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Volumn 78, Issue , 2013, Pages 245-253

The chains of the heterodimeric amphibian skin antimicrobial peptide, distinctin, are encoded by separate messenger RNAs

Author keywords

Amphibian skin peptides; CDNA cloning; Heterodimer; Homodimer; Intramolecular and intermolecular disulfide bonds; Peptidomics

Indexed keywords

AMPHIBIAN PROTEIN; DISTINCTIN; HETERODIMER; MESSENGER RNA; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG; VENOM;

EID: 84872677977     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.09.016     Document Type: Article
Times cited : (6)

References (42)
  • 1
    • 0028955594 scopus 로고
    • The chemistry of poisons in amphibian skin
    • Daly J.W. The chemistry of poisons in amphibian skin. Proc Natl Acad Sci U S A 1995, 92:9-13.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 9-13
    • Daly, J.W.1
  • 2
    • 0026493568 scopus 로고
    • Frog secretions and hunting magic in the upper Amazon: identification of a peptide that interacts with an adenosine receptor
    • Daly J.W., Caceres J., Moni R.W., Gusovsky F., Moos M., Seamon K.B., et al. Frog secretions and hunting magic in the upper Amazon: identification of a peptide that interacts with an adenosine receptor. Proc Natl Acad Sci U S A 1992, 89:10960-10963.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 10960-10963
    • Daly, J.W.1    Caceres, J.2    Moni, R.W.3    Gusovsky, F.4    Moos, M.5    Seamon, K.B.6
  • 4
    • 0020591183 scopus 로고
    • Amphibian skin peptides in mammals-looking ahead
    • Erspamer V. Amphibian skin peptides in mammals-looking ahead. Trends Neurosci 1983, 6:200-201.
    • (1983) Trends Neurosci , vol.6 , pp. 200-201
    • Erspamer, V.1
  • 5
    • 20044381842 scopus 로고    scopus 로고
    • Phylloseptins: a novel class of anti-bacterial and anti-protozoan peptides from the Phyllomedusa genus
    • Leite J.R., Silva L.P., Rodrigues M.I., Prates M.V., Brand G.D., Lacava B.M., et al. Phylloseptins: a novel class of anti-bacterial and anti-protozoan peptides from the Phyllomedusa genus. Peptides 2005, 26:565-573.
    • (2005) Peptides , vol.26 , pp. 565-573
    • Leite, J.R.1    Silva, L.P.2    Rodrigues, M.I.3    Prates, M.V.4    Brand, G.D.5    Lacava, B.M.6
  • 6
    • 78751575813 scopus 로고    scopus 로고
    • Antimicrobial peptides from Phyllomedusa frogs: from biomolecular diversity to potential nanotechnologic medical applications
    • de Azevedo Calderon L., Silva AdAE, Ciancaglini P., Stabeli R.G. Antimicrobial peptides from Phyllomedusa frogs: from biomolecular diversity to potential nanotechnologic medical applications. Amino Acids 2011, 40:29-49.
    • (2011) Amino Acids , vol.40 , pp. 29-49
    • de Azevedo Calderon, L.1    Silva, A.2    Ciancaglini, P.3    Stabeli, R.G.4
  • 7
    • 33646087190 scopus 로고    scopus 로고
    • Cloning from tissue surrogates: antimicrobial peptide (esculentin) cDNAs from the defensive skin secretions of Chinese ranid frogs
    • Chen T., Zhou M., Chen W., Lorimer J., Rao P., Walker B., et al. Cloning from tissue surrogates: antimicrobial peptide (esculentin) cDNAs from the defensive skin secretions of Chinese ranid frogs. Genomics 2006, 87:638-644.
    • (2006) Genomics , vol.87 , pp. 638-644
    • Chen, T.1    Zhou, M.2    Chen, W.3    Lorimer, J.4    Rao, P.5    Walker, B.6
  • 8
    • 0242298262 scopus 로고    scopus 로고
    • Identification of three novel Phyllomedusa sauvagei dermaseptins (sVI-sVIII) by cloning from a skin secretion-derived cDNA library
    • Chen T., Tang L., Shaw C. Identification of three novel Phyllomedusa sauvagei dermaseptins (sVI-sVIII) by cloning from a skin secretion-derived cDNA library. Regul Pept 2003, 116:139-146.
