메뉴 건너뛰기




Volumn 194, Issue 1, 2013, Pages 26-34

Cloning and characterization of a cathepsin L-like cysteine protease from Taenia pisiformis

Author keywords

Biochemical characteristics; Cysteine protease; Recombinant protein; Taenia pisiformis metacestode

Indexed keywords

BOVINE SERUM ALBUMIN; CATHEPSIN L LIKE CYSTEINE PROTEINASE; COMPLEMENTARY DNA; CYSTEINE PROTEINASE; FIBRONECTIN; IMMUNOGLOBULIN G; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; UNCLASSIFIED DRUG;

EID: 84876738606     PISSN: 03044017     EISSN: 18732550     Source Type: Journal    
DOI: 10.1016/j.vetpar.2012.12.055     Document Type: Article
Times cited : (7)

References (33)
  • 1
    • 35348932095 scopus 로고    scopus 로고
    • Cloning, site-directed mutagenesis and expression of cathepsin L-like cysteine protease from Uronema marinum (Ciliophora: Scuticociliatida)
    • Ahn S.J., Seo J.S., Kim M.S., Jeon S.J., Kim N.Y., Jang J.H., Kim K.H., Hong Y.K., Chung J.K., Lee H.H. Cloning, site-directed mutagenesis and expression of cathepsin L-like cysteine protease from Uronema marinum (Ciliophora: Scuticociliatida). Mol. Biochem. Parasitol. 2007, 156:191-198.
    • (2007) Mol. Biochem. Parasitol. , vol.156 , pp. 191-198
    • Ahn, S.J.1    Seo, J.S.2    Kim, M.S.3    Jeon, S.J.4    Kim, N.Y.5    Jang, J.H.6    Kim, K.H.7    Hong, Y.K.8    Chung, J.K.9    Lee, H.H.10
  • 2
    • 24644501763 scopus 로고    scopus 로고
    • Purification and characterization of a metacestode cysteine proteinase from Taenia solium involved in the breakdown of human IgG
    • Baig S., Damian R.T., Molinari J.L., Tato P., Morales-montor J., Welch M., Talhouk J., Hshmey R., White A.C. Purification and characterization of a metacestode cysteine proteinase from Taenia solium involved in the breakdown of human IgG. Parasitology 2005, 131:411-416.
    • (2005) Parasitology , vol.131 , pp. 411-416
    • Baig, S.1    Damian, R.T.2    Molinari, J.L.3    Tato, P.4    Morales-montor, J.5    Welch, M.6    Talhouk, J.7    Hshmey, R.8    White, A.C.9
  • 3
    • 0030900627 scopus 로고    scopus 로고
    • Proteinases secreted by Fasciola hepatica degrade extracellular matrix and basement membrane components
    • Berasain P., Goni F., McGonigle S., Dowd A., Dalton J.P., Frangione B., Carmona C. Proteinases secreted by Fasciola hepatica degrade extracellular matrix and basement membrane components. J. Parasitol. 1997, 83:1-5.
    • (1997) J. Parasitol. , vol.83 , pp. 1-5
    • Berasain, P.1    Goni, F.2    McGonigle, S.3    Dowd, A.4    Dalton, J.P.5    Frangione, B.6    Carmona, C.7
  • 4
    • 0033995763 scopus 로고    scopus 로고
    • Fasciola hepatica: parasite-secreted proteinases degrade all human IgG subclasses: determination of the specific cleavage sites and identification of the immunoglobulin fragments produced
    • Berasain P., Carmona C., Frangione B., Dalton J.P., Fernando G. Fasciola hepatica: parasite-secreted proteinases degrade all human IgG subclasses: determination of the specific cleavage sites and identification of the immunoglobulin fragments produced. Exp. Parasitol. 2000, 94:99-110.
    • (2000) Exp. Parasitol. , vol.94 , pp. 99-110
    • Berasain, P.1    Carmona, C.2    Frangione, B.3    Dalton, J.P.4    Fernando, G.5
  • 6
    • 59049087821 scopus 로고    scopus 로고
    • Cathepsin L-like genes of Trypanosoma vivax from Africa and South America - characterization, relationships and diagnostic implications
