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Volumn 30, Issue 2, 2000, Pages 145-152

Low molecular weight serine protease inhibitors from insects are proteins with highly conserved sequences

Author keywords

Insects; Protease inhibitors; Reactive site; Schistocerca gregaria; Spodoptera littoralis

Indexed keywords

CHYMOTRYPSIN; INSECT PROTEIN; LEUKOCYTE ELASTASE; SERINE PROTEINASE INHIBITOR;

EID: 0342905403     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0965-1748(99)00109-5     Document Type: Article
Times cited : (19)

References (36)
  • 1
    • 0024853901 scopus 로고
    • Isolation and characterization of a 60-residue intestinal peptide structurally related to the pancreatic secretory type of trypsin inhibitor: Influence of insulin secretion
    • Agerberth B., Soderling-Barros J., Jornvall H., Chen Z.W., Ostenson C.G., Efendic S., Mutt V. Isolation and characterization of a 60-residue intestinal peptide structurally related to the pancreatic secretory type of trypsin inhibitor: influence of insulin secretion. Proc. Natl. Acad. Sci. USA. 86:1989;8590-8594.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8590-8594
    • Agerberth, B.1    Soderling-Barros, J.2    Jornvall, H.3    Chen, Z.W.4    Ostenson, C.G.5    Efendic, S.6    Mutt, V.7
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 4
    • 0018349277 scopus 로고
    • Role of hemocytes in hemolymph coagulation in Locusta migratoria
    • Brehélin M. Role of hemocytes in hemolymph coagulation in Locusta migratoria. Experientia. 35:1979;270.
    • (1979) Experientia , vol.35 , pp. 270
    • Brehélin, M.1
  • 5
    • 0026053073 scopus 로고
    • Purification of a protease inhibitor which controls prophenoloxidase activation on hemolymph of Locusta migratoria (Insecta)
    • Brehélin M., Boigegrain R.A., Drif L., Coletti-Previero M.A. Purification of a protease inhibitor which controls prophenoloxidase activation on hemolymph of Locusta migratoria (Insecta). Biochem. Biophys. Res. Commun. 179:1991;841-846.
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 841-846
    • Brehélin, M.1    Boigegrain, R.A.2    Drif, L.3    Coletti-Previero, M.A.4
  • 6
    • 0024289854 scopus 로고
    • A peptide from the eel pancreas with structural similarity to human pancreatic secretory trypsin inhibitor
    • Colon J.M., Thim L. A peptide from the eel pancreas with structural similarity to human pancreatic secretory trypsin inhibitor. Eur. J. Biochem. 174:1988;149-153.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 149-153
    • Colon, J.M.1    Thim, L.2
  • 7
    • 0024382970 scopus 로고
    • Functional evolutionary divergence of proteolytic enzymes and their inhibitors
    • Creighton T.E., Darby N.J. Functional evolutionary divergence of proteolytic enzymes and their inhibitors. Trends Biochem. Sci. 14:1989;319-324.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 319-324
    • Creighton, T.E.1    Darby, N.J.2
  • 8
    • 0028239695 scopus 로고
    • Amino acid sequence of an inhibitor from the silkworm (Bombyx mori) hemolymph against fungal protease
    • Eguchi M., Itoh M., Nishino K., Shibata H., Tanaka T., Kamei-Hayashi K., Hara S. Amino acid sequence of an inhibitor from the silkworm (Bombyx mori) hemolymph against fungal protease. J. Biochem. 115:1994;881-884.
    • (1994) J. Biochem. , vol.115 , pp. 881-884
    • Eguchi, M.1    Itoh, M.2    Nishino, K.3    Shibata, H.4    Tanaka, T.5    Kamei-Hayashi, K.6    Hara, S.7
  • 9
    • 0024474543 scopus 로고
    • Active site chemical mutagenesis of Ecballium elaterium Trypsin Inhibitor II: New microproteins inhibiting elastase and chymotrypsin