    • (2003) Regul Pept , vol.116 , pp. 139-146
    • Chen, T.1    Tang, L.2    Shaw, C.3
  • 9
    • 33746933811 scopus 로고    scopus 로고
    • Elements of the granular gland peptidome and transcriptome persist in air-dried skin of the South American orange-legged leaf frog, Phyllomedusa hypocondrialis
    • Chen T., Zhou M., Gagliardo R., Walker B., Shaw C. Elements of the granular gland peptidome and transcriptome persist in air-dried skin of the South American orange-legged leaf frog, Phyllomedusa hypocondrialis. Peptides 2006, 27:2129-2136.
    • (2006) Peptides , vol.27 , pp. 2129-2136
    • Chen, T.1    Zhou, M.2    Gagliardo, R.3    Walker, B.4    Shaw, C.5
  • 11
    • 1242306544 scopus 로고    scopus 로고
    • Antimicrobial peptides from ranid frogs: taxonomic and phylogenetic markers and a potential source of new therapeutic agents
    • Conlon J.M., Kolodziejek J., Nowotny N. Antimicrobial peptides from ranid frogs: taxonomic and phylogenetic markers and a potential source of new therapeutic agents. Biochim Biophys Acta 2004, 1696:1-14.
    • (2004) Biochim Biophys Acta , vol.1696 , pp. 1-14
    • Conlon, J.M.1    Kolodziejek, J.2    Nowotny, N.3
  • 12
    • 33745002225 scopus 로고    scopus 로고
    • The Chinese bamboo leaf odorous frog (Rana (Odorrana) versabilis) and North American Rana frogs share the same families of skin antimicrobial peptides
    • Chen T., Zhou M., Rao P., Walker B., Shaw C. The Chinese bamboo leaf odorous frog (Rana (Odorrana) versabilis) and North American Rana frogs share the same families of skin antimicrobial peptides. Peptides 2006, 27:1738-1744.
    • (2006) Peptides , vol.27 , pp. 1738-1744
    • Chen, T.1    Zhou, M.2    Rao, P.3    Walker, B.4    Shaw, C.5
  • 13
    • 0037113127 scopus 로고    scopus 로고
    • Role of proline, cysteine and a disulphide bridge in the structure and activity of the anti-microbial peptide gaegurin 5
    • Park S.H., Kim H.E., Kim C.M., Yun H.J., Choi E.C., Lee B.J. Role of proline, cysteine and a disulphide bridge in the structure and activity of the anti-microbial peptide gaegurin 5. Biochem J 2002, 368:171-182.
    • (2002) Biochem J , vol.368 , pp. 171-182
    • Park, S.H.1    Kim, H.E.2    Kim, C.M.3    Yun, H.J.4    Choi, E.C.5    Lee, B.J.6
  • 14
    • 77749315461 scopus 로고    scopus 로고
    • Nigrocin-2 peptides from Chinese Odorrana frogs-integration of UPLC/MS/MS with molecular cloning in amphibian skin peptidome analysis
    • Wang L., Evaristo G., Zhou M., Pinkse M., Wang M., Xu Y., et al. Nigrocin-2 peptides from Chinese Odorrana frogs-integration of UPLC/MS/MS with molecular cloning in amphibian skin peptidome analysis. FEBS J 2010, 277:1519-1531.
    • (2010) FEBS J , vol.277 , pp. 1519-1531
    • Wang, L.1    Evaristo, G.2    Zhou, M.3    Pinkse, M.4    Wang, M.5    Xu, Y.6
  • 15
    • 34547834190 scopus 로고    scopus 로고
    • Purification and characterization of antimicrobial peptides from the skin secretion of Rana dybowskii
    • Kim S.S., Shim M.S., Chung J., Lim D.Y., Lee B.J. Purification and characterization of antimicrobial peptides from the skin secretion of Rana dybowskii. Peptides 2007, 28:1532-1539.
    • (2007) Peptides , vol.28 , pp. 1532-1539
    • Kim, S.S.1    Shim, M.S.2    Chung, J.3    Lim, D.Y.4    Lee, B.J.5
  • 16
    • 33748079108 scopus 로고    scopus 로고
    • A family of antimicrobial peptides related to japonicin-2 isolated from the skin of the chaochiao brown frog Rana chaochiaoensis
    • Conlon J.M., Leprince J., Vaudry H., Jiansheng H., Nielsen P.F. A family of antimicrobial peptides related to japonicin-2 isolated from the skin of the chaochiao brown frog Rana chaochiaoensis. Comp Biochem Physiol C Toxicol Pharmacol 2006, 144:101-105.
