메뉴 건너뛰기




Volumn 33, Issue 6, 2012, Pages 1276-1284

A four-domain Kunitz-type proteinase inhibitor from Solen grandis is implicated in immune response

Author keywords

Inhibitory activity; Innate immunity; Kunitz type proteinase inhibitor; Real time PCR; Solen grandis

Indexed keywords

BIVALVIA; MOLLUSCA; SOLEN GRANDIS; SOLENIDAE;

EID: 84867983503     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2012.09.015     Document Type: Article
Times cited : (16)

References (41)
  • 1
    • 0026337077 scopus 로고
    • The coagulation cascade: initiation, maintenance, and regulation
    • Davie E.W., Fujikawa K., Kisiel W. The coagulation cascade: initiation, maintenance, and regulation. Biochemistry 1991, 30:10363-10370.
    • (1991) Biochemistry , vol.30 , pp. 10363-10370
    • Davie, E.W.1    Fujikawa, K.2    Kisiel, W.3
  • 3
    • 0036545373 scopus 로고    scopus 로고
    • Novel roles of protease inhibitors in infection and inflammation
    • Hiemstra P.S. Novel roles of protease inhibitors in infection and inflammation. Biochemical Society Transactions 2002, 30:116-120.
    • (2002) Biochemical Society Transactions , vol.30 , pp. 116-120
    • Hiemstra, P.S.1
  • 5
    • 0019364862 scopus 로고
    • The proteolytic activation systems of complement
    • Reid K.B., Porter R.R. The proteolytic activation systems of complement. Annual Review of Biochemistry 1981, 50:433-464.
    • (1981) Annual Review of Biochemistry , vol.50 , pp. 433-464
    • Reid, K.B.1    Porter, R.R.2
  • 6
    • 17644367562 scopus 로고    scopus 로고
    • Manduca sexta serpin-4 and serpin-5 inhibit the prophenol oxidase activation pathway: cDNA cloning, protein expression, and characterization
    • Tong Y., Kanost M.R. Manduca sexta serpin-4 and serpin-5 inhibit the prophenol oxidase activation pathway: cDNA cloning, protein expression, and characterization. The Journal of Biological Chemistry 2005, 280:14923-14931.
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 14923-14931
    • Tong, Y.1    Kanost, M.R.2
  • 7
    • 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 Immunology 2008, 24:629-637.
    • (2008) Fish & Shellfish Immunology , vol.24 , pp. 629-637
    • Wang, B.1    Zhao, J.2    Song, L.3    Zhang, H.4    Wang, L.5    Li, C.6
  • 9
    • 0032992544 scopus 로고    scopus 로고
    • Serine proteinase inhibitors in arthropod immunity
    • Kanost M.R. Serine proteinase inhibitors in arthropod immunity. Developmental and Comparative Immunology 1999, 23:291-301.
    • (1999) Developmental and Comparative Immunology , vol.23 , pp. 291-301
    • Kanost, M.R.1
  • 10
    • 0030345078 scopus 로고    scopus 로고
    • Serine proteinase inhibitors from insect hemolymph
    • Polanowski A., Wilusz T. Serine proteinase inhibitors from insect hemolymph. Acta Biochimica Polonica 1996, 43:445-453.
    • (1996) Acta Biochimica Polonica , vol.43 , pp. 445-453
    • Polanowski, A.1    Wilusz, T.2
  • 11
    • 2542479889 scopus 로고    scopus 로고
    • Purification, characterization, and cloning of a serine proteinase inhibitor from the ectoparasite Haematobia irritans irritans (Diptera: Muscidae)
    • Azzolini S.S., Santos J.M., Souza A.F., Torquato R.J., Hirata I.Y., Andreotti R., et al. Purification, characterization, and cloning of a serine proteinase inhibitor from the ectoparasite Haematobia irritans irritans (Diptera: Muscidae). Experimental Parasitology 2004, 106:103-109.
    • (2004) Experimental Parasitology , vol.106 , pp. 103-109
    • Azzolini, S.S.1    Santos, J.M.2    Souza, A.F.3    Torquato, R.J.4    Hirata, I.Y.5    Andreotti, R.6
  • 12
    • 8844240690 scopus 로고    scopus 로고
    • Boophilus microplus tick larvae, a rich source of Kunitz type serine proteinase inhibitors
    • Sasaki S.D., Azzolini S.S., Hirata I.Y., Andreotti R., Tanaka A.S. Boophilus microplus tick larvae, a rich source of Kunitz type serine proteinase inhibitors. Biochimie 2004, 86:643-649.
    • (2004) Biochimie , vol.86 , pp. 643-649
