메뉴 건너뛰기




Volumn 31, Issue 1, 2011, Pages 164-169

Molecular characterization and expression analysis of the channel catfish cathepsin D genes

Author keywords

Antimicrobial; Catfish; Cathepsin D; Infection; Innate immunity

Indexed keywords

BACTERIA (MICROORGANISMS); EDWARDSIELLA ICTALURI; ICTALURUS PUNCTATUS; TELEOSTEI; VERTEBRATA;

EID: 79957849169     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2011.04.006     Document Type: Article
Times cited : (38)

References (33)
  • 2
    • 0031883733 scopus 로고    scopus 로고
    • Lysosomes, a meeting point of proteins, chaperones, and proteases
    • Cuervo A.M., Dice J.F. Lysosomes, a meeting point of proteins, chaperones, and proteases. J Mol Med 1998, 76:6-12.
    • (1998) J Mol Med , vol.76 , pp. 6-12
    • Cuervo, A.M.1    Dice, J.F.2
  • 5
    • 0023209825 scopus 로고
    • Evolution in the structure and function of aspartic proteases
    • Tang J., Wong R.N. Evolution in the structure and function of aspartic proteases. J Cell Biochem 1987, 33:53-63.
    • (1987) J Cell Biochem , vol.33 , pp. 53-63
    • Tang, J.1    Wong, R.N.2
  • 6
    • 0023389657 scopus 로고
    • The role of aspartic and cysteine proteinases in albumin degradation by rat kidney cortical lysosomes
    • Baricos W.H., Zhou Y.W., Fuerst R.S., Barrett A.J., Shah S.V. The role of aspartic and cysteine proteinases in albumin degradation by rat kidney cortical lysosomes. Arch Biochem Biophys 1987, 256:687-691.
    • (1987) Arch Biochem Biophys , vol.256 , pp. 687-691
    • Baricos, W.H.1    Zhou, Y.W.2    Fuerst, R.S.3    Barrett, A.J.4    Shah, S.V.5
  • 7
    • 0016723595 scopus 로고
    • Direct evidence of importance of lysosomes in degradation of intracellular proteins
    • Dean R.T. Direct evidence of importance of lysosomes in degradation of intracellular proteins. Nature 1975, 257:414-416.
    • (1975) Nature , vol.257 , pp. 414-416
    • Dean, R.T.1
  • 8
    • 0027220451 scopus 로고
    • Mass spectrometric analysis of the fragments produced by cleavage and reduction of rat prolactin: evidence that the cleaving enzyme is cathepsin D
    • Baldocchi R.A., Tan L., King D.S., Nicoll C.S. Mass spectrometric analysis of the fragments produced by cleavage and reduction of rat prolactin: evidence that the cleaving enzyme is cathepsin D. Endocrinology 1993, 133:935-938.
    • (1993) Endocrinology , vol.133 , pp. 935-938
    • Baldocchi, R.A.1    Tan, L.2    King, D.S.3    Nicoll, C.S.4
  • 9
    • 0028094420 scopus 로고
    • Mouse cathepsin D gene: molecular organization, characterization of the promoter, and chromosomal localization
    • Hetman M., Perschl A., Saftig P., Von Figura K., Peters C. Mouse cathepsin D gene: molecular organization, characterization of the promoter, and chromosomal localization. DNA Cell Biol 1994, 13:419-427.
    • (1994) DNA Cell Biol , vol.13 , pp. 419-427
    • Hetman, M.1    Perschl, A.2    Saftig, P.3    Von Figura, K.4    Peters, C.5
  • 11
    • 0006155444 scopus 로고
    • Purification and characterization of a proteinase identified as cathepsin D from tilapia muscle (Tilapia nilotica × Tilapia aurea)
    • Jiang S.T., Wang Y.T., Chen C.S. Purification and characterization of a proteinase identified as cathepsin D from tilapia muscle (Tilapia nilotica × Tilapia aurea). J Agric Food Chem 1991, 39:1597-1601.
    • (1991) J Agric Food Chem , vol.39 , pp. 1597-1601
    • Jiang, S.T.1    Wang, Y.T.2    Chen, C.S.3
  • 12
    • 0030814882 scopus 로고    scopus 로고
    • Molecular characterisation of ovarian cathepsin D in the rainbow trout, Oncorhynchus mykiss
    • Brooks S., Tyler C.R., Carnevali O., Coward K., Sumpter J.P. Molecular characterisation of ovarian cathepsin D in the rainbow trout, Oncorhynchus mykiss. Gene 1997, 201:45-54.
    • (1997) Gene , vol.201 , pp. 45-54