    • Favel A., Le Nguyen D., Coletti-Previero M.A., Castro B. Active site chemical mutagenesis of Ecballium elaterium Trypsin Inhibitor II: new microproteins inhibiting elastase and chymotrypsin. Biochem. Biophys. Res. Commun. 162:1989;79-82.
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 79-82
    • Favel, A.1    Le Nguyen, D.2    Coletti-Previero, M.A.3    Castro, B.4
  • 11
    • 0032559421 scopus 로고    scopus 로고
    • Purification and characterization of a group of five novel peptide serine protease inhibitors from ovaries of the desert locust, Schistocerca gregaria
    • Hamdaoui A., Wataleb S., Devreese B., Chiou S.J., Vanden Broeck J., Van Beeumen J., De Loof A., Schoofs L. Purification and characterization of a group of five novel peptide serine protease inhibitors from ovaries of the desert locust, Schistocerca gregaria. FEBS Lett. 422:1998;74-78.
    • (1998) FEBS Lett. , vol.422 , pp. 74-78
    • Hamdaoui, A.1    Wataleb, S.2    Devreese, B.3    Chiou, S.J.4    Vanden Broeck, J.5    Van Beeumen, J.6    De Loof, A.7    Schoofs, L.8
  • 12
    • 0024979264 scopus 로고
    • Isocratic separation of phenylthiohydantoin-amino acids by reverse phase high performance liquid chromatography
    • Hayakawa K., Oizumi J. Isocratic separation of phenylthiohydantoin-amino acids by reverse phase high performance liquid chromatography. J. Chromatogr. 487:1989;161-166.
    • (1989) J. Chromatogr. , vol.487 , pp. 161-166
    • Hayakawa, K.1    Oizumi, J.2
  • 13
    • 0023188637 scopus 로고
    • Accelerated evolution in the reactive centre regions of serine protease inhibitors
    • Hill R.E., Hastie N.D. Accelerated evolution in the reactive centre regions of serine protease inhibitors. Nature. 326:1987;96-99.
    • (1987) Nature , vol.326 , pp. 96-99
    • Hill, R.E.1    Hastie, N.D.2
  • 14
    • 84951413544 scopus 로고
    • The oxidation of ribonuclease with performic acid
    • Hirs C.H.W. The oxidation of ribonuclease with performic acid. J. Biol. Chem. 219:1956;611-621.
    • (1956) J. Biol. Chem. , vol.219 , pp. 611-621
    • Hirs, C.H.W.1
  • 15
    • 0026067029 scopus 로고
    • Amino-acid derivatization and analysis in five minutes
    • Husek P. Amino-acid derivatization and analysis in five minutes. FEBS Lett. 280:1991;354-356.
    • (1991) FEBS Lett. , vol.280 , pp. 354-356
    • Husek, P.1
  • 16
    • 0031012783 scopus 로고    scopus 로고
    • Characterization and functional analysis of 12 naturally occuring reactive site variants of serpin 1 from Manduca sexta
    • Jiang H., Kanost M.R. Characterization and functional analysis of 12 naturally occuring reactive site variants of serpin 1 from Manduca sexta. J. Biol. Chem. 272:1997;1082-1087.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1082-1087
    • Jiang, H.1    Kanost, M.R.2
  • 17
    • 0027980413 scopus 로고
    • Purification and cDNA cloning of a four domain Kazal proteinase inhibitor from crayfish blood cells
    • Johansson M.W., Keyser P., Söderhäll K. Purification and cDNA cloning of a four domain Kazal proteinase inhibitor from crayfish blood cells. Eur. J. Biochem. 223:1994;389-394.
    • (1994) Eur. J. Biochem. , vol.223 , pp. 389-394
    • Johansson, M.W.1    Keyser, P.2    Söderhäll, K.3
  • 18
    • 0032992544 scopus 로고    scopus 로고
    • Serine protease inhibitors in arthropod immunity
    • Kanost M.R. Serine protease inhibitors in arthropod immunity. Dev. Comp. Immunol. 23:1999;291-301.
    • (1999) Dev. Comp. Immunol. , vol.23 , pp. 291-301
    • Kanost, M.R.1
  • 19
    • 0028826920 scopus 로고
    • Serine protease inhibition by insect peptides containing a cystine-knot and a triple-stranded b-sheet