    • Cortez A.P., Rodrigues A.C., Garcia H.A., Neves L., Batista J.S., Bengaly Z., Paiva F., Teixeira M.M.G. Cathepsin L-like genes of Trypanosoma vivax from Africa and South America - characterization, relationships and diagnostic implications. Mol. Cell. Probes 2009, 23:44-51.
    • (2009) Mol. Cell. Probes , vol.23 , pp. 44-51
    • Cortez, A.P.1    Rodrigues, A.C.2    Garcia, H.A.3    Neves, L.4    Batista, J.S.5    Bengaly, Z.6    Paiva, F.7    Teixeira, M.M.G.8
  • 9
    • 2942538289 scopus 로고    scopus 로고
    • A gene family of cathepsin L-like proteases of filarial nematodes are associated with larval molting and cuticle and eggshell remodeling
    • Guiliano D.B., Hong X., McKerrow J.H., Blaxter M.L., Oksov Y., Liu J., Ghedin E., Lustigman S. A gene family of cathepsin L-like proteases of filarial nematodes are associated with larval molting and cuticle and eggshell remodeling. Mol. Biochem. Parasitol. 2004, 136:227-242.
    • (2004) Mol. Biochem. Parasitol. , vol.136 , pp. 227-242
    • Guiliano, D.B.1    Hong, X.2    McKerrow, J.H.3    Blaxter, M.L.4    Oksov, Y.5    Liu, J.6    Ghedin, E.7    Lustigman, S.8
  • 11
    • 0027394245 scopus 로고
    • Two distinct gene subfamilies within the family of cysteine protease genes
    • Karrer K.M., Peiffer S.L., DiTomas M.E. Two distinct gene subfamilies within the family of cysteine protease genes. Proc. Natl. Acad. Sci. U.S.A. 1993, 90:3063-3067.
    • (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
  • 12
    • 33644806733 scopus 로고    scopus 로고
    • Partial characterization of a 29kDa cysteine protease purified from Taenia solium metacestodes
    • Kim J.Y., Yang H.J., Kim K.S., Chung Y.B. Partial characterization of a 29kDa cysteine protease purified from Taenia solium metacestodes. Korean J. Parasitol. 2005, 43:157-160.
    • (2005) Korean J. Parasitol. , vol.43 , pp. 157-160
    • Kim, J.Y.1    Yang, H.J.2    Kim, K.S.3    Chung, Y.B.4
  • 13
    • 50049131642 scopus 로고    scopus 로고
    • Identification and characterization of a cathepsin L-like cysteine protease from Gnathostoma spinigerum
    • Kongkerda N., Uparanukrawb P., Morakote N., Sajid M., McKerrow J.H. Identification and characterization of a cathepsin L-like cysteine protease from Gnathostoma spinigerum. Mol. Biochem. Parasitol. 2008, 160:129-137.
    • (2008) Mol. Biochem. Parasitol. , vol.160 , pp. 129-137
    • Kongkerda, N.1    Uparanukrawb, P.2    Morakote, N.3    Sajid, M.4    McKerrow, J.H.5
  • 14
    • 37849185368 scopus 로고    scopus 로고
    • Leishmania aethiopica: identification and characterization of cathepsin L-like cysteine protease genes
    • Kuru T., Jirata D., Genetu A., Barr S., Mengistu Y., Aseffa A., Gedamu L. Leishmania aethiopica: identification and characterization of cathepsin L-like cysteine protease genes. Exp. Parasitol. 2007, 115:283-290.
    • (2007) Exp. Parasitol. , vol.115 , pp. 283-290
    • Kuru, T.1    Jirata, D.2    Genetu, A.3    Barr, S.4    Mengistu, Y.5    Aseffa, A.6    Gedamu, L.7
  • 16
    • 67649550455 scopus 로고    scopus 로고
    • Molecular cloning and analysis of stage and tissue-specific expression of cathepsin L-like protease from Clonorchis sinensis
    • Li Y.W., Hu X.C., Liu X.Q., Xu J., Hu F.Y., Ma C.L., Yu X.B. Molecular cloning and analysis of stage and tissue-specific expression of cathepsin L-like protease from Clonorchis sinensis. Parasitol. Res. 2009, 105:447-452.
    • (2009) Parasitol. Res. , vol.105 , pp. 447-452