    • Brooks, S.1    Tyler, C.R.2    Carnevali, O.3    Coward, K.4    Sumpter, J.P.5
  • 13
    • 0032963373 scopus 로고    scopus 로고
    • Cathepsin D from the liver of the antarctic icefish Chionodraco hamatus exhibits unusual activity and stability at high temperatures
    • Capasso C., Lees W.E., Capasso A., Scudiero R., Carginale V., Kille P., et al. Cathepsin D from the liver of the antarctic icefish Chionodraco hamatus exhibits unusual activity and stability at high temperatures. Biochim Biophys Acta 1999, 1431:64-73.
    • (1999) Biochim Biophys Acta , vol.1431 , pp. 64-73
    • Capasso, C.1    Lees, W.E.2    Capasso, A.3    Scudiero, R.4    Carginale, V.5    Kille, P.6
  • 14
    • 0032794641 scopus 로고    scopus 로고
    • Molecular cloning and expression of ovarian cathepsin D in seabream, Sparus aurata
    • Carnevali O., Centonze F., Brooks S., Marota I., Sumpter J.P. Molecular cloning and expression of ovarian cathepsin D in seabream, Sparus aurata. Biol Reprod 1999, 61:785-791.
    • (1999) Biol Reprod , vol.61 , pp. 785-791
    • Carnevali, O.1    Centonze, F.2    Brooks, S.3    Marota, I.4    Sumpter, J.P.5
  • 15
    • 0034736582 scopus 로고    scopus 로고
    • Sex- and tissue-specific expression of aspartic proteinases in Danio rerio (zebrafish)
    • Riggio M., Scudiero R., Filosa S., Parisi E. Sex- and tissue-specific expression of aspartic proteinases in Danio rerio (zebrafish). Gene 2000, 260:67-75.
    • (2000) Gene , vol.260 , pp. 67-75
    • Riggio, M.1    Scudiero, R.2    Filosa, S.3    Parisi, E.4
  • 16
    • 0035087731 scopus 로고    scopus 로고
    • The prognostic value of the expression of collagenase IV, cathepsin D and metallothionein in squamous cell carcinomas of the skin determined by immunohistochemistry
    • Goldmann T., Moorkamp A., Wiedorn K.H., Suter L., Otto F. The prognostic value of the expression of collagenase IV, cathepsin D and metallothionein in squamous cell carcinomas of the skin determined by immunohistochemistry. Arch Dermatol Res 2001, 293:115-120.
    • (2001) Arch Dermatol Res , vol.293 , pp. 115-120
    • Goldmann, T.1    Moorkamp, A.2    Wiedorn, K.H.3    Suter, L.4    Otto, F.5
  • 17
    • 0035132092 scopus 로고    scopus 로고
    • Purification and characterization of cathepsin D from herring muscle (Clupea harengus)
    • Nielsen L.B., Nielsen H.H. Purification and characterization of cathepsin D from herring muscle (Clupea harengus). Comp Biochem Physiol B Biochem Mol Biol 2001, 128:351-363.
    • (2001) Comp Biochem Physiol B Biochem Mol Biol , vol.128 , pp. 351-363
    • Nielsen, L.B.1    Nielsen, H.H.2
  • 18
    • 11144263603 scopus 로고    scopus 로고
    • Identification of pepsinogen gene in the genome of stomachless fish, Takifugu rubripes
    • Kurokawa T., Uji S., Suzuki T. Identification of pepsinogen gene in the genome of stomachless fish, Takifugu rubripes. Comp Biochem Physiol B Biochem Mol Biol 2005, 140:133-140.
    • (2005) Comp Biochem Physiol B Biochem Mol Biol , vol.140 , pp. 133-140
    • Kurokawa, T.1    Uji, S.2    Suzuki, T.3
  • 20
    • 64549088906 scopus 로고    scopus 로고
    • Molecular cloning, characterization and expression analysis of cathepsin D gene from turbot Scophthalmus maximus
    • Jia A., Zhang X.H. Molecular cloning, characterization and expression analysis of cathepsin D gene from turbot Scophthalmus maximus. Fish Shellfish Immunol 2009, 26:606-613.
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 606-613
    • Jia, A.1    Zhang, X.H.2
  • 21
    • 0036514179 scopus 로고    scopus 로고
    • Cathepsin D produces antimicrobial peptide parasin I from histone H2A in the skin mucosa of fish
    • Cho J.H., Park I.Y., Kim H.S., Lee W.T., Kim M.S., Kim S.C. Cathepsin D produces antimicrobial peptide parasin I from histone H2A in the skin mucosa of fish. FASEB J 2002, 16:429-431.
    • (2002) FASEB J , vol.16 , pp. 429-431
