메뉴 건너뛰기




Volumn 37, Issue 1, 2014, Pages 115-121

Molecular characterization, expression and function analysis of a five-domain Kazal-type serine proteinase inhibitor from pearl oyster Pinctada fucata

Author keywords

Inhibitory activity; Microbial challenge; Pinctada fucata; Quantitative real time PCR; Serine proteinase inhibitor

Indexed keywords

CHYMOTRYPSIN; COMPLEMENTARY DNA; PRIMER DNA; RECOMBINANT PROTEIN; SERINE PROTEINASE INHIBITOR; TRYPSIN INHIBITOR;

EID: 84893699366     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2013.12.011     Document Type: Article
Times cited : (15)

References (38)
  • 1
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski M., Kato I. Protein inhibitors of proteinases. Annu Rev Biochem 1980, 49:593-626.
    • (1980) Annu Rev Biochem , vol.49 , pp. 593-626
    • Laskowski, M.1    Kato, I.2
  • 2
    • 33646495280 scopus 로고    scopus 로고
    • Cell-mediated immunity in arthropods: hematopoiesis, coagulation, melanization and opsonization
    • Jiravanichpaisal P., Lee B.L., Söderhöll K. Cell-mediated immunity in arthropods: hematopoiesis, coagulation, melanization and opsonization. Immunobiology 2006, 211(4):213-236.
    • (2006) Immunobiology , vol.211 , Issue.4 , pp. 213-236
    • Jiravanichpaisal, P.1    Lee, B.L.2    Söderhöll, K.3
  • 3
    • 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., Yang W.J. A male-reproduction related Kazal-type peptidase inhibitor gene in the prawn, Macrobrachium rosenbergii: molecular characterization and expression patterns. Mar Biotechnol 2007, 9:45-55.
    • (2007) Mar Biotechnol , vol.9 , pp. 45-55
    • Cao, J.X.1    Dai, J.Q.2    Dai, Z.M.3    Yin, G.L.4    Yang, W.J.5
  • 4
    • 67650469954 scopus 로고    scopus 로고
    • Kazal-type serine proteinase inhibitors from the black tiger shrimp Penaeus monodon and the inhibitory activities of SPIPm4 and 5
    • Visetnan S., Donpudsa S., Supungul P., Tassanakajon A., Rimphanitchayakit V. Kazal-type serine proteinase inhibitors from the black tiger shrimp Penaeus monodon and the inhibitory activities of SPIPm4 and 5. Fish Shellfish Immunol 2009, 27(2):266-274.
    • (2009) Fish Shellfish Immunol , vol.27 , Issue.2 , pp. 266-274
    • Visetnan, S.1    Donpudsa, S.2    Supungul, P.3    Tassanakajon, A.4    Rimphanitchayakit, V.5
  • 5
    • 64149092569 scopus 로고    scopus 로고
    • Identification of a Kazal-type serine protease inhibitor with potent anti-staphylococcal activity as part of Hydra's innate immune system
    • Augustin R., Siebert S., Bosch T.C. Identification of a Kazal-type serine protease inhibitor with potent anti-staphylococcal activity as part of Hydra's innate immune system. Dev Comp Immunol 2009, 33:830-837.
    • (2009) Dev Comp Immunol , vol.33 , pp. 830-837
    • Augustin, R.1    Siebert, S.2    Bosch, T.C.3
  • 6
    • 58649094873 scopus 로고    scopus 로고
    • Domain inhibitory and bacteriostatic activities of the five-domain Kazal-type serine proteinase inhibitor from black tiger shrimp Penaeus monodon
    • Donpudsa S., Tassanakajon A., Rimphanitchayakit V. Domain inhibitory and bacteriostatic activities of the five-domain Kazal-type serine proteinase inhibitor from black tiger shrimp Penaeus monodon. Dev Comp Immunol 2009, 33(4):481-488.
    • (2009) Dev Comp Immunol , vol.33 , Issue.4 , pp. 481-488
    • Donpudsa, S.1    Tassanakajon, A.2    Rimphanitchayakit, V.3
  • 7
    • 77951126524 scopus 로고    scopus 로고
    • Three Kazal-type serine proteinase inhibitors from the red swamp crayfish Procambarus clarkii and the characterization, function analysis of hcPcSPI2
    • 5-6