    • Kellenberger C., Boudier C., Bermudez I., Bieth J.G., Luu B., Hietter H. Serine protease inhibition by insect peptides containing a cystine-knot and a triple-stranded b-sheet. J. Biol. Chem. 270:1995;25514-25519.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25514-25519
    • Kellenberger, C.1    Boudier, C.2    Bermudez, I.3    Bieth, J.G.4    Luu, B.5    Hietter, H.6
  • 21
    • 37049073307 scopus 로고
    • Renin Substrate. Part II. Rapid solid phase synthesisof ratine sequence tetradecapeptide using Bop reagent
    • Le Nguyen D., Heitz A., Castro B. Renin Substrate. Part II. Rapid solid phase synthesisof ratine sequence tetradecapeptide using Bop reagent. J. Chem. Soc. Perkin Trans. 1:1987;1915-1919.
    • (1987) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 1915-1919
    • Le Nguyen, D.1    Heitz, A.2    Castro, B.3
  • 22
    • 0030917010 scopus 로고    scopus 로고
    • Pacifastin, a novel 155-kDa heterodimeric proteinase inhibitor containing a unique transferrin chain
    • Liang Z., Sottrup-Jensen L., Aspàn A., Hall M., Söderhäll K. Pacifastin, a novel 155-kDa heterodimeric proteinase inhibitor containing a unique transferrin chain. Proc. Natl. Acad. Sci. USA. 94:1997;6682-6687.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6682-6687
    • Liang, Z.1    Sottrup-Jensen, L.2    Aspàn, A.3    Hall, M.4    Söderhäll, K.5
  • 23
    • 0030065240 scopus 로고    scopus 로고
    • Stabilization of proteins by glycosylation examined by NMR analysis of a fucosylated proteinase inhibitor
    • Mer G., Hietter H., Lefevre J.F. Stabilization of proteins by glycosylation examined by NMR analysis of a fucosylated proteinase inhibitor. Nature Struct. Biol. 3:1996;45-53.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 45-53
    • Mer, G.1    Hietter, H.2    Lefevre, J.F.3
  • 24
    • 0030004582 scopus 로고    scopus 로고
    • Solution structure of PMP-C: A new fold in the group of small serine proteinase inhibitors
    • Mer G., Hietter H., Kellenberger C., Renatus M., Luu B., Lefevre J.F. Solution structure of PMP-C: a new fold in the group of small serine proteinase inhibitors. J. Mol. Biol. 258:1996;158-171.
    • (1996) J. Mol. Biol. , vol.258 , pp. 158-171
    • Mer, G.1    Hietter, H.2    Kellenberger, C.3    Renatus, M.4    Luu, B.5    Lefevre, J.F.6
  • 26
    • 0026567538 scopus 로고
    • Isolation and structural determination of three peptides from the insect Locusta migratoria
    • Nakakura N., Hietter H., Van Dorsselaer A., Luu B. Isolation and structural determination of three peptides from the insect Locusta migratoria. Eur. J. Biochem. 204:1992;147-153.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 147-153
    • Nakakura, N.1    Hietter, H.2    Van Dorsselaer, A.3    Luu, B.4
  • 27
    • 0027195507 scopus 로고
    • Molecular cloning of silkworm (Bombyx mori) antichymotrypsin. A new member of the serpin superfamily of proteins from insect
    • Narumi H., Hishida T., Sasaki T., Feng D.H., Doolittle R.F. Molecular cloning of silkworm (Bombyx mori) antichymotrypsin. A new member of the serpin superfamily of proteins from insect. Eur. J. Biochem. 214:1993;181-187.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 181-187
    • Narumi, H.1    Hishida, T.2    Sasaki, T.3    Feng, D.H.4    Doolittle, R.F.5
  • 28
    • 0014011074 scopus 로고
    • The reactive site of trypsin inhibitors
    • Ozawa K., Laskowski M. The reactive site of trypsin inhibitors. J. Biol. Chem. 241:1966;3955-3961.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3955-3961
    • Ozawa, K.1    Laskowski, M.2
  • 29
    • 0029940506 scopus 로고    scopus 로고
    • Expression of Bombyx family fungal protease inhibitor F from Bombyx mori by baculovirus vector