    • Sasaki, S.D.1    Azzolini, S.S.2    Hirata, I.Y.3    Andreotti, R.4    Tanaka, A.S.5
  • 13
    • 0025937275 scopus 로고
    • Purification and characterization of a Kunitz-type trypsin inhibitor from Leaf-nosed viper venom
    • Siddiqi A.R., Zaidi Z.H., Jornvall H. Purification and characterization of a Kunitz-type trypsin inhibitor from Leaf-nosed viper venom. FEBS Letters 1991, 294:141-143.
    • (1991) FEBS Letters , vol.294 , pp. 141-143
    • Siddiqi, A.R.1    Zaidi, Z.H.2    Jornvall, H.3
  • 14
    • 0016840544 scopus 로고
    • The amino-acid sequence of isoinhibitor K form snails (Helix pomatia). A sequence determination by automated Edman degradation and mass-spectral identification of the phenylthiohydantoins
    • Tschesche H., Dietl T. The amino-acid sequence of isoinhibitor K form snails (Helix pomatia). A sequence determination by automated Edman degradation and mass-spectral identification of the phenylthiohydantoins. European Journal of Biochemistry/FEBS 1975, 58:439-451.
    • (1975) European Journal of Biochemistry/FEBS , vol.58 , pp. 439-451
    • Tschesche, H.1    Dietl, T.2
  • 16
    • 0026795399 scopus 로고
    • Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures
    • Berndt K.D., Guntert P., Orbons L.P., Wuthrich K. Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures. Journal of Molecular Biology 1992, 227:757-775.
    • (1992) Journal of Molecular Biology , vol.227 , pp. 757-775
    • Berndt, K.D.1    Guntert, P.2    Orbons, L.P.3    Wuthrich, K.4
  • 17
    • 0342445397 scopus 로고    scopus 로고
    • What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes?
    • Laskowski M., Qasim M.A. What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes?. Biochimica et biophysica acta 2000, 1477:324-337.
    • (2000) Biochimica et biophysica acta , vol.1477 , pp. 324-337
    • Laskowski, M.1    Qasim, M.A.2
  • 18
    • 0037025213 scopus 로고    scopus 로고
    • Activation of Drosophila Toll during fungal infection by a blood serine protease
    • Ligoxygakis P., Pelte N., Hoffmann J.A., Reichhart J.M. Activation of Drosophila Toll during fungal infection by a blood serine protease. Science (New York, NY) 2002, 297:114-116.
    • (2002) Science (New York, NY) , vol.297 , pp. 114-116
    • Ligoxygakis, P.1    Pelte, N.2    Hoffmann, J.A.3    Reichhart, J.M.4
  • 19
    • 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., Zhang Y.Z. Expression, purification and characterization of a three-domain Kazal-type inhibitor from silkworm pupae (Bombyx mori). Comparative Biochemistry and Physiology 2007, 146:234-240.
    • (2007) Comparative Biochemistry and Physiology , vol.146 , 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
  • 20
    • 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
    • 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 Immunology 2010, 28:942-951.
    • (2010) Fish & Shellfish Immunology , 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
  • 21
    • 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 Immunology 2012, 32:446-458.
    • (2012) Fish & Shellfish Immunology , vol.32 , 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
  • 22
    • 84862778119 scopus 로고    scopus 로고
    • Identification and characterization of a serine protease inhibitor (PtSerpin) in the swimming crab Portunus trituberculatus
    • Wang S., Cui Z., Liu Y., Li Q., Song C. Identification and characterization of a serine protease inhibitor (PtSerpin) in the swimming crab Portunus trituberculatus. Fish & Shellfish Immunology 2012, 32:544-550.
    • (2012) Fish & Shellfish Immunology , vol.32 , pp. 544-550
    • Wang, S.1    Cui, Z.2    Liu, Y.3    Li, Q.4    Song, C.5
  • 23
    • 65649109331 scopus 로고    scopus 로고
    • Characterization, kinetics, and possible function of Kazal-type proteinase inhibitors of Chinese white shrimp, Fenneropenaeus chinensis
    • Wang Z.H., Zhao X.F., Wang J.X. Characterization, kinetics, and possible function of Kazal-type proteinase inhibitors of Chinese white shrimp, Fenneropenaeus chinensis. Fish & Shellfish Immunology 2009, 26:885-897.
