메뉴 건너뛰기




Volumn 172, Issue 2, 2011, Pages 314-320

Caerulein-and xenopsin-related peptides with insulin-releasing activities from skin secretions of the clawed frogs, Xenopus borealis and Xenopus amieti (Pipidae)

Author keywords

Caerulein; Frog skin secretions; Insulin release; Mass spectrometry; Xenopsin; Xenopus

Indexed keywords

CAERULEIN RELATED PEPTIDE; CERULETIDE; INSULIN; LACTATE DEHYDROGENASE; NORADRENALIN; UNCLASSIFIED DRUG; XENOPSIN; XENOPSIN RELATED PEPTIDE;

EID: 79955725315     PISSN: 00166480     EISSN: 10956840     Source Type: Journal    
DOI: 10.1016/j.ygcen.2011.03.022     Document Type: Article
Times cited : (24)

References (38)
  • 1
    • 0032881940 scopus 로고    scopus 로고
    • N-terminal glycation of cholecystokinin-8 abolishes its insulinotropic action on clonal pancreatic B-cells
    • Abdel-Wahab Y.H., O'Harte F.P., Mooney M.H., Conlon J.M., Flatt P.R. N-terminal glycation of cholecystokinin-8 abolishes its insulinotropic action on clonal pancreatic B-cells. Biochim. Biophys. Acta 1999, 1452:60-67.
    • (1999) Biochim. Biophys. Acta , vol.1452 , pp. 60-67
    • Abdel-Wahab, Y.H.1    O'Harte, F.P.2    Mooney, M.H.3    Conlon, J.M.4    Flatt, P.R.5
  • 2
    • 55949094899 scopus 로고    scopus 로고
    • A peptide of the phylloseptin family from the skin of the frog Hylomantis lemur (Phyllomedusinae) with potent in vitro and in vivo insulin-releasing activity
    • Abdel-Wahab Y.H., Power G.J., Flatt P.R., Woodhams D.C., Rollins-Smith L.A., Conlon J.M. A peptide of the phylloseptin family from the skin of the frog Hylomantis lemur (Phyllomedusinae) with potent in vitro and in vivo insulin-releasing activity. Peptides 2008, 29:2136-2143.
    • (2008) Peptides , vol.29 , pp. 2136-2143
    • Abdel-Wahab, Y.H.1    Power, G.J.2    Flatt, P.R.3    Woodhams, D.C.4    Rollins-Smith, L.A.5    Conlon, J.M.6
  • 4
    • 0022428451 scopus 로고
    • Solid-phase synthesis of PYLa and isolation of its natural counterpart, PGLa [PYLa-(4-24)] from skin secretion of Xenopus laevis
    • Andreu D., Aschauer H., Kreil G., Merrifield R.B. Solid-phase synthesis of PYLa and isolation of its natural counterpart, PGLa [PYLa-(4-24)] from skin secretion of Xenopus laevis. Eur. J. Biochem. 1985, 149:531-535.
    • (1985) Eur. J. Biochem. , vol.149 , pp. 531-535
    • Andreu, D.1    Aschauer, H.2    Kreil, G.3    Merrifield, R.B.4
  • 5
    • 0015720366 scopus 로고
    • Isolation and structure of a new active peptide " Xenopsin" on the smooth muscle, especially on a strip of fundus from a rat stomach, from the skin of Xenopus laevis
    • Araki K., Tachibana S., Uchiyama M., Nakajima T., Yasuhara T. Isolation and structure of a new active peptide " Xenopsin" on the smooth muscle, especially on a strip of fundus from a rat stomach, from the skin of Xenopus laevis. Chem. Pharm. Bull. (Tokyo) 1973, 21:2801-2804.
    • (1973) Chem. Pharm. Bull. (Tokyo) , vol.21 , pp. 2801-2804
    • Araki, K.1    Tachibana, S.2    Uchiyama, M.3    Nakajima, T.4    Yasuhara, T.5
  • 6
    • 0024156895 scopus 로고
    • Xenopus skin mucus induces oral dyskinesias that promote escape from snakes
    • Barthalmus G.T., Zielinski W.J. Xenopus skin mucus induces oral dyskinesias that promote escape from snakes. Pharmacol. Biochem. Behav. 1988, 30:957-959.
    • (1988) Pharmacol. Biochem. Behav. , vol.30 , pp. 957-959
    • Barthalmus, G.T.1    Zielinski, W.J.2
  • 7
    • 0019983579 scopus 로고
    • Co-existence of thyrotrophin releasing hormone and 5-hydroxytryptamine in the skin of Xenopus laevis
    • Bennett G.W., Marsden C.A., Clothier R.M., Waters A.D., Balls M. Co-existence of thyrotrophin releasing hormone and 5-hydroxytryptamine in the skin of Xenopus laevis. Comp. Biochem. Physiol. C 1982, 72:257-261.
    • (1982) Comp. Biochem. Physiol. C , vol.72 , pp. 257-261