    • Pham T.N., Hayashi K., Takano R., Itoh M., Eguchi M., Shibata H., Tanaka T., Hara S. Expression of Bombyx family fungal protease inhibitor F from Bombyx mori by baculovirus vector. J. Biochem. 119:1996;428-434.
    • (1996) J. Biochem. , vol.119 , pp. 428-434
    • Pham, T.N.1    Hayashi, K.2    Takano, R.3    Itoh, M.4    Eguchi, M.5    Shibata, H.6    Tanaka, T.7    Hara, S.8
  • 30
    • 0030345078 scopus 로고    scopus 로고
    • Serine proteinase inhibitors from insect hemolymph.
    • Polanowski A., Wilusz T. Serine proteinase inhibitors from insect hemolymph. Acta Biochim. Polon. 43:1996;445-454.
    • (1996) Acta Biochim. Polon. , vol.43 , pp. 445-454
    • Polanowski, A.1    Wilusz, T.2
  • 31
    • 0028317559 scopus 로고
    • Two serine proteinase inhibitors from the larval hemolymph of Heliothis zea
    • Polanowski A., Wilusz T., Blum M.S., Travis J. Two serine proteinase inhibitors from the larval hemolymph of Heliothis zea. Acta Biochim. Polon. 41:1994;178-180.
    • (1994) Acta Biochim. Polon. , vol.41 , pp. 178-180
    • Polanowski, A.1    Wilusz, T.2    Blum, M.S.3    Travis, J.4
  • 32
    • 0026046935 scopus 로고
    • Patchwork-structure serpins from silkworm (Bombyx mori) larval hemolymph
    • Sasaki T. Patchwork-structure serpins from silkworm (Bombyx mori) larval hemolymph. Eur. J. Biochem. 202:1991;255-261.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 255-261
    • Sasaki, T.1
  • 33
    • 0011806217 scopus 로고
    • Determination of amino acids as phenylthiohydantoins derivatives. III Quantitative determination of 3-phenyl-2-thiohydantoins from paper chromatograms
    • Sjöquist J. Determination of amino acids as phenylthiohydantoins derivatives. III Quantitative determination of 3-phenyl-2-thiohydantoins from paper chromatograms. Biochem. Biophys. Acta. 41:1960;20-30.
    • (1960) Biochem. Biophys. Acta , vol.41 , pp. 20-30
    • Sjöquist, J.1
  • 34
    • 0025182927 scopus 로고
    • Amino-acid sequence of silkworm (Bombyx mori) hemolymph antitrypsin deduced from its homology with serpins
    • Tagaki H., Narumi H., Nakamura K., Sasaki T. Amino-acid sequence of silkworm (Bombyx mori) hemolymph antitrypsin deduced from its homology with serpins. J. Biochem. 108:1990;372-378.
    • (1990) J. Biochem. , vol.108 , pp. 372-378
    • Tagaki, H.1    Narumi, H.2    Nakamura, K.3    Sasaki, T.4
  • 35
    • 0023433076 scopus 로고
    • The covalent structure of the elastase inhibitor from Anemonia sulcata, a "non classical" Kazal-type protein
    • Tschesche H., Kolkenbrock H., Bode W. The covalent structure of the elastase inhibitor from Anemonia sulcata, a "non classical" Kazal-type protein. Biol. Chem. Hoppe-Seyler. 368:1987;1297-1304.
    • (1987) Biol. Chem. Hoppe-Seyler , vol.368 , pp. 1297-1304
    • Tschesche, H.1    Kolkenbrock, H.2    Bode, W.3
  • 36
    • 0022435216 scopus 로고
    • The squash family of serine proteinase inhibitors. Amino acid squences and association equilibrium constants of inhibitors from squash, summer squash, zucchini and cucumber seeds
    • Wieczorek M., Otlewski J., Parks K., Leluk J., Wilimowska-Pelc A., Polanowski A., Wilusz T., Lakowski M. The squash family of serine proteinase inhibitors. Amino acid squences and association equilibrium constants of inhibitors from squash, summer squash, zucchini and cucumber seeds. Biochem. Biophys. Res. Commun. 126:1985;646-652.
    • (1985) Biochem. Biophys. Res. Commun. , vol.126 , pp. 646-652
    • Wieczorek, M.1    Otlewski, J.2    Parks, K.3    Leluk, J.4    Wilimowska-Pelc, A.5    Polanowski, A.6    Wilusz, T.7    Lakowski, M.8


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