    • Li X.C., Zhang R.R., Sun R.R., Lan J.F., Zhao X.F., Wang J.X. Three Kazal-type serine proteinase inhibitors from the red swamp crayfish Procambarus clarkii and the characterization, function analysis of hcPcSPI2. Fish Shellfish Immunol 2010, 28(5-6):942-951.
    • (2010) Fish Shellfish Immunol , vol.28 , pp. 942-951
    • Li, X.C.1    Zhang, R.R.2    Sun, R.R.3    Lan, J.F.4    Zhao, X.F.5    Wang, J.X.6
  • 8
    • 0346668362 scopus 로고    scopus 로고
    • Functional analysis of Toxoplasma gondii protease inhibitor 1
    • Morris M.T., Coppin A., Tomavo S., Carruthers V.B. Functional analysis of Toxoplasma gondii protease inhibitor 1. J Biol Chem 2002, 277:45259-45266.
    • (2002) J Biol Chem , vol.277 , pp. 45259-45266
    • Morris, M.T.1    Coppin, A.2    Tomavo, S.3    Carruthers, V.B.4
  • 10
    • 0038474360 scopus 로고    scopus 로고
    • Dipetalogastin, a potent thrombin inhibitor from the blood-sucking insect Dipetalogaster maximus
    • Mende K., Petoukhova O., Koulitchkova V., Schaub G.A., Lange U., Kaufmann R., et al. Dipetalogastin, a potent thrombin inhibitor from the blood-sucking insect Dipetalogaster maximus. Eur J Biochem 1999, 266:583-590.
    • (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
  • 11
    • 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., et al. 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 2002, 32:991-997.
    • (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
  • 12
    • 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 1995, 14(21):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
  • 13
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode W., Huber R. Natural protein proteinase inhibitors and their interaction with proteinases. Eur J Biochem 1992, 204:433-451.
    • (1992) Eur J Biochem , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 14
    • 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 2001, 98(4):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
  • 15
    • 74449087251 scopus 로고    scopus 로고
    • Structure and function of invertebrate Kazal-type serine proteinase inhibitors
    • Rimphanitchayakit V., Tassanakajon A. Structure and function of invertebrate Kazal-type serine proteinase inhibitors. Dev Comp Immunol 2010, 34(4):377-386.
    • (2010) Dev Comp Immunol , vol.34 , Issue.4 , pp. 377-386
    • Rimphanitchayakit, V.1    Tassanakajon, A.2
  • 16
    • 84863301289 scopus 로고    scopus 로고
    • The first Kazal-type serine proteinase inhibitor in the swimming crab Portunus trituberculatus involved in immune response to bacteria and fungi
    • Wang S.Y., Cui Z.X., Liu Y., Li Q.Q., Song C.W. The first Kazal-type serine proteinase inhibitor in the swimming crab Portunus trituberculatus involved in immune response to bacteria and fungi. Aquaculture 2012, 356-357:55-60.
    • (2012) Aquaculture , pp. 55-60
    • Wang, S.Y.1    Cui, Z.X.2    Liu, Y.3    Li, Q.Q.4    Song, C.W.5
  • 17
    • 84861483250 scopus 로고    scopus 로고
    • A new type of Kazal proteinase inhibitor related to shrimp Penaeus (Litopenaeus) vannamei immunity
    • Vargas-Albores F., Villalpando E. A new type of Kazal proteinase inhibitor related to shrimp Penaeus (Litopenaeus) vannamei immunity. Fish Shellfish Immunol 2012, 33(1):134-137.
    • (2012) Fish Shellfish Immunol , vol.33 , Issue.1 , pp. 134-137
    • Vargas-Albores, F.1    Villalpando, E.2
  • 18
    • 84855923203 scopus 로고    scopus 로고
    • Two Kazal-type protease inhibitors from Macrobrachium nipponense and Eriocheir sinensis: comparative analysis of structure and activities
    • Qian Y.Q., Li Y., Yang F., Yu Y.Q., Yang J.S., Yang W.J. Two Kazal-type protease inhibitors from Macrobrachium nipponense and Eriocheir sinensis: comparative analysis of structure and activities. Fish Shellfish Immunol 2012, 32(3):446-458.
