메뉴 건너뛰기




Volumn 160, Issue 1-2, 2009, Pages 180-183

Characterization of an intracellular cystatin homolog from the tick Haemaphysalis longicornis

Author keywords

Cystatin; Haemaphysalis longicornis; Inhibitory activity

Indexed keywords

CATHEPSIN B; CATHEPSIN L; COMPLEMENTARY DNA; CYSTATIN; PAPAIN;

EID: 59649083646     PISSN: 03044017     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.vetpar.2008.10.086     Document Type: Article
Times cited : (37)

References (21)
  • 1
    • 0030053568 scopus 로고    scopus 로고
    • A cysteine protease inhibitor stored in the large granules of horseshoe crab hemocytes: purification, characterization, cDNA cloning, and tissue localization
    • Agarwala K.L., Kawabata S., Hirata M., Miyagi M., Tsunasawa S., and Iwanaga S. A cysteine protease inhibitor stored in the large granules of horseshoe crab hemocytes: purification, characterization, cDNA cloning, and tissue localization. J. Biochem. 119 (1996) 85-94
    • (1996) J. Biochem. , vol.119 , pp. 85-94
    • Agarwala, K.L.1    Kawabata, S.2    Hirata, M.3    Miyagi, M.4    Tsunasawa, S.5    Iwanaga, S.6
  • 2
    • 0036015245 scopus 로고    scopus 로고
    • Comparison of differentially expressed genes in the salivary glands of male ticks, Amblyomma americanum and Dermacentor andersoni
    • Bior A.D., Essenberg R.C., and Sauer J.R. Comparison of differentially expressed genes in the salivary glands of male ticks, Amblyomma americanum and Dermacentor andersoni. Insect Biochem. Mol. Biol. 32 (2002) 645-655
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 645-655
    • Bior, A.D.1    Essenberg, R.C.2    Sauer, J.R.3
  • 3
    • 0029776802 scopus 로고    scopus 로고
    • The importance of the second hairpin loop of cystatin C for proteinase binding. Characterization of the interaction of Trp-106 variants of the inhibitor with cysteine proteinases
    • Bjork I., Brieditis I., Raub-Segall E., Pol E., Hakansson K., and Abrahamson M. The importance of the second hairpin loop of cystatin C for proteinase binding. Characterization of the interaction of Trp-106 variants of the inhibitor with cysteine proteinases. Biochemistry 35 (1996) 10720-10726
    • (1996) Biochemistry , vol.35 , pp. 10720-10726
    • Bjork, I.1    Brieditis, I.2    Raub-Segall, E.3    Pol, E.4    Hakansson, K.5    Abrahamson, M.6
  • 4
    • 0031013054 scopus 로고    scopus 로고
    • Friends and relations of the cystatin superfamily-new members and their evolution
    • Brown W.M., and Dziegielewska K.M. Friends and relations of the cystatin superfamily-new members and their evolution. Protein Sci. 6 (1997) 5-12
    • (1997) Protein Sci. , vol.6 , pp. 5-12
    • Brown, W.M.1    Dziegielewska, K.M.2
  • 5
    • 0035190790 scopus 로고    scopus 로고
    • Nippocystatin, a cysteine protease inhibitor from Nippostrongylus brasiliensis, inhibits antigen processing and modulates antigen-specific immune response
    • Dainichi T., Maekawa Y., Ishii K., Zhang T., Nashed B.F., Sakai T., Takashima M., and Himeno K. Nippocystatin, a cysteine protease inhibitor from Nippostrongylus brasiliensis, inhibits antigen processing and modulates antigen-specific immune response. Infect. Immun. 69 (2001) 7380-7386
    • (2001) Infect. Immun. , vol.69 , pp. 7380-7386
    • Dainichi, T.1    Maekawa, Y.2    Ishii, K.3    Zhang, T.4    Nashed, B.F.5    Sakai, T.6    Takashima, M.7    Himeno, K.8
  • 6
    • 0017943792 scopus 로고
    • Development of acquired resistance and precipitating antibody in rabbits experimentally infested with females of Haemaphysalis longicornis (Ixodoidea: Ixodidae)