    • Bennett, G.W.1    Marsden, C.A.2    Clothier, R.M.3    Waters, A.D.4    Balls, M.5
  • 8
    • 0014347915 scopus 로고
    • The actions of caerulein on the smooth muscle of the gastrointestinal tract and the gall bladder
    • Bertaccini G., De Caro G., Endean R., Erspamer V., Impicciatore M. The actions of caerulein on the smooth muscle of the gastrointestinal tract and the gall bladder. Br. J. Pharmacol. 1968, 34:291-310.
    • (1968) Br. J. Pharmacol. , vol.34 , pp. 291-310
    • Bertaccini, G.1    De Caro, G.2    Endean, R.3    Erspamer, V.4    Impicciatore, M.5
  • 9
    • 84882894909 scopus 로고    scopus 로고
    • Host defense peptides from Australian amphibians: caerulein and other neuropeptides
    • Elsevier Science, Amsterdam, A.J. Kastin (Ed.)
    • Bowie J.H., Tyler M.J. Host defense peptides from Australian amphibians: caerulein and other neuropeptides. Handbook of Biologically Active Peptides 2006, 283-289. Elsevier Science, Amsterdam. A.J. Kastin (Ed.).
    • (2006) Handbook of Biologically Active Peptides , pp. 283-289
    • Bowie, J.H.1    Tyler, M.J.2
  • 10
    • 0025078549 scopus 로고
    • Neurotensin-related peptides inhibit spontaneous longitudinal contractions of porcine distal jejunum
    • Brown D.R., Carraway R.E., Parsons A.M., Mitra S.P. Neurotensin-related peptides inhibit spontaneous longitudinal contractions of porcine distal jejunum. Peptides 1990, 11:713-718.
    • (1990) Peptides , vol.11 , pp. 713-718
    • Brown, D.R.1    Carraway, R.E.2    Parsons, A.M.3    Mitra, S.P.4
  • 11
    • 0032911441 scopus 로고    scopus 로고
    • Characterization of high affinity neurotensin receptor NTR1 in HL-60 cells and its down regulation during granulocytic differentiation
    • Choi S.Y., Chae H.D., Park T.J., Ha H., Kim K.T. Characterization of high affinity neurotensin receptor NTR1 in HL-60 cells and its down regulation during granulocytic differentiation. Br. J. Pharmacol. 1999, 126:1050-1056.
    • (1999) Br. J. Pharmacol. , vol.126 , pp. 1050-1056
    • Choi, S.Y.1    Chae, H.D.2    Park, T.J.3    Ha, H.4    Kim, K.T.5
  • 12
    • 77952106772 scopus 로고    scopus 로고
    • Orthologs of magainin, PGLa, procaerulein-derived, and proxenopsin-derived peptides from skin secretions of the octoploid frog Xenopus amieti (Pipidae)
    • Conlon J.M., Al-Ghaferi N., Ahmed E., Meetani M.A., Leprince J., Nielsen P.F. Orthologs of magainin, PGLa, procaerulein-derived, and proxenopsin-derived peptides from skin secretions of the octoploid frog Xenopus amieti (Pipidae). Peptides 2010, 31:989-994.
    • (2010) Peptides , vol.31 , pp. 989-994
    • Conlon, J.M.1    Al-Ghaferi, N.2    Ahmed, E.3    Meetani, M.A.4    Leprince, J.5    Nielsen, P.F.6
  • 13
    • 0015892959 scopus 로고
    • Active polypeptides of the amphibian skin and their synthetic analogues
    • Erspamer V., Melchiorri P. Active polypeptides of the amphibian skin and their synthetic analogues. Pure Appl. Chem. 1973, 35:463-494.
    • (1973) Pure Appl. Chem. , vol.35 , pp. 463-494
    • Erspamer, V.1    Melchiorri, P.2
  • 14
    • 4344713315 scopus 로고    scopus 로고
    • A mitochondrial DNA phylogeny of African clawed frogs: phylogeography and implications for polyploid evolution
    • Evans B.J., Kelley D.B., Tinsley R.C., Melnick D.J., Cannatella D.C. A mitochondrial DNA phylogeny of African clawed frogs: phylogeography and implications for polyploid evolution. Mol. Phylogenet. Evol. 2004, 33:197-213.
    • (2004) Mol. Phylogenet. Evol. , vol.33 , pp. 197-213
    • Evans, B.J.1    Kelley, D.B.2    Tinsley, R.C.3    Melnick, D.J.4    Cannatella, D.C.5
  • 15
    • 0019471997 scopus 로고
    • Abnormal plasma glucose and insulin responses in heterozygous lean (ob/+) mice
    • Flatt P.R., Bailey C.J. Abnormal plasma glucose and insulin responses in heterozygous lean (ob/+) mice. Diabetelogia 1981, 20:573-577.