    • (2009) Fish & Shellfish Immunology , vol.26 , pp. 885-897
    • Wang, Z.H.1    Zhao, X.F.2    Wang, J.X.3
  • 24
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K., Bordoli L., Kopp J., Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 2006, 22:195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 26
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(T)(-Delta Delta C) method
    • Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(T)(-Delta Delta C) method. Methods 2001, 25:402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 27
    • 84859256707 scopus 로고    scopus 로고
    • Molecular cloning and mRNA expression of two peptidoglycan recognition protein (PGRP) genes from mollusk Solen grandis
    • Wei X., Yang J., Yang D., Xu J., Liu X., Yang J., et al. Molecular cloning and mRNA expression of two peptidoglycan recognition protein (PGRP) genes from mollusk Solen grandis. Fish & Shellfish Immunology 2012, 32:178-185.
    • (2012) Fish & Shellfish Immunology , vol.32 , pp. 178-185
    • Wei, X.1    Yang, J.2    Yang, D.3    Xu, J.4    Liu, X.5    Yang, J.6
  • 29
    • 78649630097 scopus 로고    scopus 로고
    • Characterization of Kunitz-type protease inhibitor purified from hemolymph of Galleria mellonella larvae
    • Lee J.H., Kim C.H., Shin Y.P., Park H.J., Park S., Lee H.M., et al. Characterization of Kunitz-type protease inhibitor purified from hemolymph of Galleria mellonella larvae. Insect Biochemistry and Molecular Biology 2010, 40:873-882.
    • (2010) Insect Biochemistry and Molecular Biology , vol.40 , pp. 873-882
    • Lee, J.H.1    Kim, C.H.2    Shin, Y.P.3    Park, H.J.4    Park, S.5    Lee, H.M.6
  • 30
    • 74449089420 scopus 로고    scopus 로고
    • Biochemical characterization of a Kunitz type inhibitor similar to dendrotoxins produced by Rhipicephalus (Boophilus) microplus (Acari: Ixodidae) hemocytes
    • Lima C.A., Torquato R.J., Sasaki S.D., Justo G.Z., Tanaka A.S. Biochemical characterization of a Kunitz type inhibitor similar to dendrotoxins produced by Rhipicephalus (Boophilus) microplus (Acari: Ixodidae) hemocytes. Veterinary Parasitology 2010, 167:279-287.
    • (2010) Veterinary Parasitology , vol.167 , pp. 279-287
    • Lima, C.A.1    Torquato, R.J.2    Sasaki, S.D.3    Justo, G.Z.4    Tanaka, A.S.5
  • 31
    • 81255150515 scopus 로고    scopus 로고
    • Functional characterization of Kunitz-type protease inhibitor Pr-mulgins identified from New Guinean Pseudechis australis
    • Inagaki H., Kimoto H., Yamauchi Y., Toriba M., Kubo T. Functional characterization of Kunitz-type protease inhibitor Pr-mulgins identified from New Guinean Pseudechis australis. Toxicon 2012, 59:74-80.
    • (2012) Toxicon , vol.59 , pp. 74-80
    • Inagaki, H.1    Kimoto, H.2    Yamauchi, Y.3    Toriba, M.4    Kubo, T.5
  • 32
    • 74849129800 scopus 로고    scopus 로고
    • A Kunitz-type proteinase inhibitor from the midgut of the ixodid tick, Haemaphysalis longicornis, and its endogenous target serine proteinase
    • Miyoshi T., Tsuji N., Islam M.K., Alim M.A., Hatta T., Yamaji K., et al. A Kunitz-type proteinase inhibitor from the midgut of the ixodid tick, Haemaphysalis longicornis, and its endogenous target serine proteinase. Molecular and Biochemical Parasitology 2010, 170:112-115.
    • (2010) Molecular and Biochemical Parasitology , vol.170 , pp. 112-115
    • Miyoshi, T.1    Tsuji, N.2    Islam, M.K.3    Alim, M.A.4    Hatta, T.5    Yamaji, K.6
  • 33
    • 77956294309 scopus 로고    scopus 로고
    • CfLGBP, a pattern recognition receptor in Chlamys farreri involved in the immune response against various bacteria
    • Yang J., Qiu L., Wang L., Wei X., Zhang H., Zhang Y., et al. CfLGBP, a pattern recognition receptor in Chlamys farreri involved in the immune response against various bacteria. Fish & Shellfish Immunology 2010, 29:825-831.
    • (2010) Fish & Shellfish Immunology , vol.29 , pp. 825-831
