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Volumn 30, Issue 11, 2006, Pages 998-1008

A five-domain Kazal-type serine proteinase inhibitor from black tiger shrimp Penaeus monodon and its inhibitory activities

Author keywords

Black tiger shrimp; Hemocyte; Kazal domain; Penaeus monodon; Serine proteinase inhibitor

Indexed keywords

APROTININ; CHYMOTRYPSIN; COMPLEMENTARY DNA; ELASTASE; SUBTILISIN;

EID: 33746321298     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2006.01.004     Document Type: Article
Times cited : (47)

References (31)
  • 1
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski Jr. M., and Kato I. Protein inhibitors of proteinases. Ann Rev Biochem 49 (1980) 593-626
    • (1980) Ann Rev Biochem , vol.49 , pp. 593-626
    • Laskowski Jr., M.1    Kato, I.2
  • 2
    • 0027241401 scopus 로고
    • Protein protease inhibitors in insects and comparison with mammalian inhibitors
    • Eguchi M. Protein protease inhibitors in insects and comparison with mammalian inhibitors. Comp Biochem Physiol B 105 3-4 (1993) 449-456
    • (1993) Comp Biochem Physiol B , vol.105 , Issue.3-4 , pp. 449-456
    • Eguchi, M.1
  • 3
    • 3242714188 scopus 로고    scopus 로고
    • A Kunitz type protease inhibitor related protein is synthesized in Drosophila prepupal salivary glands and released into the moulting fluid during pupation
    • Kress H., Jarrin A., Thüroff E., Saunders R., Weise C., Schmidt am Busch M., Knapp E.-W., Wedde M., and Vilcinskas A. A Kunitz type protease inhibitor related protein is synthesized in Drosophila prepupal salivary glands and released into the moulting fluid during pupation. Insect Biochem Mol Biol 34 8 (2004) 855-869
    • (2004) Insect Biochem Mol Biol , vol.34 , Issue.8 , pp. 855-869
    • Kress, H.1    Jarrin, A.2    Thüroff, E.3    Saunders, R.4    Weise, C.5    Schmidt am Busch, M.6    Knapp, E.-W.7    Wedde, M.8    Vilcinskas, A.9
  • 4
    • 0032992544 scopus 로고    scopus 로고
    • Serine proteinase inhibitors in arthropod immunity
    • Kanost M.R. Serine proteinase inhibitors in arthropod immunity. Devel Comp Immunol 23 4-5 (1999) 291-301
    • (1999) Devel Comp Immunol , vol.23 , Issue.4-5 , pp. 291-301
    • Kanost, M.R.1
  • 5
    • 0002779670 scopus 로고    scopus 로고
    • Proteinase inhibitors in invertebrate immunity
    • Söderhäll K., Iwanaga S., and Vanta G. (Eds), SOS Publications, Fair Haven, NJ
    • Kanost M.R., and Jiang H. Proteinase inhibitors in invertebrate immunity. In: Söderhäll K., Iwanaga S., and Vanta G. (Eds). New directions in invertebrate immunology (1996), SOS Publications, Fair Haven, NJ 155-174
    • (1996) New directions in invertebrate immunology , pp. 155-174
    • Kanost, M.R.1    Jiang, H.2
  • 6
    • 0030345078 scopus 로고    scopus 로고
    • Serine proteinase inhibitors from insect hemolymph
    • Polanowski A., and Wilusz T. Serine proteinase inhibitors from insect hemolymph. Acta Biochim Pol 43 3 (1996) 445-453
    • (1996) Acta Biochim Pol , vol.43 , Issue.3 , pp. 445-453
    • Polanowski, A.1    Wilusz, T.2
  • 7
    • 0028784163 scopus 로고
    • Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin
    • van de Locht A., Lamba D., Bauer M., Huber R., Friedrich T., Kroger B., Hoffken W., and Bode W. Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin. EMBO J 14 21 (1995) 5149-5157
    • (1995) EMBO J , vol.14 , Issue.21 , pp. 5149-5157
    • van de Locht, A.1    Lamba, D.2    Bauer, M.3    Huber, R.4    Friedrich, T.5    Kroger, B.6    Hoffken, W.7    Bode, W.8
  • 8
    • 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 2 (1999) 583-590
    • (1999) Eur J Biochem , vol.266 , Issue.2 , 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
  • 9
    • 0023129864 scopus 로고
    • Chicken ovomucoid: determination of its amino acid sequence, determination of the trypsin reactive site, and preparation of all three of its domains
    • Kato I., Schrode J., Kohr W.J., and Laskowski Jr. M. Chicken ovomucoid: determination of its amino acid sequence, determination of the trypsin reactive site, and preparation of all three of its domains. Biochemistry 26 1 (1987) 193-201
    • (1987) Biochemistry , vol.26 , Issue.1 , pp. 193-201
