dimensional structure in solution of the calcium channel - conotoxin
    • Pallaghy P.K., Duggan B.M., Pennington M.W., and Norton R.S. 3-dimensional structure in solution of the calcium channel - conotoxin. J Mol Biol 234 (1993) 405-420
    • (1993) J Mol Biol , vol.234 , pp. 405-420
    • Pallaghy, P.K.1    Duggan, B.M.2    Pennington, M.W.3    Norton, R.S.4
  • 39
    • 0034327349 scopus 로고    scopus 로고
    • Prediction of tight turns and their types in proteins
    • Chou K. Prediction of tight turns and their types in proteins. Anal Biochem 286 (2000) 1-16
    • (2000) Anal Biochem , vol.286 , pp. 1-16
    • Chou, K.1
  • 40
    • 56249141566 scopus 로고    scopus 로고
    • Psort 11 Prediction (experimental)-http://psort.nibb.ac.ip/form2.html.
    • Psort 11 Prediction (experimental)-http://psort.nibb.ac.ip/form2.html.
  • 41
    • 56249123026 scopus 로고    scopus 로고
    • Liu Y, Jackway RJ, Surinya-Johnson KH, Bowie JH. Unpublished work.
    • Liu Y, Jackway RJ, Surinya-Johnson KH, Bowie JH. Unpublished work.
  • 43
    • 3943107651 scopus 로고    scopus 로고
    • Two new species of frogs (ANURA): Myobatrachidae (Pelodryadidae) from Queensland and New South Wales
    • Liem D.S., and Ingram G.J. Two new species of frogs (ANURA): Myobatrachidae (Pelodryadidae) from Queensland and New South Wales. Vic Nat 94 (1997) 255-262
    • (1997) Vic Nat , vol.94 , pp. 255-262
    • Liem, D.S.1    Ingram, G.J.2
  • 47
    • 0024345741 scopus 로고
    • Synthesis and binding affinities of cyclic and related linear analogues of CCK8 selective for central receptors
    • Charpentier B., Dor A., Roy P., England P., Pham H., Durieux C., and Roques B.P. Synthesis and binding affinities of cyclic and related linear analogues of CCK8 selective for central receptors. J Med Chem 32 (1989) 1184-1190
    • (1989) J Med Chem , vol.32 , pp. 1184-1190
    • Charpentier, B.1    Dor, A.2    Roy, P.3    England, P.4    Pham, H.5    Durieux, C.6    Roques, B.P.7
  • 48
    • 35349020391 scopus 로고    scopus 로고
    • Further evidence for a C-terminal structural motif in CCK2 receptor active peptide hormones
    • Stone S.R., Giragossian C., Mierke D.F., and Jackson G.E. Further evidence for a C-terminal structural motif in CCK2 receptor active peptide hormones. Peptides 28 (2007) 2211-2222
    • (2007) Peptides , vol.28 , pp. 2211-2222
    • Stone, S.R.1    Giragossian, C.2    Mierke, D.F.3    Jackson, G.E.4
  • 49
    • 0038706380 scopus 로고    scopus 로고
    • Antimicrobial peptides from hylid and ranid frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but hypermutable antimicrobial domain
    • Vanhoye D., Bruston F., Nicolas P., and Amiche M. Antimicrobial peptides from hylid and ranid frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but hypermutable antimicrobial domain. Eur J Biochem 270 (2003) 2068-2081
    • (2003) Eur J Biochem , vol.270 , pp. 2068-2081
    • Vanhoye, D.1    Bruston, F.2    Nicolas, P.3    Amiche, M.4
  • 51
    • 56249146104 scopus 로고    scopus 로고
    • http://earth.leeds.ac.uk/~eargah/Gond.html.
    • http://earth.leeds.ac.uk/~eargah/Gond.html.


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