메뉴 건너뛰기




Volumn 33, Issue 4, 2009, Pages 481-488

Domain inhibitory and bacteriostatic activities of the five-domain Kazal-type serine proteinase inhibitor from black tiger shrimp Penaeus monodon

Author keywords

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

Indexed keywords

ELASTASE; SERINE PROTEINASE INHIBITOR; SERINE PROTEINASE INHIBITOR PM2; SUBTILISIN; TRYPSIN; UNCLASSIFIED DRUG;

EID: 58649094873     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2008.09.009     Document Type: Article
Times cited : (64)

References (37)
  • 1
    • 1642463826 scopus 로고    scopus 로고
    • The prophenoloxidase-activating system in invertebrates
    • Cerenius L., and Söderhäll K. The prophenoloxidase-activating system in invertebrates. Immunol Rev 198 (2004) 116-126
    • (2004) Immunol Rev , vol.198 , pp. 116-126
    • Cerenius, L.1    Söderhäll, K.2
  • 2
    • 33646495280 scopus 로고    scopus 로고
    • Cell-mediated immunity in arthropods: hematopoiesis, coagulation, melanization and opsonization
    • Jiravanichpaisal P., Lee B.L., and Söderhäll K. Cell-mediated immunity in arthropods: hematopoiesis, coagulation, melanization and opsonization. Immunobiology 211 4 (2006) 213-236
    • (2006) Immunobiology , vol.211 , Issue.4 , pp. 213-236
    • Jiravanichpaisal, P.1    Lee, B.L.2    Söderhäll, K.3
  • 3
    • 20444506858 scopus 로고    scopus 로고
    • Recent advances in the innate immunity of invertebrate animals
    • Iwanaga S., and Lee B.L. Recent advances in the innate immunity of invertebrate animals. J Biochem Mol Biol 38 2 (2005) 128-150
    • (2005) J Biochem Mol Biol , vol.38 , Issue.2 , pp. 128-150
    • Iwanaga, S.1    Lee, B.L.2
  • 4
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski Jr. M., and Kato I. Protein inhibitors of proteinases. Annu Rev Biochem 49 (1980) 593-626
    • (1980) Annu Rev Biochem , vol.49 , pp. 593-626
    • Laskowski Jr., M.1    Kato, I.2
  • 5
    • 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
  • 6
    • 0342445397 scopus 로고    scopus 로고
    • What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes?
    • Laskowski M., and Qasim M.A. What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes?. Biochim Biophys Acta 1477 1-2 (2000) 324-337
    • (2000) Biochim Biophys Acta , vol.1477 , Issue.1-2 , pp. 324-337
    • Laskowski, M.1    Qasim, M.A.2
  • 7
    • 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., et al. 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
  • 8
    • 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
  • 9
    • 0346668362 scopus 로고    scopus 로고
    • Functional analysis of Toxoplasma gondii protease inhibitor 1
    • Morris M.T., Coppin A., Tomavo S., and Carruthers V.B. Functional analysis of Toxoplasma gondii protease inhibitor 1. J Biol Chem 277 47 (2002) 45259-45266
    • (2002) J Biol Chem , vol.277 , Issue.47 , pp. 45259-45266
    • Morris, M.T.1    Coppin, A.2    Tomavo, S.3    Carruthers, V.B.4
  • 10
    • 33846600367 scopus 로고    scopus 로고
    • Expression, purification and characterization of a three-domain Kazal-type inhibitor from silkworm pupae (Bombyx mori)
    • Zheng Q.L., Chen J., Nie Z.M., Lv Z.B., Wang D., and Zhang Y.Z. Expression, purification and characterization of a three-domain Kazal-type inhibitor from silkworm pupae (Bombyx mori). Comp Biochem Physiol B: Biochem Mol Biol 146 2 (2007) 234-240
    • (2007) Comp Biochem Physiol B: Biochem Mol Biol , vol.146 , Issue.2 , pp. 234-240
    • Zheng, Q.L.1    Chen, J.2    Nie, Z.M.3    Lv, Z.B.4    Wang, D.5    Zhang, Y.Z.6
  • 11
    • 28044470978 scopus 로고    scopus 로고
    • Evolutionary mechanisms acting on proteinase inhibitor variability
    • Christeller J.T. Evolutionary mechanisms acting on proteinase inhibitor variability. FEBS J 272 22 (2005) 5710-5722
    • (2005) FEBS J , vol.272 , Issue.22 , pp. 5710-5722
    • Christeller, J.T.1
  • 12
    • 25644440644 scopus 로고    scopus 로고
    • A two disulfide bridge Kazal domain from Phytophthora exhibits stable inhibitory activity against serine proteases of the subtilisin family
    • Tian M., and Kamoun S. A two disulfide bridge Kazal domain from Phytophthora exhibits stable inhibitory activity against serine proteases of the subtilisin family. BMC Biochem 6 (2005) 15
    • (2005) BMC Biochem , vol.6 , pp. 15
    • Tian, M.1    Kamoun, S.2
