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Volumn 306, Issue 2, 2003, Pages 496-500

A melittin-related peptide from the skin of the Japanese frog, Rana tagoi, with antimicrobial and cytolytic properties

Author keywords

Antimicrobial; Antiviral; Cytolytic; Frog skin; Hemolytic; Melittin; Temporin

Indexed keywords

ALANYLISOLEUCYLGLYCYLSERYLISOLEUCYLLEUCYLGLYCYLALANYLLEUCYLALANYLLYSYLGLYCY LLEUCYLPROLYLTHREONYLLEUCYLISOLEUCYLSERYLTRYPTOPHYLISOLEUCYLLYSYLASPARAGINYLARGI NINAMIDE; ANTIINFECTIVE AGENT; BEE VENOM; CYTOTOXIC AGENT; MELITTIN; PEPTIDE; PHENYLALANYLLEUCYLPROLYLISOLEUCYLLEUCYLGLYCYLLYSYLLEUCYLLEUCYLSERYLGLYCYLIS OLEUCYLLEUCINAMIDE; UNCLASSIFIED DRUG;

EID: 0038546578     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00999-9     Document Type: Article
Times cited : (63)

References (38)
  • 1
    • 0015527253 scopus 로고
    • Bee and wasp venoms
    • Habermann E. Bee and wasp venoms. Science. 177:1972;314-322.
    • (1972) Science , vol.177 , pp. 314-322
    • Habermann, E.1
  • 2
    • 0015787259 scopus 로고
    • Structure of melittin isolated from two species of honey bees
    • Kreil G. Structure of melittin isolated from two species of honey bees. FEBS Lett. 33:1973;241-244.
    • (1973) FEBS Lett. , vol.33 , pp. 241-244
    • Kreil, G.1
  • 3
    • 0025717603 scopus 로고
    • Probing the relationships between the structure and hemolytic activity of melittin with a complete set of leucine substitution analogs
    • Blondelle S.E., Houghten R.A. Probing the relationships between the structure and hemolytic activity of melittin with a complete set of leucine substitution analogs. Pept. Res. 4:1991;12-18.
    • (1991) Pept. Res. , vol.4 , pp. 12-18
    • Blondelle, S.E.1    Houghten, R.A.2
  • 4
    • 0027324370 scopus 로고
    • The effect of sequence variations and structure on the cytolytic activity of melittin peptides
    • Werkmeister J.A., Kirkpatrick A., McKenzei J.A., Rivett D.E. The effect of sequence variations and structure on the cytolytic activity of melittin peptides. Biochim. Biophys. Acta. 1157:1993;50-54.
    • (1993) Biochim. Biophys. Acta , vol.1157 , pp. 50-54
    • Werkmeister, J.A.1    Kirkpatrick, A.2    McKenzei, J.A.3    Rivett, D.E.4
  • 5
    • 0025833449 scopus 로고
    • Hemolytic and antimicrobial activities of the twenty-four individual omission analogues of melittin
    • Blondelle S.E., Houghten R.A. Hemolytic and antimicrobial activities of the twenty-four individual omission analogues of melittin. Biochemistry. 30:1991;4671-4678.
    • (1991) Biochemistry , vol.30 , pp. 4671-4678
    • Blondelle, S.E.1    Houghten, R.A.2
  • 6
    • 0031401927 scopus 로고    scopus 로고
    • Design of novel analogue peptides with potent fungicidal but low hemolytic activity based on the cecropin A-melittin hybrid structure
    • Lee D.G., Park J.H., Shin S.Y., Lee S.G., Lee M.K., Kim K.L., Hahm K.S. Design of novel analogue peptides with potent fungicidal but low hemolytic activity based on the cecropin A-melittin hybrid structure. Biochem. Mol. Biol. Int. 43:1997;489-498.
    • (1997) Biochem. Mol. Biol. Int. , vol.43 , pp. 489-498
    • Lee, D.G.1    Park, J.H.2    Shin, S.Y.3    Lee, S.G.4    Lee, M.K.5    Kim, K.L.6    Hahm, K.S.7
  • 7
    • 0026082670 scopus 로고
    • In vitro activities of lytic peptides against the sporozoites of Cryptosporidium parvum
    • Arrowood M.J., Jaynes J.M., Healey M.C. In vitro activities of lytic peptides against the sporozoites of Cryptosporidium parvum. Antimicrob. Agents Chemother. 35:1991;224-227.
    • (1991) Antimicrob. Agents Chemother. , vol.35 , pp. 224-227
    • Arrowood, M.J.1    Jaynes, J.M.2    Healey, M.C.3
  • 8
    • 0018693835 scopus 로고
    • Further studies on the structural requirements for polypeptide-mediated histamine release from rat mast cells
    • Jasani B., Kreil G., Mackler B.F., Stanworth D.R. Further studies on the structural requirements for polypeptide-mediated histamine release from rat mast cells. Biochem. J. 181:1979;623-632.
    • (1979) Biochem. J. , vol.181 , pp. 623-632
    • Jasani, B.1    Kreil, G.2    Mackler, B.F.3    Stanworth, D.R.4
