메뉴 건너뛰기




Volumn 157, Issue 4, 2010, Pages 326-335

Vitellin- and hemoglobin-digesting enzymes in Rhipicephalus (Boophilus) microplus larvae and females

Author keywords

Aspartic endopeptidase BYC; BmCL1; Cysteine endopeptidase; Hemoglobin; Rhipicephalus (Boophilus) microplus; RmLCE; Tick; Vitellin

Indexed keywords

ASPARTIC PROTEINASE; BOOPHILUS MICROPLUS CATHEPSIN L1; CATHEPSIN L; CYSTEINE PROTEINASE; HEMOGLOBIN; HEMOGLOBIN DEGRADING CYSTEINE ENDOPEPTIDASE; RHIPICEPHALUS MICROPLUS LARVAL CYSTEINE ENDOPEPTIDASE; UNCLASSIFIED DRUG; VITELLIN; VITELLIN DEGRADING CYSTEINE ENDOPEPTIDASE;

EID: 77957907223     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2010.08.002     Document Type: Article
Times cited : (30)

References (42)
  • 1
    • 34547532754 scopus 로고    scopus 로고
    • Characterization of asparaginyl endopeptidase, legumain induced by blood feeding in the ixodid tick Haemaphysalis longicornis
    • Abdul Alim M., Tsuji N., Miyoshi T., Khyrul I.M., Huang X., Motobu M., Fujisaki K. Characterization of asparaginyl endopeptidase, legumain induced by blood feeding in the ixodid tick Haemaphysalis longicornis. Insect Biochem. Mol. Biol. 2007, 37:911-922.
    • (2007) Insect Biochem. Mol. Biol. , vol.37 , pp. 911-922
    • Abdul, A.M.1    Tsuji, N.2    Miyoshi, T.3    Khyrul, I.M.4    Huang, X.5    Motobu, M.6    Fujisaki, K.7
  • 3
    • 0033166924 scopus 로고    scopus 로고
    • A missing metabolic pathway in the cattle tick Boophilus microplus
    • Braz G.R., Coelho H.S., Masuda H., Oliveira P.L. A missing metabolic pathway in the cattle tick Boophilus microplus. Curr. Biol. 1999, 9:703-706.
    • (1999) Curr. Biol. , vol.9 , pp. 703-706
    • Braz, G.R.1    Coelho, H.S.2    Masuda, H.3    Oliveira, P.L.4
  • 5
    • 0033532165 scopus 로고    scopus 로고
    • Mosquito cathepsin B-like protease involved in embryonic degradation of vitellinVt is produced as a latent extraovarian precursor
    • Cho W.L., Tsao S.M., Hays A.R., Walter R., Chen J.S., Snigirevskaya E.S., Raikhel A.S. Mosquito cathepsin B-like protease involved in embryonic degradation of vitellinVt is produced as a latent extraovarian precursor. J. Biol. Chem. 1999, 274:13311-13321.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13311-13321
    • Cho, W.L.1    Tsao, S.M.2    Hays, A.R.3    Walter, R.4    Chen, J.S.5    Snigirevskaya, E.S.6    Raikhel, A.S.7
  • 8
    • 35648963593 scopus 로고    scopus 로고
    • A cysteine endopeptidase from tick (Rhipicephalus (Boophilus) microplus) larvae with Vt digestion activity
    • Estrela A., Seixas A., Termignoni C. A cysteine endopeptidase from tick (Rhipicephalus (Boophilus) microplus) larvae with Vt digestion activity. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 2007, 148:410-416.
    • (2007) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.148 , pp. 410-416
    • Estrela, A.1    Seixas, A.2    Termignoni, C.3
  • 9
    • 0025527484 scopus 로고
    • Yolk degradation in tick eggs: I. Occurrence of a cathepsin L- like acid proteinase in yolk spheres
    • Fagotto F. Yolk degradation in tick eggs: I. Occurrence of a cathepsin L- like acid proteinase in yolk spheres. Arch. Insect Biochem. Physiol. 1990, 14:217-235.
    • (1990) Arch. Insect Biochem. Physiol. , vol.14 , pp. 217-235
    • Fagotto, F.1
  • 10
    • 0025529201 scopus 로고
    • Yolk degradation in tick eggs: II. Evidence that cathepsin L- like proteinase is stored as a latent, acid-activable proenzyme