    • Li, Y.W.1    Hu, X.C.2    Liu, X.Q.3    Xu, J.4    Hu, F.Y.5    Ma, C.L.6    Yu, X.B.7
  • 17
    • 8844224148 scopus 로고    scopus 로고
    • RNA interference targeting cathepsin L and Z-like cysteine proteases of Onchocerca volvulus confirmed their essential function during L3 molting
    • Lustigman S., Zhang J., Liu J., Oksov Y., Hashmi S. RNA interference targeting cathepsin L and Z-like cysteine proteases of Onchocerca volvulus confirmed their essential function during L3 molting. Mol. Biochem. Parasitol. 2004, 138:165-170.
    • (2004) Mol. Biochem. Parasitol. , vol.138 , pp. 165-170
    • Lustigman, S.1    Zhang, J.2    Liu, J.3    Oksov, Y.4    Hashmi, S.5
  • 18
    • 0034126426 scopus 로고    scopus 로고
    • Taenia solium: a cysteine protease secreted by metacestodes depletes human CD4 lymphocytes in vitro
    • Molinari J.L., Mejia H., White A.C., Garrido E., Borgonio V.M., Baig S., Tato P. Taenia solium: a cysteine protease secreted by metacestodes depletes human CD4 lymphocytes in vitro. Exp. Parasitol. 2000, 94:133-142.
    • (2000) Exp. Parasitol. , vol.94 , pp. 133-142
    • Molinari, J.L.1    Mejia, H.2    White, A.C.3    Garrido, E.4    Borgonio, V.M.5    Baig, S.6    Tato, P.7
  • 19
    • 76349108044 scopus 로고    scopus 로고
    • Cathepsin B- and L-like cysteine protease activities during the in vitro development of Hysterothylacium aduncum (Nematoda: Anisakidae), a worldwide fish parasite
    • Malagón D., Díaz-López M., Benítez R., Adroher F.J. Cathepsin B- and L-like cysteine protease activities during the in vitro development of Hysterothylacium aduncum (Nematoda: Anisakidae), a worldwide fish parasite. Parasitol. Int. 2010, 59:89-92.
    • (2010) Parasitol. Int. , vol.59 , pp. 89-92
    • Malagón, D.1    Díaz-López, M.2    Benítez, R.3    Adroher, F.J.4
  • 20
    • 33646347372 scopus 로고    scopus 로고
    • Critical roles for excretory-secretory cysteine proteases during tissue invasion of Paragonimus westermani newly excysted metacercariae
    • Na B.K., Kim S.H., Lee E.G., Kim T.S., Bae Y.A., Kang I., Yu J.R., Sohn W.M., Cho S.Y., Kong Y. Critical roles for excretory-secretory cysteine proteases during tissue invasion of Paragonimus westermani newly excysted metacercariae. Cell. Microbiol. 2006, 8:1034-1046.
    • (2006) Cell. Microbiol. , vol.8 , pp. 1034-1046
    • Na, B.K.1    Kim, S.H.2    Lee, E.G.3    Kim, T.S.4    Bae, Y.A.5    Kang, I.6    Yu, J.R.7    Sohn, W.M.8    Cho, S.Y.9    Kong, Y.10
  • 21
    • 71249083882 scopus 로고    scopus 로고
    • Genes of cathepsin L-like proteases in Trypanosoma rangeli isolates: markers for diagnosis, genotyping and phylogenetic relationships
    • Ortiz P.A., Maia da Silva F., Cortez A.P., Lima L., Campaner M., Pral E.M.F., Alfieri S.C., Teixeira M.M.G. Genes of cathepsin L-like proteases in Trypanosoma rangeli isolates: markers for diagnosis, genotyping and phylogenetic relationships. Acta Trop. 2009, 112:249-259.
    • (2009) Acta Trop. , vol.112 , pp. 249-259
    • Ortiz, P.A.1    Maia da Silva, F.2    Cortez, A.P.3    Lima, L.4    Campaner, M.5    Pral, E.M.F.6    Alfieri, S.C.7    Teixeira, M.M.G.8
  • 22
    • 0036121368 scopus 로고    scopus 로고
    • Fasciola hepatica cathepsin L suppresses sheep lymphocyte proliferation in vitro and modulates surfaceCD4 expression on human and ovine T cells
