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Volumn 389, Issue 2, 2008, Pages 143-148

Insulin-releasing properties of the frog skin peptide pseudin-2 and its [Lys18]-substituted analogue

Author keywords

Frog skin; Insulin secretion; Pseudin 2; Type 2 diabetes

Indexed keywords

INSULIN; LACTATE DEHYDROGENASE; LYSINE; PEPTIDE; PEPTIDE PSEUDIN 2; UNCLASSIFIED DRUG;

EID: 38649103176     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2008.018     Document Type: Article
Times cited : (38)

References (23)
  • 1
    • 26844462726 scopus 로고    scopus 로고
    • Isolation and structural characterization of a novel 13-amino acid insulin-releasing peptide from the skin secretion of Agalychnis calcarifer
    • Abdel-Wahab, Y.H.A., Marenah, L., Orr D.F., Shaw, C., and Flatt, P.R. (2005). Isolation and structural characterization of a novel 13-amino acid insulin-releasing peptide from the skin secretion of Agalychnis calcarifer. Biol. Chem. 386, 581-587.
    • (2005) Biol. Chem , vol.386 , pp. 581-587
    • Abdel-Wahab, Y.H.A.1    Marenah, L.2    Orr, D.F.3    Shaw, C.4    Flatt, P.R.5
  • 2
    • 34548675371 scopus 로고    scopus 로고
    • Abdel-Wahab, Y.H.A., Maranah, L., Flatt, P.R., and Conlon, J.M. (2007). Insulin releasing properties of the temporin family of antimicrobial peptides. Pept. Protein Lett. 14, 702-707.
    • Abdel-Wahab, Y.H.A., Maranah, L., Flatt, P.R., and Conlon, J.M. (2007). Insulin releasing properties of the temporin family of antimicrobial peptides. Pept. Protein Lett. 14, 702-707.
  • 3
    • 0021741559 scopus 로고
    • Glucose induces closure of single potassium channels in isolated rat pancreatic β-cells
    • Ashcroft, F.M., Harrison, D.E., and Ashcroft, S.J. (1984). Glucose induces closure of single potassium channels in isolated rat pancreatic β-cells. Nature 312, 446-448.
    • (1984) Nature , vol.312 , pp. 446-448
    • Ashcroft, F.M.1    Harrison, D.E.2    Ashcroft, S.J.3
  • 4
    • 0030689711 scopus 로고    scopus 로고
    • The natural history of amphibian skin secretions, their normal functional and potential medical applications
    • Clarke, B.T. (1997). The natural history of amphibian skin secretions, their normal functional and potential medical applications. Biol. Rev. Camb. Philos. Soc. 72, 365-379.
    • (1997) Biol. Rev. Camb. Philos. Soc , vol.72 , pp. 365-379
    • Clarke, B.T.1
  • 5
    • 3242717490 scopus 로고    scopus 로고
    • The therapeutic potential of antimicrobial peptides from frog skin
    • Conlon, J.M. (2004). The therapeutic potential of antimicrobial peptides from frog skin. Rev. Med. Microbiol. 15, 17-25.
    • (2004) Rev. Med. Microbiol , vol.15 , pp. 17-25
    • Conlon, J.M.1
  • 6
    • 33748504146 scopus 로고    scopus 로고
    • Major contributions of comparative endocrinology to the development and exploitation of the incretin concept
    • Conlon, J.M., Patterson, S., and Flatt, P.R. (2006). Major contributions of comparative endocrinology to the development and exploitation of the incretin concept. J. Exp. Zool. 305A, 781-786.
    • (2006) J. Exp. Zool , vol.305 A , pp. 781-786
    • Conlon, J.M.1    Patterson, S.2    Flatt, P.R.3
  • 7
    • 0019471997 scopus 로고
    • Abnormal plasma glucose and insulin responses in heterozygous lean (ob/+) mice
    • Flatt, P.R. and Bailey, C.J. (1981). Abnormal plasma glucose and insulin responses in heterozygous lean (ob/+) mice. Diabetologia 20, 573-577.
    • (1981) Diabetologia , vol.20 , pp. 573-577
    • Flatt, P.R.1    Bailey, C.J.2
  • 8
