메뉴 건너뛰기




Volumn 88, Issue 6, 2006, Pages 673-681

The full-length cDNA of anticoagulant protein infestin revealed a novel releasable Kazal domain, a neutrophil elastase inhibitor lacking anticoagulant activity

Author keywords

Blood sucking; Elastase inhibitor; Multidomain; Serine proteinase inhibitor; Subtilisin inhibitor; Triatoma infestans

Indexed keywords

ANTICOAGULANT PROTEIN; CHYMOTRYPSIN; COMPLEMENTARY DNA; INFESTIN; PROTEIN; PROTEINASE K; SUBTILISIN; UNCLASSIFIED DRUG;

EID: 33745949100     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2005.11.011     Document Type: Article
Times cited : (43)

References (32)
  • 2
    • 0038474360 scopus 로고    scopus 로고
    • Dipetalogastin, a potent thrombin inhibitor from the blood-sucking insect. Dipetalogaster maximus cDNA cloning, expression and characterization
    • Mende K., Petoukhova O., Koulitchkova V., Schaub G.A., Lange U., Kaufmann R., and Nowak G. Dipetalogastin, a potent thrombin inhibitor from the blood-sucking insect. Dipetalogaster maximus cDNA cloning, expression and characterization. Eur. J. Biochem. 266 (1999) 583-590
    • (1999) Eur. J. Biochem. , vol.266 , pp. 583-590
    • Mende, K.1    Petoukhova, O.2    Koulitchkova, V.3    Schaub, G.A.4    Lange, U.5    Kaufmann, R.6    Nowak, G.7
  • 3
    • 0036712320 scopus 로고    scopus 로고
    • Infestin, a thrombin inhibitor presents in Triatoma infestans midgut, a Chagas' disease vector: gene cloning, expression and characterization of the inhibitor
    • Campos I.T., Amino R., Sampaio C.A., Auerswald E.A., Friedrich T., Lemaire H.G., Schenkman S., and Tanaka A.S. Infestin, a thrombin inhibitor presents in Triatoma infestans midgut, a Chagas' disease vector: gene cloning, expression and characterization of the inhibitor. Insect Biochem. Mol. Biol. 32 (2002) 991-997
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 991-997
    • Campos, I.T.1    Amino, R.2    Sampaio, C.A.3    Auerswald, E.A.4    Friedrich, T.5    Lemaire, H.G.6    Schenkman, S.7    Tanaka, A.S.8
  • 4
    • 8844236924 scopus 로고    scopus 로고
    • Identification and characterization of a novel factor XIIa inhibitor in the hematophagous insect, Triatoma infestans (Hemiptera: Reduviidae)
    • Campos I.T., Tanaka-Azevedo A.M., and Tanaka A.S. Identification and characterization of a novel factor XIIa inhibitor in the hematophagous insect, Triatoma infestans (Hemiptera: Reduviidae). FEBS Lett. 577 (2004) 512-516
    • (2004) FEBS Lett. , vol.577 , pp. 512-516
    • Campos, I.T.1    Tanaka-Azevedo, A.M.2    Tanaka, A.S.3
  • 5
    • 0022824004 scopus 로고
    • The primary structure of bdellin B-3 from the leech Hirudo medicinalis. Bdellin B-3 is a compact proteinase inhibitor of a "non-classical" Kazal type. It is present in the leech in a high molecular mass form
    • Fink E., Rehm H., Gippner C., Bode W., Eulitz M., Machleidt W., and Fritz H. The primary structure of bdellin B-3 from the leech Hirudo medicinalis. Bdellin B-3 is a compact proteinase inhibitor of a "non-classical" Kazal type. It is present in the leech in a high molecular mass form. Biol. Chem. Hoppe Seyler 367 (1986) 1235-1242
    • (1986) Biol. Chem. Hoppe Seyler , vol.367 , pp. 1235-1242
    • Fink, E.1    Rehm, H.2    Gippner, C.3    Bode, W.4    Eulitz, M.5    Machleidt, W.6    Fritz, H.7
  • 7
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode W., and Huber R. Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 204 (1992) 433-451
    • (1992) Eur. J. Biochem. , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 9
    • 0028520933 scopus 로고
    • A Kazal-type inhibitor of human mast cell tryptase: isolation from the medical leech Hirudo medicinalis, characterization, and sequence analysis
    • Sommerhoff C.P., Sollner C., Mentele R., Piechottka G.P., Auerswald E.A., and Fritz H. A Kazal-type inhibitor of human mast cell tryptase: isolation from the medical leech Hirudo medicinalis, characterization, and sequence analysis. Biol. Chem. Hoppe Seyler 375 (1994) 685-694
    • (1994) Biol. Chem. Hoppe Seyler , vol.375 , pp. 685-694
    • Sommerhoff, C.P.1    Sollner, C.2    Mentele, R.3    Piechottka, G.P.4    Auerswald, E.A.5    Fritz, H.6
  • 10
    • 0027980413 scopus 로고
    • Purification and cDNA cloning of a four-domain Kazal proteinase inhibitor from crayfish blood cells
    • Johansson M.W., Keyser P., and Soderhall 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    Soderhall, K.3
  • 13
    • 0022371307 scopus 로고
    • Turkey ovomucoid third domain inhibits eight different serine proteinases of varied specificity on the same⋯Leu18-Glu19⋯ reactive site