    • Prowse R.K., Chaplin P., Robinson H.C., Spithill T.W. Fasciola hepatica cathepsin L suppresses sheep lymphocyte proliferation in vitro and modulates surfaceCD4 expression on human and ovine T cells. Parasite Immunol. 2002, 24:57-66.
    • (2002) Parasite Immunol. , vol.24 , pp. 57-66
    • Prowse, R.K.1    Chaplin, P.2    Robinson, H.C.3    Spithill, T.W.4
  • 24
    • 38349025512 scopus 로고    scopus 로고
    • Molecular cloning and functional characterisation of a cathepsin L-like proteinase from the fish kinetoplastid parasite Trypanosoma carassii
    • Ruszczyk A., Forlenza M., Savelkoul H.F., Wiegertjes G.F. Molecular cloning and functional characterisation of a cathepsin L-like proteinase from the fish kinetoplastid parasite Trypanosoma carassii. Fish Shellfish Immun 2008, 24:205-214.
    • (2008) Fish Shellfish Immun , vol.24 , pp. 205-214
    • Ruszczyk, A.1    Forlenza, M.2    Savelkoul, H.F.3    Wiegertjes, G.F.4
  • 25
    • 0029945159 scopus 로고    scopus 로고
    • Extracellularmatrix degradation by Haemonchus contortus
    • Rhoads M.L., Fetterer R.H. Extracellularmatrix degradation by Haemonchus contortus. J. Parasitol. 1996, 82:379-383.
    • (1996) J. Parasitol. , vol.82 , pp. 379-383
    • Rhoads, M.L.1    Fetterer, R.H.2
  • 27
  • 28
    • 34447259277 scopus 로고    scopus 로고
    • Cloning and characterization of cathepsin L-like peptidases of Echinococcus multilocularis metacestodes
    • Sako Y., Yamasaki H., Nakaya K., Nakao M., Ito A. Cloning and characterization of cathepsin L-like peptidases of Echinococcus multilocularis metacestodes. Mol. Biochem. Parasitol. 2007, 154:181-189.
    • (2007) Mol. Biochem. Parasitol. , vol.154 , pp. 181-189
    • Sako, Y.1    Yamasaki, H.2    Nakaya, K.3    Nakao, M.4    Ito, A.5
  • 30
    • 0028905069 scopus 로고
    • Processing of the papain precursor. The ionization state of a conserved amino acid motif within the Pro region participates in the regulation of intramolecular processing
    • Vernet T., Berti P.J., deMC, Musil R., Tessier D.C., Ménard R., Magny M.C., Storer A.C., Thomas D.Y. Processing of the papain precursor. The ionization state of a conserved amino acid motif within the Pro region participates in the regulation of intramolecular processing. J. Biol. Chem. 1995, 270:10838-10846.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10838-10846
    • Vernet, T.1    Berti, P.J.2    de, M.C.3    Musil, R.4    Tessier, D.C.5    Ménard, R.6    Magny, M.C.7    Storer, A.C.8    Thomas, D.Y.9
  • 31
    • 0343852349 scopus 로고    scopus 로고
    • Characterization of a cysteine proteinase from Taenia crassiceps cysts
    • White A.C., Baig S., Chappell C.L. Characterization of a cysteine proteinase from Taenia crassiceps cysts. Mol. Biochem. Parasitol. 1997, 85:243-253.
    • (1997) Mol. Biochem. Parasitol. , vol.85 , pp. 243-253
    • White, A.C.1    Baig, S.2    Chappell, C.L.3
  • 32
    • 45849144337 scopus 로고    scopus 로고
    • Purification and characterization of a cathepsin L-like enzyme from the body wall of the sea cucumber Stichopus japonicus
    • Zhu B.W., Zhao L.L., Sun L.M., Li D.M., Murata Y., Yu L., Zhang L. Purification and characterization of a cathepsin L-like enzyme from the body wall of the sea cucumber Stichopus japonicus. Biosci. Biotechnol. Biochem. 2008, 72:1430-1437.
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , pp. 1430-1437
    • Zhu, B.W.1    Zhao, L.L.2    Sun, L.M.3    Li, D.M.4    Murata, Y.5    Yu, L.6    Zhang, L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.