    • 2942615064 scopus 로고    scopus 로고
    • Brevinin-1 and multiple insulin-releasing peptides in the skin of frog Rana palustris
    • Marenah, L., Flatt, P.R., Orr, D.F., McClean, S., Shaw, C., and Abdel-Wahab, Y.H.A. (2004a). Brevinin-1 and multiple insulin-releasing peptides in the skin of frog Rana palustris. J. Endocrinol. 181, 347-354.
    • (2004) J. Endocrinol , vol.181 , pp. 347-354
    • Marenah, L.1    Flatt, P.R.2    Orr, D.F.3    McClean, S.4    Shaw, C.5    Abdel-Wahab, Y.H.A.6
  • 9
    • 2542494931 scopus 로고    scopus 로고
    • Skin secretion of the toad Bombina variegata contains multiple insulin-releasing peptides including bombesin and entirely novel insulinotropic structures
    • Marenah, L., Flatt, P.R., Orr, D.F., McClean, S., Shaw, C., and Abdel-Wahab, Y.H.A. (2004b). Skin secretion of the toad Bombina variegata contains multiple insulin-releasing peptides including bombesin and entirely novel insulinotropic structures. Biol. Chem. 385, 315-321.
    • (2004) Biol. Chem , vol.385 , pp. 315-321
    • Marenah, L.1    Flatt, P.R.2    Orr, D.F.3    McClean, S.4    Shaw, C.5    Abdel-Wahab, Y.H.A.6
  • 10
    • 2642559433 scopus 로고    scopus 로고
    • Isolation and characterization of an unexpected class of insulinotropic peptides in the skin of the frog Agalychnis litodryas
    • Marenah, L., Shaw, C., Orr, D.F., McClean, S., Flatt, P.R., and Abdel-Wahab, Y.H.A. (2004c). Isolation and characterization of an unexpected class of insulinotropic peptides in the skin of the frog Agalychnis litodryas. Regul. Pept. 120, 33-38.
    • (2004) Regul. Pept , vol.120 , pp. 33-38
    • Marenah, L.1    Shaw, C.2    Orr, D.F.3    McClean, S.4    Flatt, P.R.5    Abdel-Wahab, Y.H.A.6
  • 11
    • 3242746894 scopus 로고    scopus 로고
    • Novel insulin releasing peptides in the skin of Phyllomedusa trinitatis frog includes 28 amino acid peptide from dermaseptin BIV precursor
    • Marenah, L., McClean, S., Flatt, P.R., Orr, D.F., Shaw, C., and Abdel-Wahab, Y.H.A. (2004d). Novel insulin releasing peptides in the skin of Phyllomedusa trinitatis frog includes 28 amino acid peptide from dermaseptin BIV precursor. Pancreas 29, 110-115.
    • (2004) Pancreas , vol.29 , pp. 110-115
    • Marenah, L.1    McClean, S.2    Flatt, P.R.3    Orr, D.F.4    Shaw, C.5    Abdel-Wahab, Y.H.A.6
  • 12
    • 27744595390 scopus 로고    scopus 로고
    • Characterization of naturally occurring peptides in the skin secretion of Rana pipiens frog reveal pipinin-1 as the novel insulin releasing peptide
    • Marenah, L., McClean, S., Flatt, P.R., Orr, D.F., Shaw, C., and Abdel-Wahab, Y.H.A. (2005). Characterization of naturally occurring peptides in the skin secretion of Rana pipiens frog reveal pipinin-1 as the novel insulin releasing peptide. Peptides 26, 2117-2123.
    • (2005) Peptides , vol.26 , pp. 2117-2123
    • Marenah, L.1    McClean, S.2    Flatt, P.R.3    Orr, D.F.4    Shaw, C.5    Abdel-Wahab, Y.H.A.6
  • 13
    • 31544471813 scopus 로고    scopus 로고
    • Skin secretions of Rana saharica frogs reveal antimicrobial peptides esculentins-1 and -1B and brevinins-1E and -2EC with novel insulin releasing activity
    • Marenah, L., Flatt, P.R., Orr, D.F., McClean, S., Shaw, C., and Abdel-Wahab, Y.H.A. (2006). Skin secretions of Rana saharica frogs reveal antimicrobial peptides esculentins-1 and -1B and brevinins-1E and -2EC with novel insulin releasing activity. J. Endocrinol. 188, 1-9.
    • (2006) J. Endocrinol , vol.188 , pp. 1-9