    • Fagotto F. Yolk degradation in tick eggs: II. Evidence that cathepsin L- like proteinase is stored as a latent, acid-activable proenzyme. Arch. Insect Biochem. Physiol. 1990, 14:237-252.
    • (1990) Arch. Insect Biochem. Physiol. , vol.14 , pp. 237-252
    • Fagotto, F.1
  • 11
    • 0029583839 scopus 로고
    • Regulation of yolk degradation, or how to make sleepy lysosomes
    • Fagotto F. Regulation of yolk degradation, or how to make sleepy lysosomes. J. Cell Sci. 1995, 108:3645-3647.
    • (1995) J. Cell Sci. , vol.108 , pp. 3645-3647
    • Fagotto, F.1
  • 12
    • 35649020124 scopus 로고
    • Embryonic development
    • Plenum Press, New York, C. Gillott (Ed.)
    • Gillott C. Embryonic development. Entomology 1980, 537-562. Plenum Press, New York. C. Gillott (Ed.).
    • (1980) Entomology , pp. 537-562
    • Gillott, C.1
  • 13
    • 0020983841 scopus 로고
    • Blood digestion in Ornithodorus moubata Murray sensu stricto Walton females (Ixodoidea: Argasidae): II. Modifications of midgut cells related to the digestive cycle and to the triggering action of mating
    • Grandjean O. Blood digestion in Ornithodorus moubata Murray sensu stricto Walton females (Ixodoidea: Argasidae): II. Modifications of midgut cells related to the digestive cycle and to the triggering action of mating. Ann. Parasitol. Hum. Comp. 1983, 58:493-514.
    • (1983) Ann. Parasitol. Hum. Comp. , vol.58 , pp. 493-514
    • Grandjean, O.1
  • 15
    • 16844371922 scopus 로고    scopus 로고
    • The global importance of ticks
    • S3-14
    • Jongejan F., Uilenberg G. The global importance of ticks. Parasitology 2004, 129(Suppl:S3-14):S3-S14.
    • (2004) Parasitology , vol.129 , Issue.SUPPL.
    • Jongejan, F.1    Uilenberg, G.2
  • 16
    • 0025059406 scopus 로고
    • Purification and characterization of a cysteine proteinase from silkworm eggs
    • Kageyama T., Takahashi S.Y. Purification and characterization of a cysteine proteinase from silkworm eggs. Eur. J. Biochem. 1990, 193:203-210.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 203-210
    • Kageyama, T.1    Takahashi, S.Y.2
  • 17
    • 25144490692 scopus 로고    scopus 로고
    • Tracing heme in a living cell: hemoglobin degradation and heme traffic in digest cells of the cattle tick Boophilus microplus
    • Lara F.A., Lins U., Bechara G.H., Oliveira P.L. Tracing heme in a living cell: hemoglobin degradation and heme traffic in digest cells of the cattle tick Boophilus microplus. J. Exp. Biol. 2005, 208:3093-3101.
    • (2005) J. Exp. Biol. , vol.208 , pp. 3093-3101
    • Lara, F.A.1    Lins, U.2    Bechara, G.H.3    Oliveira, P.L.4
  • 19
    • 0030479499 scopus 로고    scopus 로고
    • A cysteine protease that processes insect vitellin. Purification and partial characterization of the enzyme and the proenzyme
    • Liu X., McCarron R.C., Nordin J.H. A cysteine protease that processes insect vitellin. Purification and partial characterization of the enzyme and the proenzyme. J. Biol. Chem. 1996, 271:33344-33351.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33344-33351
    • Liu, X.1    McCarron, R.C.2    Nordin, J.H.3
  • 22
    • 0023938526 scopus 로고
    • Drosophila cathepsin B-like proteinase: a suggested role in yolk degradation
    • Medina M., Leon P., Vallejo C.G. Drosophila cathepsin B-like proteinase: a suggested role in yolk degradation. Arch. Biochem. Biophys. 1988, 263:355-363.
    • (1988) Arch. Biochem. Biophys. , vol.263 , pp. 355-363
    • Medina, M.1    Leon, P.2    Vallejo, C.G.3
  • 23
    • 0029966482 scopus 로고    scopus 로고
    • Boophilus microplus: multiple proteolytic activities in the midgut