    • Kato, I.1    Schrode, J.2    Kohr, W.J.3    Laskowski Jr., M.4
  • 10
  • 11
    • 0027980413 scopus 로고
    • Purification and cDNA cloning of a four-domain Kazal proteinase inhibitor from crayfish blood cells
    • Johansson M.W., Keyser P., and Söderhäll K. Purification and cDNA cloning of a four-domain Kazal proteinase inhibitor from crayfish blood cells. Eur J Biochem 223 2 (1994) 389-394
    • (1994) Eur J Biochem , vol.223 , Issue.2 , pp. 389-394
    • Johansson, M.W.1    Keyser, P.2    Söderhäll, K.3
  • 12
    • 13544251554 scopus 로고    scopus 로고
    • A four-Kazal domain protein in Litopenaeus vannamei hemocytes
    • Jimenez-Vega F., and Vargas-Albores F. A four-Kazal domain protein in Litopenaeus vannamei hemocytes. Dev Comp Immunol 29 5 (2005) 385-391
    • (2005) Dev Comp Immunol , vol.29 , Issue.5 , pp. 385-391
    • Jimenez-Vega, F.1    Vargas-Albores, F.2
  • 13
    • 0033571065 scopus 로고    scopus 로고
    • A Drosophila gene encoding multiple splice variants of Kazal-type serine protease inhibitor-like proteins with potential destinations of mitochondria, cytosol and the secretory pathway
    • Niimi T., Yokoyama H., Goto A., Beck K., and Kitagawa Y. A Drosophila gene encoding multiple splice variants of Kazal-type serine protease inhibitor-like proteins with potential destinations of mitochondria, cytosol and the secretory pathway. Eur J Biochem 266 1 (1999) 282-292
    • (1999) Eur J Biochem , vol.266 , Issue.1 , pp. 282-292
    • Niimi, T.1    Yokoyama, H.2    Goto, A.3    Beck, K.4    Kitagawa, Y.5
  • 15
    • 21644484884 scopus 로고    scopus 로고
    • Recombinant expression and characterization of five-domain Kazal-type serine proteinase inhibitor of black tiger shrimp (Penaeus monodon)
    • Jarasrassamee B., Supungul P., Panyim S., Klinbunga S., Rimphanichayakit V., and Tassanakajon A. Recombinant expression and characterization of five-domain Kazal-type serine proteinase inhibitor of black tiger shrimp (Penaeus monodon). Mar Biotechnol (NY) 7 1 (2005) 46-52
    • (2005) Mar Biotechnol (NY) , vol.7 , Issue.1 , pp. 46-52
    • Jarasrassamee, B.1    Supungul, P.2    Panyim, S.3    Klinbunga, S.4    Rimphanichayakit, V.5    Tassanakajon, A.6
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation 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.M.1
  • 17
    • 0023656771 scopus 로고
    • Purification and characterization of a high-Mr proteinase inhibitor of pro-phenol oxidase activation from crayfish plasma
    • Hergenhahn H.G., Aspan A., and Söderhäll K. Purification and characterization of a high-Mr proteinase inhibitor of pro-phenol oxidase activation from crayfish plasma. Biochem J 248 1 (1987) 223-228
    • (1987) Biochem J , vol.248 , Issue.1 , pp. 223-228
    • Hergenhahn, H.G.1    Aspan, A.2    Söderhäll, K.3
  • 18
    • 0031240609 scopus 로고    scopus 로고
    • A neural network method for identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., and von Heijne G. A neural network method for identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Int J Neural Syst 8 5-6 (1997) 581-599
    • (1997) Int J Neural Syst , vol.8 , Issue.5-6 , pp. 581-599
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 19
    • 0036204976 scopus 로고    scopus 로고
    • Genetic design for facilitated production and recovery of recombinant proteins in Escherichia coli
    • Jonasson P., Liljeqvist S., Nygren P.A., and Stahl S. Genetic design for facilitated production and recovery of recombinant proteins in Escherichia coli. Biotechnol Appl Biochem 35 Pt 2 (2002) 91-105
    • (2002) Biotechnol Appl Biochem , vol.35 , Issue.PART 2 , pp. 91-105
    • Jonasson, P.1    Liljeqvist, S.2    Nygren, P.A.3    Stahl, S.4
  • 20
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx F., and Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat Biotechnol 22 11 (2004) 1399-1408
    • (2004) Nat Biotechnol , vol.22 , Issue.11 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 21
    • 25644432194 scopus 로고    scopus 로고
    • A second Kazal-like protease inhibitor from Phytophthora infestans inhibits and interacts with the apoplastic pathogenesis-related protease P69B of tomato
