메뉴 건너뛰기




Volumn 34, Issue 2, 2010, Pages 168-176

A clip domain serine proteinase plays a role in antibacterial defense but is not required for prophenoloxidase activation in shrimp

Author keywords

Clip domain serine proteinase; Penaeus monodon; Prophenoloxidase; RNA interference; Shrimp immunity; Vibrio harveyi

Indexed keywords

DOUBLE STRANDED RNA; GREEN FLUORESCENT PROTEIN; MONOPHENOL MONOOXYGENASE; OXYGENASE; PROPHENOL OXIDASE; SERINE PROTEINASE; UNCLASSIFIED DRUG;

EID: 70450273342     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2009.09.004     Document Type: Article
Times cited : (40)

References (38)
  • 1
    • 0033141885 scopus 로고    scopus 로고
    • Invertebrate immunity
    • Söderhäll K. Invertebrate immunity. Dev Comp Immunol 23 (1999) 263-266
    • (1999) Dev Comp Immunol , vol.23 , pp. 263-266
    • Söderhäll, K.1
  • 2
    • 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 (2005) 128-150
    • (2005) J Biochem Mol Biol , vol.38 , pp. 128-150
    • Iwanaga, S.1    Lee, B.L.2
  • 3
    • 0036076660 scopus 로고    scopus 로고
    • Early events in crustacean innate immunity
    • Lee S.Y., and Söderhäll K. Early events in crustacean innate immunity. Fish Shellfish Immunol 12 (2002) 421-437
    • (2002) Fish Shellfish Immunol , vol.12 , pp. 421-437
    • Lee, S.Y.1    Söderhäll, K.2
  • 4
    • 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
  • 5
    • 0025606964 scopus 로고
    • Proclotting enzyme from horseshoe crab hemocytes: cDNA cloning, disulfide locations, and subcellular localisation
    • Muta T., Hashimoto R., Miyata T., Nishimura H., Toh Y., and Iwanaga S. Proclotting enzyme from horseshoe crab hemocytes: cDNA cloning, disulfide locations, and subcellular localisation. J Biol Chem 265 (1990) 22426-22433
    • (1990) J Biol Chem , vol.265 , pp. 22426-22433
    • Muta, T.1    Hashimoto, R.2    Miyata, T.3    Nishimura, H.4    Toh, Y.5    Iwanaga, S.6
  • 6
    • 40549103093 scopus 로고    scopus 로고
    • CLIP-domain serine proteases in Drosophila innate immunity
    • Jang I.H., Nam H.J., and Lee W.J. CLIP-domain serine proteases in Drosophila innate immunity. BMB Rep 41 (2008) 102-107
    • (2008) BMB Rep , vol.41 , pp. 102-107
    • Jang, I.H.1    Nam, H.J.2    Lee, W.J.3
  • 7
    • 0033953792 scopus 로고    scopus 로고
    • The clip-domain family of serine proteinases in arthropods
    • Jiang H., and Kanost M.R. The clip-domain family of serine proteinases in arthropods. Insect Biochem Mol Biol 30 (2000) 95-105
    • (2000) Insect Biochem Mol Biol , vol.30 , pp. 95-105
    • Jiang, H.1    Kanost, M.R.2
  • 8
    • 64549105261 scopus 로고    scopus 로고
    • Gene silencing of a prophenoloxidase activating enzyme in the shrimp, Penaeus monodon, increases susceptibility to Vibrio harveyi infection
    • Charoensapsri W., Amparyup P., Hirono I., Aoki T., and Tassanakajon A. Gene silencing of a prophenoloxidase activating enzyme in the shrimp, Penaeus monodon, increases susceptibility to Vibrio harveyi infection. Dev Comp Immunol 33 (2009) 811-820
    • (2009) Dev Comp Immunol , vol.33 , pp. 811-820
    • Charoensapsri, W.1    Amparyup, P.2    Hirono, I.3    Aoki, T.4    Tassanakajon, A.5
  • 9
    • 0037472685 scopus 로고    scopus 로고
    • Serine proteases and their homologs in the Drosophila melanogaster genome: an initial analysis of sequence conservation and phylogenetic relationships
    • Ross J., Jiang H., Kanost M.R., and Wang Y. Serine proteases and their homologs in the Drosophila melanogaster genome: an initial analysis of sequence conservation and phylogenetic relationships. Gene 304 (2003) 117-131
    • (2003) Gene , vol.304 , pp. 117-131
    • Ross, J.1    Jiang, H.2    Kanost, M.R.3    Wang, Y.4
  • 10
    • 0029167738 scopus 로고