  • 9
    • 0024343903 scopus 로고
    • ATP-sensitive binding of melittin to the catalytic domain of protein kinase C
    • O'Brian C.A., Ward N.E. ATP-sensitive binding of melittin to the catalytic domain of protein kinase C. Mol. Pharmacol. 36:1989;355-359.
    • (1989) Mol. Pharmacol. , vol.36 , pp. 355-359
    • O'Brian, C.A.1    Ward, N.E.2
  • 11
    • 0033231591 scopus 로고    scopus 로고
    • Melittin activates endogenous phospholipase D during cytolysis of human monocytic leukemia cells
    • Saini S.S., Chopra A.K., Peterson J.W. Melittin activates endogenous phospholipase D during cytolysis of human monocytic leukemia cells. Toxicon. 37:1999;1605-1619.
    • (1999) Toxicon , vol.37 , pp. 1605-1619
    • Saini, S.S.1    Chopra, A.K.2    Peterson, J.W.3
  • 12
    • 0022102036 scopus 로고
    • Endothelium-dependent vasodilatation by melittin: Are lipoxygenase products involved?
    • Fostermann U., Neufang B. Endothelium-dependent vasodilatation by melittin: are lipoxygenase products involved? Am. J. Physiol. 249:1985;H14-H19.
    • (1985) Am. J. Physiol. , vol.249
    • Fostermann, U.1    Neufang, B.2
  • 14
    • 0027272985 scopus 로고
    • Influence of epithelium on the inhibition of melittin-induced contraction of guinea-pig isolated trachea by the potassium channel opener NIP-121
    • Shikada K., Tanaka S. Influence of epithelium on the inhibition of melittin-induced contraction of guinea-pig isolated trachea by the potassium channel opener NIP-121. Br. J. Pharmacol. 109:1993;1091-1096.
    • (1993) Br. J. Pharmacol. , vol.109 , pp. 1091-1096
    • Shikada, K.1    Tanaka, S.2
  • 16
    • 0028330441 scopus 로고
    • Increase in filtration coefficient from actions of melittin on neutrophils in isolated rabbit lungs
    • Littner M.R., Lott F.D. Increase in filtration coefficient from actions of melittin on neutrophils in isolated rabbit lungs. Am. J. Respir. Crit. Care Med. 149:1994;867-872.
    • (1994) Am. J. Respir. Crit. Care Med. , vol.149 , pp. 867-872
    • Littner, M.R.1    Lott, F.D.2
  • 18
    • 0024473982 scopus 로고
    • 2 activation by melittin causes amylase release from exocrine pancreas
    • 2 activation by melittin causes amylase release from exocrine pancreas. Can. J. Physiol. Pharmacol. 67:1989;411-416.
    • (1989) Can. J. Physiol. Pharmacol. , vol.67 , pp. 411-416
    • Heisler, S.1
  • 19
    • 0032703776 scopus 로고    scopus 로고
    • Melittin enhances amino acid and free fatty acid release from the in vivo cerebral cortex
    • Phillis J.W., Song D., O'Regan M.H. Melittin enhances amino acid and free fatty acid release from the in vivo cerebral cortex. Brain Res. 847:1999;270-275.
    • (1999) Brain Res. , vol.847 , pp. 270-275
    • Phillis, J.W.1    Song, D.2    O'Regan, M.H.3
  • 20
    • 0036229112 scopus 로고    scopus 로고
    • Effects of a lytic peptide conjugated to βHCG on ovarian cancer: Studies in viro and in vivo
    • Gawronska B., Leuschner C., Enright F.M., Hansel W. Effects of a lytic peptide conjugated to βHCG on ovarian cancer: studies in viro and in vivo. Gynecol. Oncol. 85:2002;45-52.
    • (2002) Gynecol. Oncol. , vol.85 , pp. 45-52
    • Gawronska, B.1    Leuschner, C.2    Enright, F.M.3    Hansel, W.4
  • 22
    • 0034736299 scopus 로고    scopus 로고
    • Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from the skin secretions of the North American pickerel frog, Rana palustris
    • Basir Y.J., Knoop F.C., Dulka J., Conlon J.M. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from the skin secretions of the North American pickerel frog, Rana palustris. Biochim. Biophys. Acta. 1543:2000;95-105.
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 95-105
    • Basir, Y.J.1    Knoop, F.C.2    Dulka, J.3    Conlon, J.M.4
  • 23
    • 1242296295 scopus 로고    scopus 로고
    • Antimicrobial peptides and protease inhibitors in the skin secretions of the crawfish frog, Rana areolata
    • Ali M.F., Lips K.R., Knoop F.C., Fritzsch B., Miller C., Conlon J.M. Antimicrobial peptides and protease inhibitors in the skin secretions of the crawfish frog, Rana areolata. Biochim. Biophys. Acta. 1601:2002;55-63.
