메뉴 건너뛰기




Volumn 26, Issue 2, 2009, Pages 332-338

Channel catfish, Ictalurus punctatus, cysteine proteinases: Cloning, characterisation and expression of cathepsin H and L

Author keywords

Cathepsin H; Cathepsin L; Channel catfish; CTSH; CTSL; Ictalurus punctatus

Indexed keywords

EDWARDSIELLA ICTALURI; ICTALURUS PUNCTATUS;

EID: 60649107590     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2008.11.010     Document Type: Article
Times cited : (39)

References (36)
  • 1
    • 0023162530 scopus 로고
    • T-cell recognition of lysozyme: the biochemical basis of presentation
    • Allen P.M., Babbitt B.P., and Unanue E.R. T-cell recognition of lysozyme: the biochemical basis of presentation. Immunol Rev 98 (1987) 171-187
    • (1987) Immunol Rev , vol.98 , pp. 171-187
    • Allen, P.M.1    Babbitt, B.P.2    Unanue, E.R.3
  • 2
    • 0025315557 scopus 로고
    • The relationship between antigen concentration, antigen internalization, and antigenic complexes: modeling insights into antigen processing and presentation
    • Singer D.F., and Linderman J.J. The relationship between antigen concentration, antigen internalization, and antigenic complexes: modeling insights into antigen processing and presentation. J Cell Biol 111 (1990) 55-68
    • (1990) J Cell Biol , vol.111 , pp. 55-68
    • Singer, D.F.1    Linderman, J.J.2
  • 3
    • 0023067325 scopus 로고
    • Biophysical aspects of antigen recognition by T cells
    • Watts T.H., and McConnell H.M. Biophysical aspects of antigen recognition by T cells. Annu Rev Immunol 5 (1987) 461-475
    • (1987) Annu Rev Immunol , vol.5 , pp. 461-475
    • Watts, T.H.1    McConnell, H.M.2
  • 4
    • 26244445000 scopus 로고    scopus 로고
    • The lysosomal cysteine proteases in MHC class II antigen presentation
    • Hsing L.C., and Rudensky A.Y. The lysosomal cysteine proteases in MHC class II antigen presentation. Immunol Rev 207 (2005) 229-241
    • (2005) Immunol Rev , vol.207 , pp. 229-241
    • Hsing, L.C.1    Rudensky, A.Y.2
  • 5
    • 0037805704 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases regulate antigen presentation
    • Honey K., and Rudensky A.Y. Lysosomal cysteine proteases regulate antigen presentation. Nat Rev Immunol 3 (2003) 472-482
    • (2003) Nat Rev Immunol , vol.3 , pp. 472-482
    • Honey, K.1    Rudensky, A.Y.2
  • 6
    • 38649111363 scopus 로고    scopus 로고
    • Cysteine cathepsins: cellular roadmap to different functions
    • Brix K., Dunkhorst A., Mayer K., and Jordans S. Cysteine cathepsins: cellular roadmap to different functions. Biochimie 90 (2008) 194-207
    • (2008) Biochimie , vol.90 , pp. 194-207
    • Brix, K.1    Dunkhorst, A.2    Mayer, K.3    Jordans, S.4
  • 7
    • 34249893895 scopus 로고    scopus 로고
    • Protease signaling in cell death: caspases versus cysteine cathepsins
    • Turk B., and Stoka V. Protease signaling in cell death: caspases versus cysteine cathepsins. FEBS Lett 581 (2007) 2761-2767
    • (2007) FEBS Lett , vol.581 , pp. 2761-2767
    • Turk, B.1    Stoka, V.2
  • 8
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: facts and opportunities
    • Turk V., Turk B., and Turk D. Lysosomal cysteine proteases: facts and opportunities. EMBO J 20 (2001) 4629-4633
    • (2001) EMBO J , vol.20 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 9
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: more than scavengers
    • Turk B., Turk D., and Turk V. Lysosomal cysteine proteases: more than scavengers. Biochim Biophys Acta 1477 (2000) 98-111
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 98-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 10
    • 38749105868 scopus 로고    scopus 로고
    • The MEROPS batch BLAST: a tool to detect peptidases and their non-peptidase homologues in a genome
    • Rawlings N.D., and Morton F.R. The MEROPS batch BLAST: a tool to detect peptidases and their non-peptidase homologues in a genome. Biochimie 90 (2008) 243-259
    • (2008) Biochimie , vol.90 , pp. 243-259
    • Rawlings, N.D.1    Morton, F.R.2
  • 11
    • 0032540474 scopus 로고    scopus 로고
    • Critical role in Ii degradation and CD4 T cell selection in the thymus