    • (2006) Comp Biochem Physiol C Toxicol Pharmacol , vol.144 , pp. 101-105
    • Conlon, J.M.1    Leprince, J.2    Vaudry, H.3    Jiansheng, H.4    Nielsen, P.F.5
  • 17
    • 0034094377 scopus 로고    scopus 로고
    • Isolation, structure, synthesis, and activity of a new member of the calcitonin gene-related peptide family from frog skin and molecular cloning of its precursor
    • Seon A.A., Pierre T.N., Redeker V., Lacombe C., Delfour A., Nicolas P., et al. Isolation, structure, synthesis, and activity of a new member of the calcitonin gene-related peptide family from frog skin and molecular cloning of its precursor. J Biol Chem 2000, 275:5934-5940.
    • (2000) J Biol Chem , vol.275 , pp. 5934-5940
    • Seon, A.A.1    Pierre, T.N.2    Redeker, V.3    Lacombe, C.4    Delfour, A.5    Nicolas, P.6
  • 19
    • 20944432603 scopus 로고    scopus 로고
    • A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin
    • Raimondo D., Andreotti G., Saint N., Amodeo P., Renzone G., Sanseverino M., et al. A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin. Proc Natl Acad Sci U S A 2005, 102:6309-6314.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 6309-6314
    • Raimondo, D.1    Andreotti, G.2    Saint, N.3    Amodeo, P.4    Renzone, G.5    Sanseverino, M.6
  • 20
    • 48249129108 scopus 로고    scopus 로고
    • Structural features of distinctin affecting peptide biological and biochemical properties
    • Dalla Serra M., Cirioni O., Vitale R.M., Renzone G., Coraiola M., Giacometti A., et al. Structural features of distinctin affecting peptide biological and biochemical properties. Biochemistry 2008, 47:7888-7899.
    • (2008) Biochemistry , vol.47 , pp. 7888-7899
    • Dalla Serra, M.1    Cirioni, O.2    Vitale, R.M.3    Renzone, G.4    Coraiola, M.5    Giacometti, A.6
  • 21
    • 67649262183 scopus 로고    scopus 로고
    • Structure, membrane orientation, mechanism, and function of pexiganan-a highly potent antimicrobial peptide designed from magainin
    • Gottler L.M., Ramamoorthy A. Structure, membrane orientation, mechanism, and function of pexiganan-a highly potent antimicrobial peptide designed from magainin. Biochim Biophys Acta 2009, 1788:1680-1686.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1680-1686
    • Gottler, L.M.1    Ramamoorthy, A.2
  • 22
    • 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., Bowie J.H. A novel method for the release and collection of dermal, glandular secretions from the skin of frogs. J Pharmacol Toxicol Methods 1992, 28:199-200.
    • (1992) J Pharmacol Toxicol Methods , vol.28 , pp. 199-200
    • Tyler, M.J.1    Stone, D.J.2    Bowie, J.H.3
  • 24
    • 78751584053 scopus 로고    scopus 로고
    • A genomic/proteomic approach to isolating and identifying bioactive peptides from the skin secretions of Phyllomedusa hypochondrialis azurea
    • Uniprot acccession number Q17UZ0 2006;Thesis:University of Ulster Coleraine, United Kingdom.
    • Thompson AH. A genomic/proteomic approach to isolating and identifying bioactive peptides from the skin secretions of Phyllomedusa hypochondrialis azurea. Uniprot acccession number Q17UZ0 2006;Thesis:University of Ulster Coleraine, United Kingdom.
    • Thompson, A.H.1
  • 25
    • 0036891096 scopus 로고    scopus 로고
    • Purification of pimplin, a paralytic heterodimeric polypeptide from venom of the parasitoid wasp Pimpla hypochondriaca, and cloning of the cDNA encoding one of the subunits
    • Parkinson N., Smith I., Audsley N., Edwards J.P. Purification of pimplin, a paralytic heterodimeric polypeptide from venom of the parasitoid wasp Pimpla hypochondriaca, and cloning of the cDNA encoding one of the subunits. Insect Biochem Mol Biol 2002, 32:1769-1773.
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 1769-1773
    • Parkinson, N.1    Smith, I.2    Audsley, N.3    Edwards, J.P.4
  • 26
    • 50149097016 scopus 로고    scopus 로고
    • Pilosulin 5, a novel histamine-releasing peptide of the Australian ant, Myrmecia pilosula (Jack Jumper Ant)
    • Inagaki H., Akagi M., Imai H.T., Taylor R.W., Wiese M.D., Davies N.W., et al. Pilosulin 5, a novel histamine-releasing peptide of the Australian ant, Myrmecia pilosula (Jack Jumper Ant). Arch Biochem Biophys 2008, 477:411-416.