    • Masquerade: a novel secreted serine protease-like molecule is required for somatic muscle attachment in the Drosophila embryo
    • Murugasu-Oei B., Rodrigues V., Yang X., and Jang C.W. Masquerade: a novel secreted serine protease-like molecule is required for somatic muscle attachment in the Drosophila embryo. Genes Dev 9 (1995) 139-154
    • (1995) Genes Dev , vol.9 , pp. 139-154
    • Murugasu-Oei, B.1    Rodrigues, V.2    Yang, X.3    Jang, C.W.4
  • 11
    • 0031934614 scopus 로고    scopus 로고
    • New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structures and functions
    • Iwanaga S., Kawabata S., and Muta T. New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structures and functions. J Biochem (Tokyo) 123 (1998) 1-15
    • (1998) J Biochem (Tokyo) , vol.123 , pp. 1-15
    • Iwanaga, S.1    Kawabata, S.2    Muta, T.3
  • 12
    • 0027394999 scopus 로고
    • The limulus clotting reaction
    • Iwanaga S. The limulus clotting reaction. Curr Opin Immunol 5 (1993) 74-82
    • (1993) Curr Opin Immunol , vol.5 , pp. 74-82
    • Iwanaga, S.1
  • 13
    • 0000929276 scopus 로고    scopus 로고
    • The clotting cascade and defense molecules found in the hemolymph of the horseshoe crab
    • Söderhäll K., Iwanaga S., and Vasta G.R. (Eds), SOS Publications, Fair Haven
    • Kawabata S.I., Muta T., and Iwanaga S. The clotting cascade and defense molecules found in the hemolymph of the horseshoe crab. In: Söderhäll K., Iwanaga S., and Vasta G.R. (Eds). New Directions in Invertebrate Immunology (1996), SOS Publications, Fair Haven 255-283
    • (1996) New Directions in Invertebrate Immunology , pp. 255-283
    • Kawabata, S.I.1    Muta, T.2    Iwanaga, S.3
  • 14
    • 0029928757 scopus 로고    scopus 로고
    • The role of hemolymph coagulation in innate immunity
    • Muta T., and Iwanaga S. The role of hemolymph coagulation in innate immunity. Curr Opin Immunol 8 (1996) 41-47
    • (1996) Curr Opin Immunol , vol.8 , pp. 41-47
    • Muta, T.1    Iwanaga, S.2
  • 15
    • 0037134532 scopus 로고    scopus 로고
    • Duplicated binding sites for (1 → 3)-beta-d-glucan in the horseshoe crab coagulation factor G: implications for a molecular basis of the pattern recognition in innate immunity
    • Takaki Y., Seki N., Kawabata S., Iwanaga S., and Muta T. Duplicated binding sites for (1 → 3)-beta-d-glucan in the horseshoe crab coagulation factor G: implications for a molecular basis of the pattern recognition in innate immunity. J Biol Chem 277 (2002) 14281-14287
    • (2002) J Biol Chem , vol.277 , pp. 14281-14287
    • Takaki, Y.1    Seki, N.2    Kawabata, S.3    Iwanaga, S.4    Muta, T.5
  • 16
    • 0033973826 scopus 로고    scopus 로고
    • Signaling mechanisms in the antimicrobial host defense of Drosophila
    • Imler J.L., and Hoffmann J.A. Signaling mechanisms in the antimicrobial host defense of Drosophila. Curr Opin Microbiol 3 (2000) 16-22
    • (2000) Curr Opin Microbiol , vol.3 , pp. 16-22
    • Imler, J.L.1    Hoffmann, J.A.2
  • 17
    • 0032005367 scopus 로고    scopus 로고
    • Role of the prophenoloxidase activating system in invertebrate immunity
    • Söderhäll K., and Cerenius L. Role of the prophenoloxidase activating system in invertebrate immunity. Curr Opin Immunol 10 (1998) 23-28
    • (1998) Curr Opin Immunol , vol.10 , pp. 23-28
    • Söderhäll, K.1    Cerenius, L.2
  • 18
    • 33746284239 scopus 로고    scopus 로고
    • Cloning and characterization of a shrimp clip domain serine protease homolog (c-SPH) as a cell adhesion molecule
    • Lin C.Y., Hu K.Y., Ho S.H., and Song Y.L. Cloning and characterization of a shrimp clip domain serine protease homolog (c-SPH) as a cell adhesion molecule. Dev Comp Immunol 30 (2006) 1132-1144
    • (2006) Dev Comp Immunol , vol.30 , pp. 1132-1144
