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      Manila clam, Ruditapes philippinarum Cathepsin D: Molecular analysis and immune response against brown ring disease causing Vibrio tapetis challenge

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      https://www.riss.kr/link?id=A104099052

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      다국어 초록 (Multilingual Abstract)

      Cathepsins are lysosomal /cysteine proteases belong to papain family (C1 family) that is involved in intracellular protein degradation, antigen processing, hormone maturation, and immune responses. In this study, member of cathepsin family was identified from Manila clam (Mc-Cathepsin D) and investigated the immune response against brown ring disease (BRD) causing Vibrio tapetis challenge. The identified Mc-Cathepsin D gene encodes characteristic features typical for the cathepsin family including eukaryotic and viral aspartyl protease signature domain and two highly conserved active sites (84VVFDTGSSNLWV95 and 270IADTGTSLLAG281). Moreover, MC-Cathepsin D shows higher identity values (-50-70%) and conserved amino acids with known cathepsin D members. Transcriptional results (by quantitative real-time RT-PCR) showed that Mc-Cathepsin D was expressed at higher levels in gills and hemocytes than mantle, adductor muscle, foot, and siphon. After the V. tapetis challenge under laboratory conditions, Mc-Cathepsin D mRNA was up-regulated in gills and hemocytes. Present study indicates that Mc-Cathepsin D is constitutively expressed in different tissues and potentially inducible when infecting BRD by V. tapetis. It is further suggesting that Mc-Cathepsin D may be involved in multiple role including immune response reactions against BRD.
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      Cathepsins are lysosomal /cysteine proteases belong to papain family (C1 family) that is involved in intracellular protein degradation, antigen processing, hormone maturation, and immune responses. In this study, member of cathepsin family was identif...

      Cathepsins are lysosomal /cysteine proteases belong to papain family (C1 family) that is involved in intracellular protein degradation, antigen processing, hormone maturation, and immune responses. In this study, member of cathepsin family was identified from Manila clam (Mc-Cathepsin D) and investigated the immune response against brown ring disease (BRD) causing Vibrio tapetis challenge. The identified Mc-Cathepsin D gene encodes characteristic features typical for the cathepsin family including eukaryotic and viral aspartyl protease signature domain and two highly conserved active sites (84VVFDTGSSNLWV95 and 270IADTGTSLLAG281). Moreover, MC-Cathepsin D shows higher identity values (-50-70%) and conserved amino acids with known cathepsin D members. Transcriptional results (by quantitative real-time RT-PCR) showed that Mc-Cathepsin D was expressed at higher levels in gills and hemocytes than mantle, adductor muscle, foot, and siphon. After the V. tapetis challenge under laboratory conditions, Mc-Cathepsin D mRNA was up-regulated in gills and hemocytes. Present study indicates that Mc-Cathepsin D is constitutively expressed in different tissues and potentially inducible when infecting BRD by V. tapetis. It is further suggesting that Mc-Cathepsin D may be involved in multiple role including immune response reactions against BRD.

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      참고문헌 (Reference)

      1 Borrego, J. J., "Vibrio tapetis sp. nov., the causative agent of the brown ring disease affecting cultured clams" 46 : 480-484, 1996

      2 Hsing, L.C., "The lysosomal cysteine proteases in MHC class II antigen presentation" 207 : 229-241, 2005

      3 Paillard, C., "The brown ring disease in the Manila clam, Ruditapes philippinarum. Ultrastructural alterations of the periostracal lamina" 65 : 91-100, 1995

      4 Paillard, C., "The brown ring disease in manila clam, Ruditapes philippinarum: establishment of a classification system" 19 : 137-146, 1994

      5 Park K. I., "Report on the occurrence of brown ring disease (BRD) in Manila clam, Ruditapes philippinarum, on the west coast of Korea" 255 : 610-613, 2006

      6 Allam, B., "Pathogenicity of Vibrio tapetis, the etiological agent of brown ring disease in clams" 48 : 221-231, 2002

      7 Jia, A., "Molecular cloning, characterization and expression analysis of cathepsin D from turbot Scophthalmus maximus" 26 : 606-613, 2009