    • Yang, J.1    Qiu, L.2    Wang, L.3    Wei, X.4    Zhang, H.5    Zhang, Y.6
  • 34
    • 79951867051 scopus 로고    scopus 로고
    • C-type lectin in Chlamys farreri (CfLec-1) mediating immune recognition and opsonization
    • Yang J., Wang L., Zhang H., Qiu L., Wang H., Song L. C-type lectin in Chlamys farreri (CfLec-1) mediating immune recognition and opsonization. PloS One 2011, 6:e17089.
    • (2011) PloS One , vol.6
    • Yang, J.1    Wang, L.2    Zhang, H.3    Qiu, L.4    Wang, H.5    Song, L.6
  • 35
    • 67349211169 scopus 로고    scopus 로고
    • A novel C-type lectin (Cflec-3) from Chlamys farreri with three carbohydrate-recognition domains
    • Zhang H., Wang H., Wang L., Song X., Zhao J., Qiu L., et al. A novel C-type lectin (Cflec-3) from Chlamys farreri with three carbohydrate-recognition domains. Fish & Shellfish Immunology 2009, 26:707-715.
    • (2009) Fish & Shellfish Immunology , vol.26 , pp. 707-715
    • Zhang, H.1    Wang, H.2    Wang, L.3    Song, X.4    Zhao, J.5    Qiu, L.6
  • 36
    • 5344266791 scopus 로고    scopus 로고
    • Overexpression in Escherichia coli and purification of recombinant CI-b1, a Kunitz-type chymotrypsin inhibitor of silkworm
    • He N., Fujii H., Kusakabe T., Aso Y., Banno Y., Yamamoto K. Overexpression in Escherichia coli and purification of recombinant CI-b1, a Kunitz-type chymotrypsin inhibitor of silkworm. Protein Expression and Purification 2004, 38:9-16.
    • (2004) Protein Expression and Purification , vol.38 , pp. 9-16
    • He, N.1    Fujii, H.2    Kusakabe, T.3    Aso, Y.4    Banno, Y.5    Yamamoto, K.6
  • 37
    • 78650236051 scopus 로고    scopus 로고
    • Protease inhibitors and proteolytic signalling cascades in insects
    • Gubb D., Sanz-Parra A., Barcena L., Troxler L., Fullaondo A. Protease inhibitors and proteolytic signalling cascades in insects. Biochimie 2010, 92:1749-1759.
    • (2010) Biochimie , vol.92 , pp. 1749-1759
    • Gubb, D.1    Sanz-Parra, A.2    Barcena, L.3    Troxler, L.4    Fullaondo, A.5
  • 38
    • 79551646855 scopus 로고    scopus 로고
    • A Crassostrea gigas Toll-like receptor and comparative analysis of TLR pathway in invertebrates
    • Zhang L., Li L., Zhang G. A Crassostrea gigas Toll-like receptor and comparative analysis of TLR pathway in invertebrates. Fish & Shellfish Immunology 2011, 30:653-660.
    • (2011) Fish & Shellfish Immunology , vol.30 , pp. 653-660
    • Zhang, L.1    Li, L.2    Zhang, G.3
  • 39
    • 79952009250 scopus 로고    scopus 로고
    • A primitive Toll-like receptor signaling pathway in mollusk Zhikong scallop Chlamys farreri
    • Wang M., Yang J., Zhou Z., Qiu L., Wang L., Zhang H., et al. A primitive Toll-like receptor signaling pathway in mollusk Zhikong scallop Chlamys farreri. Developmental and Comparative Immunology 2011, 35:511-520.
    • (2011) Developmental and Comparative Immunology , vol.35 , pp. 511-520
    • Wang, M.1    Yang, J.2    Zhou, Z.3    Qiu, L.4    Wang, L.5    Zhang, H.6
  • 40
    • 77956933257 scopus 로고    scopus 로고
    • Peptidoglycan recognition protein of Chlamys farreri (CfPGRP-S1) mediates immune defenses against bacterial infection
    • Yang J., Wang W., Wei X., Qiu L., Wang L., Zhang H., et al. Peptidoglycan recognition protein of Chlamys farreri (CfPGRP-S1) mediates immune defenses against bacterial infection. Developmental and Comparative Immunology 2010, 34:1300-1307.
    • (2010) Developmental and Comparative Immunology , vol.34 , pp. 1300-1307
    • Yang, J.1    Wang, W.2    Wei, X.3    Qiu, L.4    Wang, L.5    Zhang, H.6
  • 41
    • 44049095738 scopus 로고    scopus 로고
    • A novel serine protease with clip domain from scallop Chlamys farreri
    • Zhu L., Song L., Mao Y., Zhao J., Li C., Xu W. A novel serine protease with clip domain from scallop Chlamys farreri. Molecular Biology Reports 2008, 35:257-264.
    • (2008) Molecular Biology Reports , vol.35 , pp. 257-264
    • Zhu, L.1    Song, L.2    Mao, Y.3    Zhao, J.4    Li, C.5    Xu, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.