  • 13
    • 0032992544 scopus 로고    scopus 로고
    • Serine proteinase inhibitors in arthropod immunity
    • Kanost M.R. Serine proteinase inhibitors in arthropod immunity. Dev Comp Immunol 23 4-5 (1999) 291-301
    • (1999) Dev Comp Immunol , vol.23 , Issue.4-5 , pp. 291-301
    • Kanost, M.R.1
  • 14
    • 0346729741 scopus 로고    scopus 로고
    • Genomics, evolution and biological functions of the pacifastin peptide family: a conserved serine protease inhibitor family in arthropods
    • Simonet G., Claeys I., Franssens V., De Loof A., and Broeck J.V. Genomics, evolution and biological functions of the pacifastin peptide family: a conserved serine protease inhibitor family in arthropods. Peptides 24 10 (2003) 1633-1644
    • (2003) Peptides , vol.24 , Issue.10 , pp. 1633-1644
    • Simonet, G.1    Claeys, I.2    Franssens, V.3    De Loof, A.4    Broeck, J.V.5
  • 15
    • 1642464622 scopus 로고    scopus 로고
    • Evolutionary families of peptidase inhibitors
    • Rawlings N.D., Tolle D.P., and Barrett A.J. Evolutionary families of peptidase inhibitors. Biochem J 378 Pt 3 (2004) 705-716
    • (2004) Biochem J , vol.378 , Issue.PART 3 , pp. 705-716
    • Rawlings, N.D.1    Tolle, D.P.2    Barrett, A.J.3
  • 16
    • 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., Kröger B., et al. 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    Kröger, B.6
  • 17
    • 0035852744 scopus 로고    scopus 로고
    • Predicting the reactivity of proteins from their sequence alone: Kazal family of protein inhibitors of serine proteinases
    • Lu S.M., Lu W., Qasim M.A., Anderson S., Apostol I., Ardelt W., et al. Predicting the reactivity of proteins from their sequence alone: Kazal family of protein inhibitors of serine proteinases. Proc Natl Acad Sci USA 98 4 (2001) 1410-1415
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.4 , pp. 1410-1415
    • Lu, S.M.1    Lu, W.2    Qasim, M.A.3    Anderson, S.4    Apostol, I.5    Ardelt, W.6
  • 19
    • 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
  • 20
    • 13544251554 scopus 로고    scopus 로고
    • A four-Kazal domain protein in Litopenaeus vannamei hemocytes
    • Jiménez-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
    • Jiménez-Vega, F.1    Vargas-Albores, F.2
  • 21
    • 33746321298 scopus 로고    scopus 로고
    • A five-domain Kazal-type serine proteinase inhibitor from black tiger shrimp Penaeus monodon and its inhibitory activities
    • Somprasong N., Rimphanitchayakit V., and Tassanakajon A. A five-domain Kazal-type serine proteinase inhibitor from black tiger shrimp Penaeus monodon and its inhibitory activities. Dev Comp Immunol 30 11 (2006) 998-1008
    • (2006) Dev Comp Immunol , vol.30 , Issue.11 , pp. 998-1008
    • Somprasong, N.1    Rimphanitchayakit, V.2    Tassanakajon, A.3
  • 22
    • 22244438235 scopus 로고    scopus 로고
    • Structural and functional study of an Anemonia elastase inhibitor, a "nonclassical" Kazal-type inhibitor from Anemonia sulcata
    • Hemmi H., Kumazaki T., Yoshizawa-Kumagaye K., Nishiuchi Y., Yoshida T., Ohkubo T., et al. Structural and functional study of an Anemonia elastase inhibitor, a "nonclassical" Kazal-type inhibitor from Anemonia sulcata. Biochemistry 44 28 (2005) 9626-9636
    • (2005) Biochemistry , vol.44 , Issue.28 , pp. 9626-9636
    • Hemmi, H.1    Kumazaki, T.2    Yoshizawa-Kumagaye, K.3    Nishiuchi, Y.4    Yoshida, T.5    Ohkubo, T.6
  • 23
    • 33845802542 scopus 로고    scopus 로고
    • A novel locust (Schistocerca gregaria) serine protease inhibitor with a high affinity for neutrophil elastase
    • Brillard-Bourdet M., Hamdaoui A., Hajjar E., Boudier C., Reuter N., Ehret-Sabatier L., et al. A novel locust (Schistocerca gregaria) serine protease inhibitor with a high affinity for neutrophil elastase. Biochem J 400 3 (2006) 467-476
    • (2006) Biochem J , vol.400 , Issue.3 , pp. 467-476
    • Brillard-Bourdet, M.1    Hamdaoui, A.2    Hajjar, E.3    Boudier, C.4    Reuter, N.5    Ehret-Sabatier, L.6
  • 24
    • 25844455314 scopus 로고    scopus 로고
    • Molecular cloning, characterization and expression of a novel serine proteinase inhibitor gene in bay scallops (Argopecten irradians, Lamarck 1819)
    • Zhu L., Song L., Chang Y., Xu W., and Wu L. Molecular cloning, characterization and expression of a novel serine proteinase inhibitor gene in bay scallops (Argopecten irradians, Lamarck 1819). Fish Shellfish Immunol 20 3 (2006) 320-331