    • Lin, C.Y.1    Hu, K.Y.2    Ho, S.H.3    Song, Y.L.4
  • 19
    • 33846706752 scopus 로고    scopus 로고
    • Molecular cloning, characterization and expression of a masquerade-like serine proteinase homologue from black tiger shrimp Penaeus monodon
    • Amparyup P., Jitvaropas R., Pulsook N., and Tassanakajon A. Molecular cloning, characterization and expression of a masquerade-like serine proteinase homologue from black tiger shrimp Penaeus monodon. Fish Shellfish Immunol 22 (2007) 535-546
    • (2007) Fish Shellfish Immunol , vol.22 , pp. 535-546
    • Amparyup, P.1    Jitvaropas, R.2    Pulsook, N.3    Tassanakajon, A.4
  • 20
    • 35348831700 scopus 로고    scopus 로고
    • Characterization of a shrimp serine protease homolog, a binding protein of yellow head virus
    • Sriphaijit T., Flegel T.W., and Senapin S. Characterization of a shrimp serine protease homolog, a binding protein of yellow head virus. Dev Comp Immunol 31 (2007) 1145-1158
    • (2007) Dev Comp Immunol , vol.31 , pp. 1145-1158
    • Sriphaijit, T.1    Flegel, T.W.2    Senapin, S.3
  • 21
    • 67349103442 scopus 로고    scopus 로고
    • Clip domain serine protease and its homolog respond to Vibrio challenge in Chinese white shrimp, Fenneropenaeus chinensis
    • Ren Q., Xu Z.L., Wang X.W., Zhao X.F., and Wang J.X. Clip domain serine protease and its homolog respond to Vibrio challenge in Chinese white shrimp, Fenneropenaeus chinensis. Fish Shellfish Immunol 26 (2009) 787-798
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 787-798
    • Ren, Q.1    Xu, Z.L.2    Wang, X.W.3    Zhao, X.F.4    Wang, J.X.5
  • 22
    • 4644280167 scopus 로고    scopus 로고
    • Peptidoglycan inducible expression of a serine proteinase homologue from kuruma shrimp (Marsupenaeus japonicus)
    • Rattanachai A., Hirono I., Ohira T., Takahashi Y., and Aoki T. Peptidoglycan inducible expression of a serine proteinase homologue from kuruma shrimp (Marsupenaeus japonicus). Fish Shellfish Immunol 18 (2005) 39-48
    • (2005) Fish Shellfish Immunol , vol.18 , pp. 39-48
    • Rattanachai, A.1    Hirono, I.2    Ohira, T.3    Takahashi, Y.4    Aoki, T.5
  • 23
    • 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
  • 25
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl M.W. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 29 (2001) 2004-2007
    • (2001) Nucleic Acids Res , vol.29 , pp. 2004-2007
    • Pfaffl, M.W.1
  • 26
    • 84954358612 scopus 로고    scopus 로고
    • Two prophenoloxidases are important for the survival of Vibrio harveyi challenged shrimp Penaeus monodon
    • Amparyup P., Charoensapsri W., and Tassanakajon A. Two prophenoloxidases are important for the survival of Vibrio harveyi challenged shrimp Penaeus monodon. Dev Comp Immunol 33 (2009) 247-256
    • (2009) Dev Comp Immunol , vol.33 , pp. 247-256
    • Amparyup, P.1    Charoensapsri, W.2    Tassanakajon, A.3
  • 27
    • 0033771124 scopus 로고    scopus 로고
    • A masquerade-like serine proteinase homologue is necessary for phenoloxidase activity in the coleopteran insect, Holotrichia diomphalia larvae
    • Kwon T.H., Kim M.S., Choi H.W., Joo C.H., Cho M.Y., and Lee B.L. A masquerade-like serine proteinase homologue is necessary for phenoloxidase activity in the coleopteran insect, Holotrichia diomphalia larvae. Eur J Biochem 267 (2000) 6188-6196
    • (2000) Eur J Biochem , vol.267 , pp. 6188-6196
    • Kwon, T.H.1    Kim, M.S.2    Choi, H.W.3    Joo, C.H.4    Cho, M.Y.5    Lee, B.L.6
  • 28
    • 0035059407 scopus 로고    scopus 로고
    • Properties of the prophenoloxidase activating enzyme of the freshwater crayfish Pacifastacus leniusculus
    • Wang R., Lee S.Y., Cerenius L., and Söderhäll K. Properties of the prophenoloxidase activating enzyme of the freshwater crayfish Pacifastacus leniusculus. Eur J Biochem 268 (2001) 895-902