    • Fujisaki K. Development of acquired resistance and precipitating antibody in rabbits experimentally infested with females of Haemaphysalis longicornis (Ixodoidea: Ixodidae). Natl. Inst. Anim. Health Quart. (Tokyo) 18 (1978) 27-38
    • (1978) Natl. Inst. Anim. Health Quart. (Tokyo) , vol.18 , pp. 27-38
    • Fujisaki, K.1
  • 7
    • 0028366341 scopus 로고
    • The taxonomy of the bovine Theileria spp.
    • Fujisaki K., Kawazu S., and Kamio T. The taxonomy of the bovine Theileria spp. Parasitol. Today 10 (1994) 31-33
    • (1994) Parasitol. Today , vol.10 , pp. 31-33
    • Fujisaki, K.1    Kawazu, S.2    Kamio, T.3
  • 8
    • 33751538306 scopus 로고    scopus 로고
    • Two secreted cystatins of the soft tick Ornithodoros moubata: differential expression pattern and inhibitory specificity
    • Grunclova L., Horn M., Vancova M., Sojka D., Franta Z., Mares M., and Kopacek P. Two secreted cystatins of the soft tick Ornithodoros moubata: differential expression pattern and inhibitory specificity. Biol. Chem. 387 (2006) 1635-1644
    • (2006) Biol. Chem. , vol.387 , pp. 1635-1644
    • Grunclova, L.1    Horn, M.2    Vancova, M.3    Sojka, D.4    Franta, Z.5    Mares, M.6    Kopacek, P.7
  • 9
    • 16844371922 scopus 로고    scopus 로고
    • The global importance of ticks
    • Jongejan F., and Uilenberg G. The global importance of ticks. Parasitology 129 (2004) S3-S14
    • (2004) Parasitology , vol.129
    • Jongejan, F.1    Uilenberg, G.2
  • 10
    • 23044433357 scopus 로고    scopus 로고
    • RNAi-mediated gene silencing to assess the role of synaptobrevin and cystatin in tick blood feeding
    • Karim S., Miller N.J., Valenzuela J., Sauer J.R., and Mather T.N. RNAi-mediated gene silencing to assess the role of synaptobrevin and cystatin in tick blood feeding. Biochem. Biophys. Res. Commun. 334 (2005) 1336-1342
    • (2005) Biochem. Biophys. Res. Commun. , vol.334 , pp. 1336-1342
    • Karim, S.1    Miller, N.J.2    Valenzuela, J.3    Sauer, J.R.4    Mather, T.N.5
  • 11
    • 35748942888 scopus 로고    scopus 로고
    • Selective cysteine protease inhibition contributes to blood-feeding success of the tick Ixodes scapularis
    • Kotsyfakis M., Karim S., Andersen J.F., Mather T.N., and Ribeiro J.M. Selective cysteine protease inhibition contributes to blood-feeding success of the tick Ixodes scapularis. J. Biol. Chem. 282 (2007) 29256-29263
    • (2007) J. Biol. Chem. , vol.282 , pp. 29256-29263
    • Kotsyfakis, M.1    Karim, S.2    Andersen, J.F.3    Mather, T.N.4    Ribeiro, J.M.5
  • 12
    • 33748746599 scopus 로고    scopus 로고
    • Anti-inflammatory and immunosuppressive activity of sialostatin L, a salivary cystatin from the tick Ixodes scapularis
    • Kotsyfakis M., Sa-Nunes A., Francischetti I.M., Mather T.N., Andersen J.F., and Ribeiro J.M. Anti-inflammatory and immunosuppressive activity of sialostatin L, a salivary cystatin from the tick Ixodes scapularis. J. Biol. Chem. 281 (2006) 26298-26307
    • (2006) J. Biol. Chem. , vol.281 , pp. 26298-26307
    • Kotsyfakis, M.1    Sa-Nunes, A.2    Francischetti, I.M.3    Mather, T.N.4    Andersen, J.F.5    Ribeiro, J.M.6
  • 13
    • 33745746366 scopus 로고    scopus 로고
    • Bmcystatin, a cysteine proteinase inhibitor characterized from the tick Boophilus microplus
    • Lima C.A., Sasaki S.D., and Tanaka A.S. Bmcystatin, a cysteine proteinase inhibitor characterized from the tick Boophilus microplus. Biochem. Biophys. Res. Commun. 347 (2006) 44-50