    • (1981) Diabetelogia , vol.20 , pp. 573-577
    • Flatt, P.R.1    Bailey, C.J.2
  • 16
    • 65549144889 scopus 로고    scopus 로고
    • Recent advances in antidiabetic drug therapies targeting the enteroinsular axis
    • Flatt P.R., Bailey C.J., Green B.D. Recent advances in antidiabetic drug therapies targeting the enteroinsular axis. Curr. Drug Metab. 2009, 10:125-137.
    • (2009) Curr. Drug Metab. , vol.10 , pp. 125-137
    • Flatt, P.R.1    Bailey, C.J.2    Green, B.D.3
  • 17
    • 85029624696 scopus 로고    scopus 로고
    • Amphibian species of the world: an online reference, Version 5.5, American Museum of Natural History, New York, USA, 2011, Electronic database accessible at
    • D.R. Frost, Amphibian species of the world: an online reference, Version 5.5, American Museum of Natural History, New York, USA, 2011, Electronic database accessible at http://research.amnh.org/herpetology/amphibia/index.php.
    • Frost, D.R.1
  • 18
    • 0022996088 scopus 로고
    • Novel peptide fragments originating from PGLa and the caerulein and xenopsin precursors from Xenopus laevis
    • Gibson B.W., Poulter L., Williams D.H., Maggio J.E. Novel peptide fragments originating from PGLa and the caerulein and xenopsin precursors from Xenopus laevis. J. Biol. Chem. 1986, 261:5341-5349.
    • (1986) J. Biol. Chem. , vol.261 , pp. 5341-5349
    • Gibson, B.W.1    Poulter, L.2    Williams, D.H.3    Maggio, J.E.4
  • 19
    • 0023100945 scopus 로고
    • Biosynthesis and degradation of peptides derived from Xenopus laevis prohormones
    • Giovannini M.G., Poulter L., Gibson B.W., Williams D.H. Biosynthesis and degradation of peptides derived from Xenopus laevis prohormones. Biochem. J. 1987, 243:113-120.
    • (1987) Biochem. J. , vol.243 , pp. 113-120
    • Giovannini, M.G.1    Poulter, L.2    Gibson, B.W.3    Williams, D.H.4
  • 20
    • 0026681653 scopus 로고
    • A new member of the P-domain peptide family of potential growth factors, is synthesized in Xenopus laevis skin
    • Hauser F., Roeben C., Hoffmann W. A new member of the P-domain peptide family of potential growth factors, is synthesized in Xenopus laevis skin. J. Biol. Chem. 1992, 267:14451-14455.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14451-14455
    • Hauser, F.1    Roeben, C.2    Hoffmann, W.3
  • 21
    • 85029653404 scopus 로고    scopus 로고
    • International Diabetes Federation Diabetes Atlas, Electronic Database accessible at
    • International Diabetes Federation Diabetes Atlas, 2010, Electronic Database accessible at http://www.diabetesatlas.org.
    • (2010)
  • 22
    • 0028008878 scopus 로고
    • Purification of antimicrobial peptides from an extract of the skin of Xenopus laevis using heparin-affinity HPLC: characterization by ion-spray mass spectrometry
    • James S., Gibbs B.F., Toney K., Bennett H.P. Purification of antimicrobial peptides from an extract of the skin of Xenopus laevis using heparin-affinity HPLC: characterization by ion-spray mass spectrometry. Anal. Biochem. 1994, 217:84-90.
    • (1994) Anal. Biochem. , vol.217 , pp. 84-90
    • James, S.1    Gibbs, B.F.2    Toney, K.3    Bennett, H.P.4
  • 23
    • 0023814410 scopus 로고    scopus 로고
    • Effects of neurotensin-related peptides on the motility of the guinea pig oesophagus
    • Katsoulis S., Conlon J.M. Effects of neurotensin-related peptides on the motility of the guinea pig oesophagus. Eur. J. Pharmacol. 1998, 152:363-366.
    • (1998) Eur. J. Pharmacol. , vol.152 , pp. 363-366
    • Katsoulis, S.1    Conlon, J.M.2
  • 26
    • 0027219233 scopus 로고
    • Xenoxins, a family of peptides from dorsal gland secretion of Xenopus laevis related to snake venom cytotoxins and neurotoxins