    • (2012) Fish Shellfish Immunol , vol.32 , Issue.3 , pp. 446-458
    • Qian, Y.Q.1    Li, Y.2    Yang, F.3    Yu, Y.Q.4    Yang, J.S.5    Yang, W.J.6
  • 19
    • 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.S., Chang Y.Q., Xu W., Wu L.T. Molecular cloning, characterization and expression of a novel serine proteinase inhibitor gene in bay scallops (Argopecten irradians, Lamarck 1819). Fish Shellfish Immunol 2006, 20(3):320-331.
    • (2006) Fish Shellfish Immunol , vol.20 , Issue.3 , pp. 320-331
    • Zhu, L.1    Song, L.S.2    Chang, Y.Q.3    Xu, W.4    Wu, L.T.5
  • 20
    • 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 2008, 24(5):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
  • 21
    • 84877632084 scopus 로고    scopus 로고
    • Molecular characterization of two Kazal-type serine proteinase inhibitor genes in the surf clam Mesodesma donacium exposed to Vibrio anguillarum
    • Maldonado-Aguayo W., Núñez-Acuña G., Valenzuela-Muñoz V., Chávez-Mardones J., Gallardo-Escárate C. Molecular characterization of two Kazal-type serine proteinase inhibitor genes in the surf clam Mesodesma donacium exposed to Vibrio anguillarum. Fish Shellfish Immunol 2013, 34(6):1448-1454.
    • (2013) Fish Shellfish Immunol , vol.34 , Issue.6 , pp. 1448-1454
    • Maldonado-Aguayo, W.1    Núñez-Acuña, G.2    Valenzuela-Muñoz, V.3    Chávez-Mardones, J.4    Gallardo-Escárate, C.5
  • 22
    • 84882841913 scopus 로고    scopus 로고
    • Kazal-type proteinase inhibitor from disk abalone (Haliotis discus discus): molecular characterization and transcriptional response upon immune stimulation
    • Wickramaarachchi W.D., De Zoysa M., Whang I., Wan Q., Lee J. Kazal-type proteinase inhibitor from disk abalone (Haliotis discus discus): molecular characterization and transcriptional response upon immune stimulation. Fish Shellfish Immunol 2013, 35:1039-1043.
    • (2013) Fish Shellfish Immunol , vol.35 , pp. 1039-1043
    • Wickramaarachchi, W.D.1    De Zoysa, M.2    Whang, I.3    Wan, Q.4    Lee, J.5
  • 23
    • 59549084520 scopus 로고    scopus 로고
    • Molecular characterization and expression analysis of the IκB gene from pearl oyster Pinctada fucata
    • Zhang D.C., Jiang S.G., Qiu L.H., Su T.F., Wu K.C., Li Y.N., et al. Molecular characterization and expression analysis of the IκB gene from pearl oyster Pinctada fucata. Fish Shellfish Immunol 2009, 26(1):84-90.
    • (2009) Fish Shellfish Immunol , vol.26 , Issue.1 , pp. 84-90
    • Zhang, D.C.1    Jiang, S.G.2    Qiu, L.H.3    Su, T.F.4    Wu, K.C.5    Li, Y.N.6
  • 24
    • 77957877692 scopus 로고    scopus 로고
    • A multidomain galectin involved in innate immune response of pearl oyster Pinctada fucata
    • Zhang D.C., Jiang S.G., Hu Y.T., Cui S.G., Guo H.Y., Wu K.C., et al. A multidomain galectin involved in innate immune response of pearl oyster Pinctada fucata. Dev Comp Immunol 2011, 35(1):1-6.
    • (2011) Dev Comp Immunol , vol.35 , Issue.1 , pp. 1-6
    • Zhang, D.C.1    Jiang, S.G.2    Hu, Y.T.3    Cui, S.G.4    Guo, H.Y.5    Wu, K.C.6
  • 25
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen T.N., Brunak S., von Heijne G., Nielsen H. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 2011, 8(10):785-786.
    • (2011) Nat Methods , vol.8 , Issue.10 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 28
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K., Peterson D., Peterson N., Stecher G., Nei M., Kumar S. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 2011, 28:2731-2739.
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 29
    • 79959784118 scopus 로고    scopus 로고
    • A macrophage migration inhibitory factor like oxidoreductase from pearl oyster Pinctada fucata involved in innate immune responses