    • (2006) Fish Shellfish Immunol , vol.20 , Issue.3 , pp. 320-331
    • Zhu, L.1    Song, L.2    Chang, Y.3    Xu, W.4    Wu, L.5
  • 25
    • 33847338086 scopus 로고    scopus 로고
    • Purification and partial characterization of human neutrophil elastase inhibitors from the marine snail Cenchritis muricatus (Mollusca)
    • González Y., Tanaka A.S., Hirata I.Y., del Rivero M.A., Oliva M.L., Araujo M.S., et al. Purification and partial characterization of human neutrophil elastase inhibitors from the marine snail Cenchritis muricatus (Mollusca). Comp Biochem Physiol A: Mol Integr Physiol 146 4 (2007) 506-513
    • (2007) Comp Biochem Physiol A: Mol Integr Physiol , vol.146 , Issue.4 , pp. 506-513
    • González, Y.1    Tanaka, A.S.2    Hirata, I.Y.3    del Rivero, M.A.4    Oliva, M.L.5    Araujo, M.S.6
  • 26
    • 33847383646 scopus 로고    scopus 로고
    • A male reproduction-related Kazal-type peptidase inhibitor gene in the prawn. Macrobrachium rosenbergii: molecular characterization and expression patterns
    • Cao J.X., Dai J.Q., Dai Z.M., Yin G.L., and Yang W.J. A male reproduction-related Kazal-type peptidase inhibitor gene in the prawn. Macrobrachium rosenbergii: molecular characterization and expression patterns. Mar Biotechnol (NY) 9 1 (2007) 45-55
    • (2007) Mar Biotechnol (NY) , vol.9 , Issue.1 , pp. 45-55
    • Cao, J.X.1    Dai, J.Q.2    Dai, Z.M.3    Yin, G.L.4    Yang, W.J.5
  • 27
    • 41949130870 scopus 로고    scopus 로고
    • Molecular cloning and expression of a novel Kazal-type serine proteinase inhibitor gene from Zhikong scallop Chlamys farreri, and the inhibitory activity of its recombinant domain
    • Wang B., Zhao J., Song L., Zhang H., Wang L., Li C., et al. Molecular cloning and expression of a novel Kazal-type serine proteinase inhibitor gene from Zhikong scallop Chlamys farreri, and the inhibitory activity of its recombinant domain. Fish Shellfish Immunol 24 5 (2008) 629-637
    • (2008) Fish Shellfish Immunol , vol.24 , Issue.5 , pp. 629-637
    • Wang, B.1    Zhao, J.2    Song, L.3    Zhang, H.4    Wang, L.5    Li, C.6
  • 28
    • 33750965196 scopus 로고    scopus 로고
    • Penaeus monodon gene discovery project: the generation of an EST collection and establishment of a database
    • Tassanakajon A., Klinbunga S., Paunglarp N., Rimphanitchayakit V., Udomkit A., Jitrapakdee S., et al. Penaeus monodon gene discovery project: the generation of an EST collection and establishment of a database. Gene 384 (2006) 104-112
    • (2006) Gene , vol.384 , pp. 104-112
    • Tassanakajon, A.1    Klinbunga, S.2    Paunglarp, N.3    Rimphanitchayakit, V.4    Udomkit, A.5    Jitrapakdee, S.6
  • 29
    • 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
  • 30
    • 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
  • 33
    • 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
  • 34
    • 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
  • 35
    • 0031581824 scopus 로고    scopus 로고
    • Binding of amino acid side-chains to S1 cavities of serine proteinases
    • Lu W., Apostol I., Qasim M.A., Warne N., Wynn R., Zhang W.L., et al. Binding of amino acid side-chains to S1 cavities of serine proteinases. J Mol Biol 266 2 (1997) 441-461
    • (1997) J Mol Biol , vol.266 , Issue.2 , pp. 441-461
    • Lu, W.1    Apostol, I.2    Qasim, M.A.3    Warne, N.4    Wynn, R.5    Zhang, W.L.6
  • 36
    • 0034844371 scopus 로고    scopus 로고
    • Insect silk contains both a Kunitz-type and a unique Kazal-type proteinase inhibitor
    • Nirmala X., Kodrík D., Zurovec 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    Zurovec, M.3    Sehnal, F.4
  • 37
    • 0344642994 scopus 로고    scopus 로고
    • Homologous proteins with different folds: the three-dimensional structures of domains 1 and 6 of the multiple Kazal-type inhibitor LEKTI
    • Lauber T., Schulz A., Schweimer K., Adermann K., and Marx U.C. Homologous proteins with different folds: the three-dimensional structures of domains 1 and 6 of the multiple Kazal-type inhibitor LEKTI. J Mol Biol 328 1 (2003) 205-219
    • (2003) J Mol Biol , vol.328 , Issue.1 , pp. 205-219
    • Lauber, T.1    Schulz, A.2    Schweimer, K.3    Adermann, K.4    Marx, U.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.