    • Nakagawa T., Roth W., Wong P., Nelson A., Farr A., Deussing J., et al. Critical role in Ii degradation and CD4 T cell selection in the thymus. Science 280 (1998) 450-453
    • (1998) Science , vol.280 , pp. 450-453
    • Nakagawa, T.1    Roth, W.2    Wong, P.3    Nelson, A.4    Farr, A.5    Deussing, J.6
  • 14
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran K., Sullivan N.J., Felbor U., Whelan S.P., and Cunningham J.M. Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 308 (2005) 1643-1645
    • (2005) Science , vol.308 , pp. 1643-1645
    • Chandran, K.1    Sullivan, N.J.2    Felbor, U.3    Whelan, S.P.4    Cunningham, J.M.5
  • 15
    • 0017088422 scopus 로고
    • Intracellular protein breakdown: VII. Cathepsin L and H; two new proteinases from rat liver lysosomes
    • Kirschke H., Langner J., Wiederanders B., Ansorge S., Bohley P., and Broghammer U. Intracellular protein breakdown: VII. Cathepsin L and H; two new proteinases from rat liver lysosomes. Acta Biol Med Ger 35 (1976) 285-299
    • (1976) Acta Biol Med Ger , vol.35 , pp. 285-299
    • Kirschke, H.1    Langner, J.2    Wiederanders, B.3    Ansorge, S.4    Bohley, P.5    Broghammer, U.6
  • 16
    • 0037215592 scopus 로고    scopus 로고
    • Cysteine protease activity is required for surfactant protein B processing and lamellar body genesis
    • Guttentag S., Robinson L., Zhang P., Brasch F., Bühling F., and Beers M. Cysteine protease activity is required for surfactant protein B processing and lamellar body genesis. Am J Respir Cell Mol Biol 28 (2003) 69-79
    • (2003) Am J Respir Cell Mol Biol , vol.28 , pp. 69-79
    • Guttentag, S.1    Robinson, L.2    Zhang, P.3    Brasch, F.4    Bühling, F.5    Beers, M.6
  • 17
    • 34547609892 scopus 로고    scopus 로고
    • Cathepsin H is an Fgf10 target involved in Bmp4 degradation during lung branching morphogenesis
    • Lü J., Qian J., Keppler D., and Cardoso W.V. Cathepsin H is an Fgf10 target involved in Bmp4 degradation during lung branching morphogenesis. J Biol Chem 282 (2007) 22176-22184
    • (2007) J Biol Chem , vol.282 , pp. 22176-22184
    • Lü, J.1    Qian, J.2    Keppler, D.3    Cardoso, W.V.4
  • 18
    • 56149124011 scopus 로고    scopus 로고
    • Molecular cloning, sequencing and characterisation of channel catfish (Ictalurus punctatus, Rafinesque 1818) cathepsin S gene
    • Yeh H.-Y., and Klesius P.H. Molecular cloning, sequencing and characterisation of channel catfish (Ictalurus punctatus, Rafinesque 1818) cathepsin S gene. Vet Immunol Immunopathol 126 (2008) 382-387
    • (2008) Vet Immunol Immunopathol , vol.126 , pp. 382-387
    • Yeh, H.-Y.1    Klesius, P.H.2
  • 20
    • 41549140969 scopus 로고    scopus 로고
    • Complete structure, genomic organization, and expression of channel catfish (Ictalurus punctatus, Rafinesque 1818) matrix metalloproteinase-9 gene
    • Yeh H.-Y., and Klesius P.H. Complete structure, genomic organization, and expression of channel catfish (Ictalurus punctatus, Rafinesque 1818) matrix metalloproteinase-9 gene. Biosci Biotechnol Biochem 72 (2008) 702-714
    • (2008) Biosci Biotechnol Biochem , vol.72 , pp. 702-714
    • Yeh, H.-Y.1    Klesius, P.H.2
  • 21
    • 38549130374 scopus 로고    scopus 로고
    • Channel catfish, Ictalurus punctatus, cyclophilin A and B cDNA characterisation and expression analysis
    • Yeh H.-Y., and Klesius P.H. Channel catfish, Ictalurus punctatus, cyclophilin A and B cDNA characterisation and expression analysis. Vet Immunol Immunopathol 121 (2008) 370-377
    • (2008) Vet Immunol Immunopathol , vol.121 , pp. 370-377
    • Yeh, H.-Y.1    Klesius, P.H.2
  • 22
    • 0031978181 scopus 로고    scopus 로고
    • Base-calling of automated sequencer traces using phred. II. Error probabilities
    • Ewing B., and Green P. Base-calling of automated sequencer traces using phred. II. Error probabilities. Genome Res 8 (1998) 186-194
    • (1998) Genome Res , vol.8 , pp. 186-194
    • Ewing, B.1    Green, P.2
  • 23
    • 0031955518 scopus 로고    scopus 로고
    • Base-calling of automated sequencer traces using phred. I. Accuracy assessment
    • Ewing B., Hillier L., Wendl M.C., and Green P. Base-calling of automated sequencer traces using phred. I. Accuracy assessment. Genome Res 8 (1998) 175-185