    • Cui S.G., Zhang D.C., Jiang S.G., Pu H.L., Hu Y.T., Guo H.Y., et al. A macrophage migration inhibitory factor like oxidoreductase from pearl oyster Pinctada fucata involved in innate immune responses. Fish Shellfish Immunol 2011, 31(2):173-181.
    • (2011) Fish Shellfish Immunol , vol.31 , Issue.2 , pp. 173-181
    • Cui, S.G.1    Zhang, D.C.2    Jiang, S.G.3    Pu, H.L.4    Hu, Y.T.5    Guo, H.Y.6
  • 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., Söderhöll K. Purification and characterization of a high-Mr proteinase inhibitor of pro-phenol oxidase activation from crayfish plasma. Biochem J 1987, 248:223-228.
    • (1987) Biochem J , vol.248 , pp. 223-228
    • Hergenhahn, H.G.1    Aspan, A.2    Söderhöll, K.3
  • 31
    • 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., Söllner C., Mentele R., Piechottka G.P., Auerswald E.A., 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 1994, 375(10):685-694.
    • (1994) Biol Chem Hoppe Seyler , vol.375 , Issue.10 , pp. 685-694
    • Sommerhoff, C.P.1    Söllner, C.2    Mentele, R.3    Piechottka, G.P.4    Auerswald, E.A.5    Fritz, H.6
  • 32
    • 13544251554 scopus 로고    scopus 로고
    • A four-Kazal domain protein in Litopenaeus vannamei hemocytes
    • Jiménez-Vega F., Vargas-Albores F. A four-Kazal domain protein in Litopenaeus vannamei hemocytes. Dev Comp Immunol 2005, 29:385-391.
    • (2005) Dev Comp Immunol , vol.29 , pp. 385-391
    • Jiménez-Vega, F.1    Vargas-Albores, F.2
  • 33
    • 0030754090 scopus 로고    scopus 로고
    • The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition
    • Stubbs M.T., Morenweiser R., Sturzebecher J., Bauer M., Bode W., Huber R., et al. The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition. J Biol Chem 1997, 272:19931-19937.
    • (1997) J Biol Chem , vol.272 , pp. 19931-19937
    • Stubbs, M.T.1    Morenweiser, R.2    Sturzebecher, J.3    Bauer, M.4    Bode, W.5    Huber, R.6
  • 35
    • 5644268137 scopus 로고    scopus 로고
    • Defense mechanisms in farmed marine mollusks
    • Tisca P.G., Mosca F. Defense mechanisms in farmed marine mollusks. Vet Res Commun 2004, 28:57-62.
    • (2004) Vet Res Commun , vol.28 , pp. 57-62
    • Tisca, P.G.1    Mosca, F.2
  • 36
    • 0028826920 scopus 로고
    • Serine protease inhibition by insect peptides containing a cysteine knot and a triplestranded beta-sheet
    • Kellenberger C., Boudier C., Bermudez I., Bieth J.G., Luu B., Hietter H. Serine protease inhibition by insect peptides containing a cysteine knot and a triplestranded beta-sheet. J Biol Chem 1995, 270:25514-25519.
    • (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
  • 37
    • 0027980413 scopus 로고
    • Purification and cDNA cloning of a fourdomain Kazal proteinase inhibitor from crayfish blood cells
    • Johansson M.W., Keyser P., Söderhall K. Purification and cDNA cloning of a fourdomain Kazal proteinase inhibitor from crayfish blood cells. Eur J Biochem 1994, 223(2):389-394.
    • (1994) Eur J Biochem , vol.223 , Issue.2 , pp. 389-394
    • Johansson, M.W.1    Keyser, P.2    Söderhall, K.3
  • 38
    • 33746321298 scopus 로고    scopus 로고
    • A fivedomain Kazal-type serine proteinase inhibitor from black tiger shrimp Penaeus monodon and its inhibitory activities
    • Somprasong N., Rimphanitchayakit V., Tassanakajon A. A fivedomain Kazal-type serine proteinase inhibitor from black tiger shrimp Penaeus monodon and its inhibitory activities. Dev Comp Immunol 2006, 30:998-1008.
    • (2006) Dev Comp Immunol , vol.30 , pp. 998-1008
    • Somprasong, N.1    Rimphanitchayakit, V.2    Tassanakajon, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.