    • Tian M., Benedetti B., and Kamoun S. A second Kazal-like protease inhibitor from Phytophthora infestans inhibits and interacts with the apoplastic pathogenesis-related protease P69B of tomato. Plant Physiol 138 3 (2005) 1785-1793
    • (2005) Plant Physiol , vol.138 , Issue.3 , pp. 1785-1793
    • Tian, M.1    Benedetti, B.2    Kamoun, S.3
  • 22
    • 33947444147 scopus 로고
    • Isolation of a crystalline trypsin inhibitor-anticoagulant protein from pancreas
    • Kazal L.A., Spicer D.S., and Brahinsky R.A. Isolation of a crystalline trypsin inhibitor-anticoagulant protein from pancreas. J Am Chem Soc 70 9 (1948) 3034-3040
    • (1948) J Am Chem Soc , vol.70 , Issue.9 , pp. 3034-3040
    • Kazal, L.A.1    Spicer, D.S.2    Brahinsky, R.A.3
  • 23
    • 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 2 (1992) 433-451
    • (1992) Eur J Biochem , vol.204 , Issue.2 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 25
    • 0023433076 scopus 로고
    • The covalent structure of the elastase inhibitor from Anemonia sulcata-a 'non-classical' Kazal-type protein
    • Tschesche H., Kolkenbrock H., and Bode W. The covalent structure of the elastase inhibitor from Anemonia sulcata-a 'non-classical' Kazal-type protein. Biol Chem Hoppe-Seyler 368 10 (1987) 1297-1304
    • (1987) Biol Chem Hoppe-Seyler , vol.368 , Issue.10 , pp. 1297-1304
    • Tschesche, H.1    Kolkenbrock, H.2    Bode, W.3
  • 26
    • 0030699522 scopus 로고    scopus 로고
    • Purification and characterization of a novel Kazal-type serine proteinase inhibitor of neutrophil elastase from sheep lung
    • Mistry R., Snashall P.D., Totty N., Briskin S., Guz A., and Tetley T.D. Purification and characterization of a novel Kazal-type serine proteinase inhibitor of neutrophil elastase from sheep lung. Biochim Biophys Acta 1342 1 (1997) 51-61
    • (1997) Biochim Biophys Acta , vol.1342 , Issue.1 , pp. 51-61
    • Mistry, R.1    Snashall, P.D.2    Totty, N.3    Briskin, S.4    Guz, A.5    Tetley, T.D.6
  • 27
    • 0034771748 scopus 로고    scopus 로고
    • Identification of four small molecular mass proteins in the silk of Bombyx mori
    • Nirmala X., Mita K., Vanisree V., Zurovec M., and Sehnal F. Identification of four small molecular mass proteins in the silk of Bombyx mori. Insect Mol Biol 10 5 (2001) 437-445
    • (2001) Insect Mol Biol , vol.10 , Issue.5 , pp. 437-445
    • Nirmala, X.1    Mita, K.2    Vanisree, V.3    Zurovec, M.4    Sehnal, F.5
  • 28
    • 0034844371 scopus 로고    scopus 로고
    • Insect silk contains both a Kunitz-type and a unique Kazal-type proteinase inhibitor
    • Nirmala X., Kodrík D., Žurovec M., and Sehnal F. Insect silk contains both a Kunitz-type and a unique Kazal-type proteinase inhibitor. Eur J Biochem 268 7 (2001) 2064-2073
    • (2001) Eur J Biochem , vol.268 , Issue.7 , pp. 2064-2073
    • Nirmala, X.1    Kodrík, D.2    Žurovec, M.3    Sehnal, F.4
  • 29
    • 0031817835 scopus 로고    scopus 로고
    • The inhibition of extracellular proteinases from Aphanomyces spp. by three different proteinase inhibitors from crayfish blood
    • Dieguez-Uribeondo J., and Cerenius L. The inhibition of extracellular proteinases from Aphanomyces spp. by three different proteinase inhibitors from crayfish blood. Mycol Res 102 7 (1998) 820-824
    • (1998) Mycol Res , vol.102 , Issue.7 , pp. 820-824
    • Dieguez-Uribeondo, J.1    Cerenius, L.2
  • 30
    • 19344377535 scopus 로고    scopus 로고
    • Interactions between the innate immune and blood coagulation systems
    • Esmon C.T. Interactions between the innate immune and blood coagulation systems. Trends Immunol 25 10 (2004) 536-542
    • (2004) Trends Immunol , vol.25 , Issue.10 , pp. 536-542
    • Esmon, C.T.1
  • 31
    • 1842800032 scopus 로고    scopus 로고
    • Coagulation in arthropods: defense, wound closure and healing
    • Theopold U., Schmidt O., Söderhäll K., and Dushay M.S. Coagulation in arthropods: defense, wound closure and healing. Trends Immunol 25 6 (2004) 289-294
    • (2004) Trends Immunol , vol.25 , Issue.6 , pp. 289-294
    • Theopold, U.1    Schmidt, O.2    Söderhäll, K.3    Dushay, M.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.