    • (2008) Arch Biochem Biophys , vol.477 , pp. 411-416
    • Inagaki, H.1    Akagi, M.2    Imai, H.T.3    Taylor, R.W.4    Wiese, M.D.5    Davies, N.W.6
  • 27
    • 66049155827 scopus 로고    scopus 로고
    • Novel alpha D-conopeptides and their precursors identified by cDNA cloning define the D-conotoxin superfamily
    • Loughnan M.L., Nicke A., Lawrence N., Lewis R.J. Novel alpha D-conopeptides and their precursors identified by cDNA cloning define the D-conotoxin superfamily. Biochemistry 2009, 48:3717-3729.
    • (2009) Biochemistry , vol.48 , pp. 3717-3729
    • Loughnan, M.L.1    Nicke, A.2    Lawrence, N.3    Lewis, R.J.4
  • 28
    • 0034663075 scopus 로고    scopus 로고
    • Purification and cDNA cloning of salmorin that inhibits fibrinogen clotting
    • Koh Y., Chung K., Kim D. Purification and cDNA cloning of salmorin that inhibits fibrinogen clotting. Thromb Res 2000, 99:389-398.
    • (2000) Thromb Res , vol.99 , pp. 389-398
    • Koh, Y.1    Chung, K.2    Kim, D.3
  • 29
    • 67349253023 scopus 로고    scopus 로고
    • VGD and MLD-motifs containing heterodimeric disintegrin viplebedin-2 from Vipera lebetina snake venom. Purification and cDNA cloning
    • Vija H., Samel M., Siigur E., Aaspollu A., Tonismagi K., Trummal K., et al. VGD and MLD-motifs containing heterodimeric disintegrin viplebedin-2 from Vipera lebetina snake venom. Purification and cDNA cloning. Comp Biochem Physiol 2009, 153:253-260.
    • (2009) Comp Biochem Physiol , vol.153 , pp. 253-260
    • Vija, H.1    Samel, M.2    Siigur, E.3    Aaspollu, A.4    Tonismagi, K.5    Trummal, K.6
  • 31
    • 0037591683 scopus 로고    scopus 로고
    • Snake venom disintegrins: novel dimeric disintegrins and structural diversification by disulphide bond engineering
    • Calvete J.J., Moreno-Murciano M.P., Theakston R.D., Kisiel D.G., Marcinkiewicz C. Snake venom disintegrins: novel dimeric disintegrins and structural diversification by disulphide bond engineering. Biochem J 2003, 372:725-734.
    • (2003) Biochem J , vol.372 , pp. 725-734
    • Calvete, J.J.1    Moreno-Murciano, M.P.2    Theakston, R.D.3    Kisiel, D.G.4    Marcinkiewicz, C.5
  • 32
    • 59649116734 scopus 로고    scopus 로고
    • Irditoxin, a novel covalently linked heterodimeric three-finger toxin with high taxon-specific neurotoxicity
    • Pawlak J., Mackessy S.P., Sixberry N.M., Stura E.A., Le Du M.H., Menez R., et al. Irditoxin, a novel covalently linked heterodimeric three-finger toxin with high taxon-specific neurotoxicity. FASEB J 2009, 23:534-545.
    • (2009) FASEB J , vol.23 , pp. 534-545
    • Pawlak, J.1    Mackessy, S.P.2    Sixberry, N.M.3    Stura, E.A.4    Le Du, M.H.5    Menez, R.6
  • 33
    • 0030946126 scopus 로고    scopus 로고
    • The mechanism of inhibition of ryanodine receptor channels by imperatoxin I, a heterodimeric protein from the scorpion Pandinus imperator
    • Zamudio F.Z., Conde R., Arevalo C., Becerril B., Martin B.M., Valdivia H.H., et al. The mechanism of inhibition of ryanodine receptor channels by imperatoxin I, a heterodimeric protein from the scorpion Pandinus imperator. J Biol Chem 1997, 272:11886-11894.
    • (1997) J Biol Chem , vol.272 , pp. 11886-11894
    • Zamudio, F.Z.1    Conde, R.2    Arevalo, C.3    Becerril, B.4    Martin, B.M.5    Valdivia, H.H.6
  • 34
    • 0032731227 scopus 로고    scopus 로고
    • Phospholipin, a novel heterodimeric phospholipase A2 from Pandinus imperator scp6pion venom
    • Conde R., Zamudio F.Z., Becerril B., Possani L.D. Phospholipin, a novel heterodimeric phospholipase A2 from Pandinus imperator scp6pion venom. FEBS Lett 1999, 460:447-450.