      8 Maa, J., "Molecular characterization and expression analysis of cathepsin L1 cysteine protease from pearl oyster Pinctada fucata" 29 : 501-507, 2010

      9 Nair, S. V., "Microarray analysis of coelomocyte gene expression in response to LPS in the sea urchin. Identification of unexpected immune diversity in an invertebrate" 22 : 33-47, 2005

      10 Kumar, S., "MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment" 5 : 150-163, 2004

      1 Borrego, J. J., "Vibrio tapetis sp. nov., the causative agent of the brown ring disease affecting cultured clams" 46 : 480-484, 1996

      2 Hsing, L.C., "The lysosomal cysteine proteases in MHC class II antigen presentation" 207 : 229-241, 2005

      3 Paillard, C., "The brown ring disease in the Manila clam, Ruditapes philippinarum. Ultrastructural alterations of the periostracal lamina" 65 : 91-100, 1995

      4 Paillard, C., "The brown ring disease in manila clam, Ruditapes philippinarum: establishment of a classification system" 19 : 137-146, 1994

      5 Park K. I., "Report on the occurrence of brown ring disease (BRD) in Manila clam, Ruditapes philippinarum, on the west coast of Korea" 255 : 610-613, 2006

      6 Allam, B., "Pathogenicity of Vibrio tapetis, the etiological agent of brown ring disease in clams" 48 : 221-231, 2002

      7 Jia, A., "Molecular cloning, characterization and expression analysis of cathepsin D from turbot Scophthalmus maximus" 26 : 606-613, 2009

      8 Maa, J., "Molecular characterization and expression analysis of cathepsin L1 cysteine protease from pearl oyster Pinctada fucata" 29 : 501-507, 2010

      9 Nair, S. V., "Microarray analysis of coelomocyte gene expression in response to LPS in the sea urchin. Identification of unexpected immune diversity in an invertebrate" 22 : 33-47, 2005

      10 Kumar, S., "MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment" 5 : 150-163, 2004

      11 Bond, J.S., "Intracellularproteases. Annual Review of Biochemistry" 56 : 333-364, 1987

      12 Dixit, A. K., "Immunodiagnostic/protective role of Cathepsin L cysteine proteinases secreted by Fasciola species" 154 : 177-184, 2008

      13 Lee, Y., "Immune response-related gene expression profile of a novel molluscan IκB protein member from manila clam (Ruditapes philippinarum)" 40 : 1519-1527, 2013

      14 Lecaille, F., "Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design" 102 : 4459-4488, 2002

      15 Zhang, F. T., "Expressional induction of Paralichthys olivaceus cathepsin B gene in response to virus, poly I:C and lipopolysaccharide" 25 : 542-549, 2008

      16 Bühling, F., "Expression of cathepsins B, H,K,L and S during human fetal lung development" 225 : 14-21, 2002

      17 Paillard, C., "Etiologie de la maladie de l'anneau brunchez Tapes philippinarum: pathogenicité d'un Vibrio sp" 310 : 15-20, 1990

      18 Park, K.I., "Epizootiology of Perkinsus sp. found in the Manila clam, Ruditapes philippinarum in Komsoe Bay, Korea" 32 : 303-309, 1999

      19 Paillard, C., "Effect of temperature on defense parameters in manila clam Ruditapes philippinarum challenged with Vibrio tapetis" 59 : 249-262, 2004

      20 Yasothornsrikul, S., "Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter" 100 : 9590-9595, 2003

      21 Thompson, J. D., "CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice" 22 : 4673-4680, 1994

      22 Park, K.I., "Application of enzyme-linked immunosorbent assay for studying of reproduction in the Manila clam Ruditapes philippinarum (Mollusca: Bivalvia): I. Quantifying eggs" 241 : 667-687, 2004

      23 Livak, K.J., "Analysis of relative gene expression data using real time quantitative PCR and the 2??CT method" 25 : 402-408, 2001

      24 FAO, "2012 World review of fisheries and aquaculture"

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      기준연도 WOS-KCI 통합IF(2년) KCIF(2년) KCIF(3년)
      2016 0.33 0.33 0.34
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