    • (2006) Biochem. Biophys. Res. Commun. , vol.347 , pp. 44-50
    • Lima, C.A.1    Sasaki, S.D.2    Tanaka, A.S.3
  • 14
    • 0035916803 scopus 로고    scopus 로고
    • Bm-CPI-2, a cystatin homolog secreted by the filarial parasite Brugia malayi, inhibits class II MHC-restricted antigen processing
    • Manoury B., Gregory W.F., Maizels R.M., and Watts C. Bm-CPI-2, a cystatin homolog secreted by the filarial parasite Brugia malayi, inhibits class II MHC-restricted antigen processing. Curr. Biol. 11 (2001) 447-451
    • (2001) Curr. Biol. , vol.11 , pp. 447-451
    • Manoury, B.1    Gregory, W.F.2    Maizels, R.M.3    Watts, C.4
  • 15
    • 0033781718 scopus 로고    scopus 로고
    • Issues in tick vaccine development: identification and characterization of potential candidate vaccine antigens
    • Mulenga A., Sugimoto C., and Onuma M. Issues in tick vaccine development: identification and characterization of potential candidate vaccine antigens. Microbes Infect. 2 (2000) 1353-1361
    • (2000) Microbes Infect. , vol.2 , pp. 1353-1361
    • Mulenga, A.1    Sugimoto, C.2    Onuma, M.3
  • 16
    • 0025022426 scopus 로고
    • Evolution of proteins of the cystatin superfamily
    • Rawlings N.D., and Barrett A.J. Evolution of proteins of the cystatin superfamily. J. Mol. Evol. 30 (1990) 60-71
    • (1990) J. Mol. Evol. , vol.30 , pp. 60-71
    • Rawlings, N.D.1    Barrett, A.J.2
  • 18
    • 0025817602 scopus 로고
    • The cystatins: protein inhibitors of cysteine proteinases
    • Turk V., and Bode W. The cystatins: protein inhibitors of cysteine proteinases. Fed. Eur. Biol. Soc. Lett. 285 (1991) 213-219
    • (1991) Fed. Eur. Biol. Soc. Lett. , vol.285 , pp. 213-219
    • Turk, V.1    Bode, W.2
  • 19
    • 0033210951 scopus 로고    scopus 로고
    • Purification and characterization of Bombyx cysteine proteinase specific inhibitors from the hemolymph of Bombyx mori
    • Yamamoto Y., Watabe S., Kageyama T., and Takahashi S. Purification and characterization of Bombyx cysteine proteinase specific inhibitors from the hemolymph of Bombyx mori. Arch. Insect Biochem. Physiol. 41 (1999) 119-129
    • (1999) Arch. Insect Biochem. Physiol. , vol.41 , pp. 119-129
    • Yamamoto, Y.1    Watabe, S.2    Kageyama, T.3    Takahashi, S.4
  • 20
    • 34249669650 scopus 로고    scopus 로고
    • Sequence characterization and expression patterns of two defensin-like antimicrobial peptides from the tick Haemaphysalis longicornis
    • Zhou J., Liao M., Ueda M., Gong H., Xuan X., and Fujisaki K. Sequence characterization and expression patterns of two defensin-like antimicrobial peptides from the tick Haemaphysalis longicornis. Peptides 28 (2007) 1304-1310
    • (2007) Peptides , vol.28 , pp. 1304-1310
    • Zhou, J.1    Liao, M.2    Ueda, M.3    Gong, H.4    Xuan, X.5    Fujisaki, K.6
  • 21
    • 33745713839 scopus 로고    scopus 로고
    • A secreted cystatin from the tick Haemaphysalis longicornis and its distinct expression patterns in relation to innate immunity
    • Zhou J., Ueda M., Umemiya R., Battsetseg B., Boldbaatar D., Xuan X., and Fujisaki K. A secreted cystatin from the tick Haemaphysalis longicornis and its distinct expression patterns in relation to innate immunity. Insect Biochem. Mol. Biol. 36 (2006) 527-535
    • (2006) Insect Biochem. Mol. Biol. , vol.36 , pp. 527-535
    • Zhou, J.1    Ueda, M.2    Umemiya, R.3    Battsetseg, B.4    Boldbaatar, D.5    Xuan, X.6    Fujisaki, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.