    • (1998) Genome Res , vol.8 , pp. 175-185
    • Ewing, B.1    Hillier, L.2    Wendl, M.C.3    Green, P.4
  • 24
    • 8844230989 scopus 로고    scopus 로고
    • LUCY (2): an interactive DNA sequence quality trimming and vector removal tool
    • Li S., and Chou H.-H. LUCY (2): an interactive DNA sequence quality trimming and vector removal tool. Bioinformatics 20 (2004) 2865-2866
    • (2004) Bioinformatics , vol.20 , pp. 2865-2866
    • Li, S.1    Chou, H.-H.2
  • 25
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: the European molecular biology open software suite
    • Rice P., Longden I., and Bleasby A. EMBOSS: the European molecular biology open software suite. Trends Genet 16 (2000) 276-277
    • (2000) Trends Genet , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 27
  • 29
    • 0024212067 scopus 로고
    • Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer
    • Frohman M.A., Dush M.K., and Martin G.R. Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer. Proc Natl Acad Sci U S A 85 (1988) 8998-9002
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 30
    • 0026630108 scopus 로고
    • Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease
    • Shi G.-P., Munger J.S., Meara J.P., Rich D.H., and Chapman H.A. Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease. J Biol Chem 267 (1992) 7258-7262
    • (1992) J Biol Chem , vol.267 , pp. 7258-7262
    • Shi, G.-P.1    Munger, J.S.2    Meara, J.P.3    Rich, D.H.4    Chapman, H.A.5
  • 31
    • 0029902382 scopus 로고    scopus 로고
    • Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment
    • Coulombe R., Grochulski P., Sivaraman J., Ménard R., Mort J.S., and Cygler M. Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment. EMBO J 15 (1996) 5492-5503
    • (1996) EMBO J , vol.15 , pp. 5492-5503
    • Coulombe, R.1    Grochulski, P.2    Sivaraman, J.3    Ménard, R.4    Mort, J.S.5    Cygler, M.6
  • 32
    • 0032518496 scopus 로고    scopus 로고
    • Crystal structure of porcine cathepsin H determined at 2.1 Å resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function
    • Gunčar G., Podobnik M., Pungerčar J., Štrukelj B., Turk V., and Turk D. Crystal structure of porcine cathepsin H determined at 2.1 Å resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function. Structure 6 (1998) 51-61
    • (1998) Structure , vol.6 , pp. 51-61
    • Gunčar, G.1    Podobnik, M.2    Pungerčar, J.3    Štrukelj, B.4    Turk, V.5    Turk, D.6
  • 33
    • 33845565360 scopus 로고    scopus 로고
    • Phylogenetic relationships and gene expression pattern of three different cathepsin L (Ctsl) isoforms in zebrafish: ctsla is the putative yolk processing enzyme
    • Tingaud-Sequeira A., and Cerda J. Phylogenetic relationships and gene expression pattern of three different cathepsin L (Ctsl) isoforms in zebrafish: ctsla is the putative yolk processing enzyme. Gene 386 (2007) 98-106
    • (2007) Gene , vol.386 , pp. 98-106
    • Tingaud-Sequeira, A.1    Cerda, J.2
  • 34
    • 0027394245 scopus 로고
    • Two distinct gene subfamilies within the family of cysteine protease genes
    • Karrer K.M., Peiffer S.L., and DiTomas M.E. Two distinct gene subfamilies within the family of cysteine protease genes. Proc Natl Acad Sci U S A 90 (1993) 3063-3067
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 3063-3067
    • Karrer, K.M.1    Peiffer, S.L.2    DiTomas, M.E.3
  • 35
    • 0021875579 scopus 로고
    • Distribution of cathepsins B and H in rat tissues and peripheral blood cells
    • Kominami E., Tsukahara T., Bando Y., and Katunuma N. Distribution of cathepsins B and H in rat tissues and peripheral blood cells. J Biochem 98 (1985) 87-93
    • (1985) J Biochem , vol.98 , pp. 87-93
    • Kominami, E.1    Tsukahara, T.2    Bando, Y.3    Katunuma, N.4
  • 36
    • 0028936712 scopus 로고
    • IFN-γ increases cathepsin H mRNA levels in mouse macrophages
    • Lafuse W.P., Brown D., Castle L., and Zwilling B.S. IFN-γ increases cathepsin H mRNA levels in mouse macrophages. J Leukoc Biol 57 (1995) 663-669
    • (1995) J Leukoc Biol , vol.57 , pp. 663-669
    • Lafuse, W.P.1    Brown, D.2    Castle, L.3    Zwilling, B.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.