    • (2002) Biochim. Biophys. Acta , vol.1601 , pp. 55-63
    • Ali, M.F.1    Lips, K.R.2    Knoop, F.C.3    Fritzsch, B.4    Miller, C.5    Conlon, J.M.6
  • 24
    • 0035183366 scopus 로고    scopus 로고
    • Antimicrobial peptides from the skin of the Japanese mountain brown frog, Rana ornativentris
    • Kim J.B., Iwamuro S., Knoop F.C., Conlon J.M. Antimicrobial peptides from the skin of the Japanese mountain brown frog, Rana ornativentris. J. Peptide Res. 58:2001;349-356.
    • (2001) J. Peptide Res. , vol.58 , pp. 349-356
    • Kim, J.B.1    Iwamuro, S.2    Knoop, F.C.3    Conlon, J.M.4
  • 25
    • 0036170116 scopus 로고    scopus 로고
    • Antimicrobial peptides with atypical structural features from the skin of the Japanese brown frog Rana japonica
    • Isaacson T., Soto A., Iwamuro S., Knoop F.C., Conlon J.M. Antimicrobial peptides with atypical structural features from the skin of the Japanese brown frog Rana japonica. Peptides. 23:2002;419-425.
    • (2002) Peptides , vol.23 , pp. 419-425
    • Isaacson, T.1    Soto, A.2    Iwamuro, S.3    Knoop, F.C.4    Conlon, J.M.5
  • 27
    • 0037436393 scopus 로고    scopus 로고
    • Effect of malathion on apoptosis of murine L929 fibroblasts: A possible mechanism for toxicity in low dose exposure
    • Masoud L., Vijayasarathy C., Fernandez-Cabezudo M., Petroianu G., Saleh A.M. Effect of malathion on apoptosis of murine L929 fibroblasts: a possible mechanism for toxicity in low dose exposure. Toxicology. 185:2003;89-102.
    • (2003) Toxicology , vol.185 , pp. 89-102
    • Masoud, L.1    Vijayasarathy, C.2    Fernandez-Cabezudo, M.3    Petroianu, G.4    Saleh, A.M.5
  • 28
    • 0037255488 scopus 로고    scopus 로고
    • Influence of paraoxon (POX) and parathion (PAT) on apoptosis: A possible mechanism for toxicity in low-dose exposure
    • Saleh A.M., Vijayasarathy C., Fernandez-Cabezudo M., Taleb M., Petroianu G. Influence of paraoxon (POX) and parathion (PAT) on apoptosis: a possible mechanism for toxicity in low-dose exposure. J. Appl. Toxicol. 23:2003;23-29.
    • (2003) J. Appl. Toxicol. , vol.23 , pp. 23-29
    • Saleh, A.M.1    Vijayasarathy, C.2    Fernandez-Cabezudo, M.3    Taleb, M.4    Petroianu, G.5
  • 30
    • 0033973411 scopus 로고    scopus 로고
    • Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs, Rana luteiventris, Rana berlandieri, and Rana pipiens
    • Goraya J., Wang Y., Li Z., O'Flaherty M., Knoop F.C., Platz J.E., Conlon J.M. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs, Rana luteiventris, Rana berlandieri, and Rana pipiens. Eur. J. Biochem. 267:2000;894-900.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 894-900
    • Goraya, J.1    Wang, Y.2    Li, Z.3    O'Flaherty, M.4    Knoop, F.C.5    Platz, J.E.6    Conlon, J.M.7
  • 33
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-stave or toroidal model? A case study on melittin pores
    • Yang L., Harroun T.A., Weiss T.M., Ding L., Huang H.W. Barrel-stave or toroidal model? A case study on melittin pores. Biophys. J. 81:2001;1475-1485.
    • (2001) Biophys. J. , vol.81 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 36
    • 0035975639 scopus 로고    scopus 로고
    • Inactivation of frog virus 3 and channel catfish virus by esculentin-2P and ranatuerin-2P, two antimicrobial peptides isolated from frog skin
    • Chinchar V.G., Wang J., Murti G., Carey C., Rollins-Smith L. Inactivation of frog virus 3 and channel catfish virus by esculentin-2P and ranatuerin-2P, two antimicrobial peptides isolated from frog skin. Virology. 288:2001;351-357.
    • (2001) Virology , vol.288 , pp. 351-357
    • Chinchar, V.G.1    Wang, J.2    Murti, G.3    Carey, C.4    Rollins-Smith, L.5
  • 38
    • 0020826315 scopus 로고
    • Nucleotide sequence of cloned cDNA coding for honeybee prepromelittin
    • Vlasak R., Unger-Ullmann C., Kreil G., Frischauf A.-M. Nucleotide sequence of cloned cDNA coding for honeybee prepromelittin. Eur. J. Biochem. 135:1983;123-126.
    • (1983) Eur. J. Biochem. , vol.135 , pp. 123-126
    • Vlasak, R.1    Unger-Ullmann, C.2    Kreil, G.3    Frischauf, A.-M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.