    • Ardelt W., and Laskowski Jr. M. Turkey ovomucoid third domain inhibits eight different serine proteinases of varied specificity on the same⋯Leu18-Glu19⋯ reactive site. Biochemistry 24 (1985) 5313-5320
    • (1985) Biochemistry , vol.24 , pp. 5313-5320
    • Ardelt, W.1    Laskowski Jr., M.2
  • 17
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., and von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10 (1997) 1-6
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 19
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0019282838 scopus 로고
    • Pathophysiological interpretation of kinetic constants of protease inhibitors
    • Bieth J.G. Pathophysiological interpretation of kinetic constants of protease inhibitors. Bull. Eur. Physiopathol. Respir. 16 Suppl (1980) 183-197
    • (1980) Bull. Eur. Physiopathol. Respir. , vol.16 , Issue.SUPPL , pp. 183-197
    • Bieth, J.G.1
  • 22
    • 0014454095 scopus 로고
    • Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors
    • Morrison J.F. Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors. Biochim. Biophys. Acta 185 (1969) 269-286
    • (1969) Biochim. Biophys. Acta , vol.185 , pp. 269-286
    • Morrison, J.F.1
  • 23
    • 0027399530 scopus 로고
    • Identification of protein coding regions by database similarity search
    • Gish W., and States D.J. Identification of protein coding regions by database similarity search. Nat. Genet. 3 (1993) 266-272
    • (1993) Nat. Genet. , vol.3 , pp. 266-272
    • Gish, W.1    States, D.J.2
  • 25
    • 1842635744 scopus 로고    scopus 로고
    • Evaluation of phage display system and leech-derived tryptase inhibitor as a tool for understanding the serine proteinase specificities
    • Campos I.T., Silva M.M., Azzolini S.S., Souza A.F., Sampaio C.A., Fritz H., and Tanaka A.S. Evaluation of phage display system and leech-derived tryptase inhibitor as a tool for understanding the serine proteinase specificities. Arch. Biochem. Biophys. 425 (2004) 87-94
    • (2004) Arch. Biochem. Biophys. , vol.425 , pp. 87-94
    • Campos, I.T.1    Silva, M.M.2    Azzolini, S.S.3    Souza, A.F.4    Sampaio, C.A.5    Fritz, H.6    Tanaka, A.S.7
  • 26
    • 0032858094 scopus 로고    scopus 로고
    • Functional phage display of leech-derived tryptase inhibitor (LDTI): construction of a library and selection of thrombin inhibitors
    • Tanaka A.S., Silva M.M., Torquato R.J., Noguti M.A., Sampaio C.A., Fritz H., and Auerswald E.A. Functional phage display of leech-derived tryptase inhibitor (LDTI): construction of a library and selection of thrombin inhibitors. FEBS Lett. 458 (1999) 11-16
    • (1999) FEBS Lett. , vol.458 , pp. 11-16
    • Tanaka, A.S.1    Silva, M.M.2    Torquato, R.J.3    Noguti, M.A.4    Sampaio, C.A.5    Fritz, H.6    Auerswald, E.A.7
  • 27
    • 0037384450 scopus 로고    scopus 로고
    • Purification, properties and substrate specificity of a digestive trypsin from Periplaneta americana (Dictyoptera) adults
    • Lopes A.R., and Terra W.R. Purification, properties and substrate specificity of a digestive trypsin from Periplaneta americana (Dictyoptera) adults. Insect Biochem. Mol. Biol. 33 (2003) 407-415
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 407-415
    • Lopes, A.R.1    Terra, W.R.2
  • 28
    • 0041347814 scopus 로고    scopus 로고
    • Structure and energetics of protein-protein interactions: the role of conformational heterogeneity in OMTKY3 binding to serine proteases
    • Horn J.R., Ramaswamy S., and Murphy K.P. Structure and energetics of protein-protein interactions: the role of conformational heterogeneity in OMTKY3 binding to serine proteases. J. Mol. Biol. 331 (2003) 497-508
    • (2003) J. Mol. Biol. , vol.331 , pp. 497-508
    • Horn, J.R.1    Ramaswamy, S.2    Murphy, K.P.3
  • 30
    • 0024464147 scopus 로고
    • Protease-modulation of neutrophil superoxide response
    • Kusner D.J., and King C.H. Protease-modulation of neutrophil superoxide response. J. Immunol. 143 (1989) 1696-1702
    • (1989) J. Immunol. , vol.143 , pp. 1696-1702
    • Kusner, D.J.1    King, C.H.2
  • 32
    • 13544276564 scopus 로고    scopus 로고
    • Sivelestat, a neutrophil elastase inhibitor, attenuates neutrophil priming after hepatoenteric ischemia in rabbits
    • Kotake Y., Yamamoto M., Matsumoto M., Morisaki H., and Takeda J. Sivelestat, a neutrophil elastase inhibitor, attenuates neutrophil priming after hepatoenteric ischemia in rabbits. Shock 23 (2005) 156-160
    • (2005) Shock , vol.23 , pp. 156-160
    • Kotake, Y.1    Yamamoto, M.2    Matsumoto, M.3    Morisaki, H.4    Takeda, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.