    • Marenah, L.1    Flatt, P.R.2    Orr, D.F.3    McClean, S.4    Shaw, C.5    Abdel-Wahab, Y.H.A.6
  • 14
    • 33645537215 scopus 로고    scopus 로고
    • Asparagus adscendens (Shweta musali) stimulates insulin secretion, insulin action and inhibits starch digestion
    • Mathews, J.N., Flatt, P.R., and Abdel-Wahab, Y.H.A. (2006). Asparagus adscendens (Shweta musali) stimulates insulin secretion, insulin action and inhibits starch digestion. Br. J. Nutr. 95, 576-581.
    • (2006) Br. J. Nutr , vol.95 , pp. 576-581
    • Mathews, J.N.1    Flatt, P.R.2    Abdel-Wahab, Y.H.A.3
  • 15
    • 0030067124 scopus 로고    scopus 로고
    • Metabolic regulation inspired by the glucokinase glucose sensor paradigm
    • Matschinsky, F.M. (1996). Metabolic regulation inspired by the glucokinase glucose sensor paradigm. Diabetes 45, 223-241.
    • (1996) Diabetes , vol.45 , pp. 223-241
    • Matschinsky, F.M.1
  • 16
    • 0033123538 scopus 로고    scopus 로고
    • Physiological and pharmacological regulation of insulin release: Insights offered through exploitation of insulin-secreting cell lines
    • McClenaghan, N.H. and Flatt, P.R. (1999). Physiological and pharmacological regulation of insulin release: insights offered through exploitation of insulin-secreting cell lines. Diabetes Obes. Metab. 1, 137-50.
    • (1999) Diabetes Obes. Metab , vol.1 , pp. 137-150
    • McClenaghan, N.H.1    Flatt, P.R.2
  • 19
    • 0029071517 scopus 로고
    • Metabolic coupling factors in pancreatic β-cell signal transduction
    • Newgard, C.B. and McGarry, J.D. (1995). Metabolic coupling factors in pancreatic β-cell signal transduction. Annu. Rev. Biochem. 64, 689-719.
    • (1995) Annu. Rev. Biochem , vol.64 , pp. 689-719
    • Newgard, C.B.1    McGarry, J.D.2
  • 20
    • 0035834573 scopus 로고    scopus 로고
    • Pseudin-2: An antimicrobial peptide with low hemolytic activity from the skin of the paradoxical frog
    • Olson, L., Soto, A., Knoop, F.C., and Conlon, J.M. (2001). Pseudin-2: an antimicrobial peptide with low hemolytic activity from the skin of the paradoxical frog. Biochem. Biophys. Res. Commun. 288, 1001-1005.
    • (2001) Biochem. Biophys. Res. Commun , vol.288 , pp. 1001-1005
    • Olson, L.1    Soto, A.2    Knoop, F.C.3    Conlon, J.M.4
  • 21
    • 20144376875 scopus 로고    scopus 로고
    • Design of potent, non-toxic antimicrobial agents based upon the structure of the frog skin peptide, pseudin-2
    • Pal, T., Sonnevend, A., Galadari, S., and Conlon, J.M. (2005). Design of potent, non-toxic antimicrobial agents based upon the structure of the frog skin peptide, pseudin-2. Regul. Pept. 129, 85-91.
    • (2005) Regul. Pept , vol.129 , pp. 85-91
    • Pal, T.1    Sonnevend, A.2    Galadari, S.3    Conlon, J.M.4
  • 22
    • 0036900093 scopus 로고    scopus 로고
    • Antimicrobial peptides from amphibian skin: An expanding scenario
    • Rinaldi, A.C. (2002). Antimicrobial peptides from amphibian skin: an expanding scenario. Curr. Opin. Chem. Biol. 6, 799-804.
    • (2002) Curr. Opin. Chem. Biol , vol.6 , pp. 799-804
    • Rinaldi, A.C.1
  • 23
    • 0014062165 scopus 로고
    • Use of helical wheels to represent the structures of proteins and to identify segments with helical potential
    • Schiffer, M., and Edmundson, A.B. (1967). Use of helical wheels to represent the structures of proteins and to identify segments with helical potential. Biophys. J. 7, 121-135.
    • (1967) Biophys. J , vol.7 , pp. 121-135
    • Schiffer, M.1    Edmundson, A.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.