    • (1999) FEBS Lett , vol.460 , pp. 447-450
    • Conde, R.1    Zamudio, F.Z.2    Becerril, B.3    Possani, L.D.4
  • 35
    • 40249091901 scopus 로고    scopus 로고
    • Heterodimeric neurotoxic phospholipases A2-the first proteins from venom of recently established species Vipera nikolskii: implication of venom composition in viper systematics
    • Ramazanova A.S., Zavada L.L., Starkov V.G., Kovyazina I.V., Subbotina T.F., Kostyukhina E.E., et al. Heterodimeric neurotoxic phospholipases A2-the first proteins from venom of recently established species Vipera nikolskii: implication of venom composition in viper systematics. Toxicon 2008, 51:524-537.
    • (2008) Toxicon , vol.51 , pp. 524-537
    • Ramazanova, A.S.1    Zavada, L.L.2    Starkov, V.G.3    Kovyazina, I.V.4    Subbotina, T.F.5    Kostyukhina, E.E.6
  • 37
    • 0014809596 scopus 로고
    • Intracellular events underlying synthesis and secretion of immunoglobulin
    • Uhr J.W. Intracellular events underlying synthesis and secretion of immunoglobulin. Cell Immunol 1970, 1:228-244.
    • (1970) Cell Immunol , vol.1 , pp. 228-244
    • Uhr, J.W.1
  • 38
    • 0035899984 scopus 로고    scopus 로고
    • Heterodimer formation between the antimicrobial peptides magainin 2 and PGLa in lipid bilayers: a cross-linking study
    • Hara T., Mitani Y., Tanaka K., Uematsu N., Takakura A., Tachi T., et al. Heterodimer formation between the antimicrobial peptides magainin 2 and PGLa in lipid bilayers: a cross-linking study. Biochemistry 2001, 40:12395-12399.
    • (2001) Biochemistry , vol.40 , pp. 12395-12399
    • Hara, T.1    Mitani, Y.2    Tanaka, K.3    Uematsu, N.4    Takakura, A.5    Tachi, T.6
  • 39
    • 77952104633 scopus 로고    scopus 로고
    • Novel conopeptides in a form of disulfide-crosslinked dimer
    • Wu X.C., Zhou M., Peng C., Shao X.X., Guo Z.Y., Chi C.W. Novel conopeptides in a form of disulfide-crosslinked dimer. Peptides 2010, 31:1001-1006.
    • (2010) Peptides , vol.31 , pp. 1001-1006
    • Wu, X.C.1    Zhou, M.2    Peng, C.3    Shao, X.X.4    Guo, Z.Y.5    Chi, C.W.6
  • 40
    • 70349751730 scopus 로고    scopus 로고
    • Membrane structure and conformational changes of the antibiotic heterodimeric peptide distinctin by solid-state NMR spectroscopy
    • Resende J.M., Moraes C.M., Munhoz V.H., Aisenbrey C., Verly R.M., Bertani P., et al. Membrane structure and conformational changes of the antibiotic heterodimeric peptide distinctin by solid-state NMR spectroscopy. Proc Natl Acad Sci U S A 2009, 106:16639-16644.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 16639-16644
    • Resende, J.M.1    Moraes, C.M.2    Munhoz, V.H.3    Aisenbrey, C.4    Verly, R.M.5    Bertani, P.6
  • 41
    • 78649798561 scopus 로고    scopus 로고
    • Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR spectroscopy in zwitterionic and charged lipid bilayers
    • Verardi R., Traaseth N.J., Shi L., Porcelli F., Monfregola L., De Luca S., et al. Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR spectroscopy in zwitterionic and charged lipid bilayers. Biochim Biophys Acta 2011, 1808:34-40.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 34-40
    • Verardi, R.1    Traaseth, N.J.2    Shi, L.3    Porcelli, F.4    Monfregola, L.5    De Luca, S.6
  • 42
    • 46049109376 scopus 로고    scopus 로고
    • Análise Conformacional por Cálculos Teóricos da Distinctina, Peptídeo Antimicrobiano Isolado de Anuros da Espécie Phyllomedusa distincta
    • VHdO Munhoz, AFdC Alcântara, Piló-Veloso D. Análise Conformacional por Cálculos Teóricos da Distinctina, Peptídeo Antimicrobiano Isolado de Anuros da Espécie Phyllomedusa distincta. Quím Nova 2008, 31:822-827.
    • (2008) Quím Nova , vol.31 , pp. 822-827
    • Munhoz, V.H.O.1    Alcântara, A.F.C.2    Piló-Veloso, D.3


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