    • Cho, J.H.1    Park, I.Y.2    Kim, H.S.3    Lee, W.T.4    Kim, M.S.5    Kim, S.C.6
  • 22
    • 0024256915 scopus 로고
    • Aspartic proteinases in fishes and aquatic invertebrates
    • Gildberg A. Aspartic proteinases in fishes and aquatic invertebrates. Comp Biochem Physiol B 1988, 91:425-435.
    • (1988) Comp Biochem Physiol B , vol.91 , pp. 425-435
    • Gildberg, A.1
  • 23
    • 77349083472 scopus 로고    scopus 로고
    • Assembly of 500,000 inter-specific catfish expressed sequence tags and large scale gene-associated marker development for whole genome association studies
    • Wang S., Peatman E., Abernathy J., Waldbieser G., Lindquist E., Richardson P., et al. Assembly of 500,000 inter-specific catfish expressed sequence tags and large scale gene-associated marker development for whole genome association studies. Genome Biol 2010, 11:R8.
    • (2010) Genome Biol , vol.11
    • Wang, S.1    Peatman, E.2    Abernathy, J.3    Waldbieser, G.4    Lindquist, E.5    Richardson, P.6
  • 24
    • 73249124822 scopus 로고    scopus 로고
    • Structure and expression of transferrin gene of channel catfish, Ictalurus punctatus
    • Liu H., Takano T., Abernathy J., Wang S., Sha Z., Jiang Y., et al. Structure and expression of transferrin gene of channel catfish, Ictalurus punctatus. Fish Shellfish Immunol 2010, 28:159-166.
    • (2010) Fish Shellfish Immunol , vol.28 , pp. 159-166
    • Liu, H.1    Takano, T.2    Abernathy, J.3    Wang, S.4    Sha, Z.5    Jiang, Y.6
  • 25
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 1987, 162:156-159.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 27
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR
    • Pfaffl M.W., Horgan G.W., Dempfle L. Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR. Nucleic Acids Res 2002, 30:e36.
    • (2002) Nucleic Acids Res , vol.30
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3
  • 28
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • Tamura K., Dudley J., Nei M., Kumar S. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol Biol Evol 2007, 24:1596-1599.
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 29
    • 77955354748 scopus 로고    scopus 로고
    • Identification and characterization of full-length cDNAs in channel catfish (Ictalurus punctatus) and blue catfish (Ictalurus furcatus)
    • Chen F., Lee Y., Jiang Y., Wang S., Peatman E., Abernathy J., et al. Identification and characterization of full-length cDNAs in channel catfish (Ictalurus punctatus) and blue catfish (Ictalurus furcatus). PLoS One 2010, 5:e11546.
    • (2010) PLoS One , vol.5
    • Chen, F.1    Lee, Y.2    Jiang, Y.3    Wang, S.4    Peatman, E.5    Abernathy, J.6
  • 31
    • 0242558200 scopus 로고    scopus 로고
    • Genome duplication, subfunction partitioning, and lineage divergence: Sox9 in stickleback and zebrafish
    • Cresko W.A., Yan Y.L., Baltrus D.A., Amores A., Singer A., Rodriguez-Mari A., et al. Genome duplication, subfunction partitioning, and lineage divergence: Sox9 in stickleback and zebrafish. Dev Dyn 2003, 228:480-489.
    • (2003) Dev Dyn , vol.228 , pp. 480-489
    • Cresko, W.A.1    Yan, Y.L.2    Baltrus, D.A.3    Amores, A.4    Singer, A.5    Rodriguez-Mari, A.6
  • 32
    • 79551618369 scopus 로고    scopus 로고
    • Cathepsin-d, a key protease in breast cancer, is up-regulated in obese mouse and human adipose tissue, and controls adipogenesis
    • Masson O., Prebois C., Derocq D., Meulle A., Dray C., Daviaud D., et al. Cathepsin-d, a key protease in breast cancer, is up-regulated in obese mouse and human adipose tissue, and controls adipogenesis. PLoS One 2011, 6:e16452.
    • (2011) PLoS One , vol.6
    • Masson, O.1    Prebois, C.2    Derocq, D.3    Meulle, A.4    Dray, C.5    Daviaud, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.