    • Kolbe H.V., Huber A., Cordier P., Rasmussen U.B., Bouchon B., Jaquinod M., Vlasak R., Délot E.C., Kreil G. Xenoxins, a family of peptides from dorsal gland secretion of Xenopus laevis related to snake venom cytotoxins and neurotoxins. J. Biol. Chem. 1993, 268:16458-16464.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16458-16464
    • Kolbe, H.V.1    Huber, A.2    Cordier, P.3    Rasmussen, U.B.4    Bouchon, B.5    Jaquinod, M.6    Vlasak, R.7    Délot, E.C.8    Kreil, G.9
  • 27
    • 0032493740 scopus 로고    scopus 로고
    • Isolation of a member of the neurotoxin/cytotoxin peptide family from Xenopus laevis skin which activates dihydropyridine-sensitive Ca2+ channels in mammalian epithelial cells
    • Macleod R.J., Lembessis P., James S., Bennett H.P. Isolation of a member of the neurotoxin/cytotoxin peptide family from Xenopus laevis skin which activates dihydropyridine-sensitive Ca2+ channels in mammalian epithelial cells. J. Biol. Chem. 1998, 273:20046-20051.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20046-20051
    • Macleod, R.J.1    Lembessis, P.2    James, S.3    Bennett, H.P.4
  • 30
    • 78649578592 scopus 로고    scopus 로고
    • Investigation of the pyrolysis products of methionine-enkephalin-Arg-Gly-Leu using liquid chromatography-tandem mass spectrometry
    • Meetani M.A., Zahid O.K., Conlon J.M. Investigation of the pyrolysis products of methionine-enkephalin-Arg-Gly-Leu using liquid chromatography-tandem mass spectrometry. J. Mass Spectrom. 2010, 45:1320-1331.
    • (2010) J. Mass Spectrom. , vol.45 , pp. 1320-1331
    • Meetani, M.A.1    Zahid, O.K.2    Conlon, J.M.3
  • 32
  • 33
    • 0018574953 scopus 로고
    • Effect of caerulein on exocrine and endocrine pancreas in the rat
    • Otsuki M., Sakamoto C., Maeda M., Yuu H., Morita S., Baba S. Effect of caerulein on exocrine and endocrine pancreas in the rat. Endocrinology 1979, 105:1396-1399.
    • (1979) Endocrinology , vol.105 , pp. 1396-1399
    • Otsuki, M.1    Sakamoto, C.2    Maeda, M.3    Yuu, H.4    Morita, S.5    Baba, S.6
  • 35
    • 0031778623 scopus 로고    scopus 로고
    • Different actions of CCK on pancreatic and gastric growth in the rat: effect of CCK(A) receptor blockade
    • Varga G., Kisfalvi K., Pelosini I., D'Amato M., Scarpignato C. Different actions of CCK on pancreatic and gastric growth in the rat: effect of CCK(A) receptor blockade. Br. J. Pharmacol. 1998, 124:435-440.
    • (1998) Br. J. Pharmacol. , vol.124 , pp. 435-440
    • Varga, G.1    Kisfalvi, K.2    Pelosini, I.3    D'Amato, M.4    Scarpignato, C.5
  • 36
    • 0032786091 scopus 로고    scopus 로고
    • Caerulein-like peptides from the skin glands of the Australian Blue Mountains tree frog Litoria citropa. Part 1: Sequence determination using electrospray mass spectrometry
    • Wabnitz P.A., Bowie J.H., Tyler M.J. Caerulein-like peptides from the skin glands of the Australian Blue Mountains tree frog Litoria citropa. Part 1: Sequence determination using electrospray mass spectrometry. Rapid Commun. Mass Spectrom. 1999, 13:2498-2502.
    • (1999) Rapid Commun. Mass Spectrom. , vol.13 , pp. 2498-2502
    • Wabnitz, P.A.1    Bowie, J.H.2    Tyler, M.J.3
  • 37
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms and partial cDNA sequence of a precursor
    • Zasloff M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA 1987, 84:5449-5453.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 38
    • 0020183948 scopus 로고
    • Effect of xenopsin on blood flow, hormone release, and acid secretion
    • Zinner M.J., Kasher F., Modlin I.M., Jaffe B.M. Effect of xenopsin on blood flow, hormone release, and acid secretion. Am. J. Physiol. 1982, 243:G195-G199.
    • (1982) Am. J. Physiol. , vol.243
    • Zinner, M.J.1    Kasher, F.2    Modlin, I.M.3    Jaffe, B.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.