    • (2001) Eur J Biochem , vol.268 , pp. 895-902
    • Wang, R.1    Lee, S.Y.2    Cerenius, L.3    Söderhäll, K.4
  • 29
    • 67349234897 scopus 로고    scopus 로고
    • Functional characterization of a masquerade-like serine proteinase homologue from the black tiger shrimp Penaeus monodon
    • Jitvaropas R., Amparyup P., Gross P.S., and Tassanakajon A. Functional characterization of a masquerade-like serine proteinase homologue from the black tiger shrimp Penaeus monodon. Comp Biochem Physiol B 153 (2009) 236-243
    • (2009) Comp Biochem Physiol B , vol.153 , pp. 236-243
    • Jitvaropas, R.1    Amparyup, P.2    Gross, P.S.3    Tassanakajon, A.4
  • 30
    • 0027479821 scopus 로고
    • Evolutionary families of peptidases
    • Rawlings N.D., and Barrett A.J. Evolutionary families of peptidases. Biochem J 290 (1993) 205-218
    • (1993) Biochem J , vol.290 , pp. 205-218
    • Rawlings, N.D.1    Barrett, A.J.2
  • 31
    • 33747777740 scopus 로고    scopus 로고
    • Gene silencing of serine proteases affects melanization of Sephadex beads in Anopheles gambiae
    • Paskewitz S.M., Andreev O., and Shi L. Gene silencing of serine proteases affects melanization of Sephadex beads in Anopheles gambiae. Insect Biochem Mol Biol 36 (2006) 701-711
    • (2006) Insect Biochem Mol Biol , vol.36 , pp. 701-711
    • Paskewitz, S.M.1    Andreev, O.2    Shi, L.3
  • 32
    • 0000533788 scopus 로고    scopus 로고
    • Molecular cloning of cDNA for prophenol-oxidase-activating factor I, a serine protease is induced by lipopolysaccharide or 1,3-b-glucan in coleopteran insect, Holotrichia diomphalia larvae
    • Lee S.Y., Cho M.Y., Hyun J.H., Lee K.M., Homma K.I., Natori S., et al. Molecular cloning of cDNA for prophenol-oxidase-activating factor I, a serine protease is induced by lipopolysaccharide or 1,3-b-glucan in coleopteran insect, Holotrichia diomphalia larvae. Eur J Biochem 257 (1998) 615-621
    • (1998) Eur J Biochem , vol.257 , pp. 615-621
    • Lee, S.Y.1    Cho, M.Y.2    Hyun, J.H.3    Lee, K.M.4    Homma, K.I.5    Natori, S.6
  • 33
    • 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 (2006) 213-236
    • (2006) Immunobiology , vol.211 , pp. 213-236
    • Jiravanichpaisal, P.1    Lee, B.L.2    Söderhäll, K.3
  • 34
    • 0037083557 scopus 로고    scopus 로고
    • Cutting edge: the toll pathway is required for resistance to Gram-positive bacterial infections in Drosophila
    • Rutschmann S., Kilinc A., and Ferrandon D. Cutting edge: the toll pathway is required for resistance to Gram-positive bacterial infections in Drosophila. J Immunol 168 (2002) 1542-1546
    • (2002) J Immunol , vol.168 , pp. 1542-1546
    • Rutschmann, S.1    Kilinc, A.2    Ferrandon, D.3
  • 35
    • 43149121130 scopus 로고    scopus 로고
    • A Three-step proteolytic cascade mediates the activation of the peptidoglycan-induced toll pathway in an insect
    • Kim C.H., Kim S.J., Kan H., Kwon H.M., Roh K.B., Jiang R., et al. A Three-step proteolytic cascade mediates the activation of the peptidoglycan-induced toll pathway in an insect. J Biol Chem 283 (2008) 7599-7607
    • (2008) J Biol Chem , vol.283 , pp. 7599-7607
    • Kim, C.H.1    Kim, S.J.2    Kan, H.3    Kwon, H.M.4    Roh, K.B.5    Jiang, R.6
  • 36
    • 54449085542 scopus 로고    scopus 로고
    • Molecular control of phenoloxidase-induced melanin synthesis in an insect
    • Kan H., Kim C.H., Kwon H.M., Park J.W., Roh K.B., Lee H., et al. Molecular control of phenoloxidase-induced melanin synthesis in an insect. J Biol Chem 283 (2008) 25316-25323
    • (2008) J Biol Chem , vol.283 , pp. 25316-25323
    • Kan, H.1    Kim, C.H.2    Kwon, H.M.3    Park, J.W.4    Roh, K.B.5    Lee, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.