    • Mendiola J., Alonso M., Marquetti M.C., Finlay C. Boophilus microplus: multiple proteolytic activities in the midgut. Exp. Parasitol. 1996, 82:27-33.
    • (1996) Exp. Parasitol. , vol.82 , pp. 27-33
    • Mendiola, J.1    Alonso, M.2    Marquetti, M.C.3    Finlay, C.4
  • 25
    • 0033962771 scopus 로고    scopus 로고
    • A comparative survey of the hydrolytic enzymes of ectoparasitic and free-living mites
    • Nisbet A.J., Billingsley P.F. A comparative survey of the hydrolytic enzymes of ectoparasitic and free-living mites. Int. J. Parasitol. 2000, 30:19-27.
    • (2000) Int. J. Parasitol. , vol.30 , pp. 19-27
    • Nisbet, A.J.1    Billingsley, P.F.2
  • 26
    • 0035846971 scopus 로고    scopus 로고
    • Substrate specificity of human cathepsin D using internally quenched fluorescent peptides derived from reactive site loop of kallistatin
    • Pimenta D.C., Oliveira A., Juliano M.A., Juliano L. Substrate specificity of human cathepsin D using internally quenched fluorescent peptides derived from reactive site loop of kallistatin. Biochim. Biophys. Acta 2001, 1544:113-122.
    • (2001) Biochim. Biophys. Acta , vol.1544 , pp. 113-122
    • Pimenta, D.C.1    Oliveira, A.2    Juliano, M.A.3    Juliano, L.4
  • 27
    • 75549091468 scopus 로고    scopus 로고
    • MEROPS: the peptidase database. Nucleic Acids Res. 38 (Database issue)
    • Rawlings, N.D., Barrett, A.J., Bateman, A., 2010. MEROPS: the peptidase database. Nucleic Acids Res. 38 (Database issue), D227-D233.
    • (2010)
    • Rawlings, N.D.1    Barrett, A.J.2    Bateman, A.3
  • 30
  • 33
    • 77957915509 scopus 로고    scopus 로고
    • Localization and function of Rhipicephalus (Boophilus) microplus vitellin-degrading cysteine Q6 endopeptidase
    • Seixas A., Estrela A., Ceolato J.C., Pontes E.G., Lara F., Gondim K.C., Termignoni C. Localization and function of Rhipicephalus (Boophilus) microplus vitellin-degrading cysteine Q6 endopeptidase. Parasitology 2010, 137:1819-1831.
    • (2010) Parasitology , vol.137 , pp. 1819-1831
    • Seixas, A.1    Estrela, A.2    Ceolato, J.C.3    Pontes, E.G.4    Lara, F.5    Gondim, K.C.6    Termignoni, C.7
  • 36
    • 57549115852 scopus 로고    scopus 로고
    • Profiling of proteolytic enzymes in the gut of the tick Ixodes ricinus reveals an evolutionarily conserved network of aspartic and cysteine peptidases
    • Sojka D., Franta Z., Horn M., Hajdusek O., Caffrey C.R., Mares M., Kopacek P. Profiling of proteolytic enzymes in the gut of the tick Ixodes ricinus reveals an evolutionarily conserved network of aspartic and cysteine peptidases. Parasit. Vectors. 2008, 1:7.
    • (2008) Parasit. Vectors. , vol.1 , pp. 7
    • Sojka, D.1    Franta, Z.2    Horn, M.3    Hajdusek, O.4    Caffrey, C.R.5    Mares, M.6    Kopacek, P.7
  • 38
    • 0015522277 scopus 로고
    • Fluorescamine: A reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range
    • Udenfriend S., Stein S., Bohlen P., Dairman W., Leimgruber W., Weigele M. Fluorescamine: A reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range. Science 1972, 178:871-872.
    • (1972) Science , vol.178 , pp. 871-872
    • Udenfriend, S.1    Stein, S.2    Bohlen, P.3    Dairman, W.4    Leimgruber, W.5    Weigele, M.6
  • 39
    • 33846840838 scopus 로고    scopus 로고
    • Vaccination against ectoparasites
    • Willadsen P. Vaccination against ectoparasites. Parasitology 2006, 133:S9-S25.
    • (2006) Parasitology , vol.133
    • Willadsen, P.1
  • 42
    • 0035000312 scopus 로고    scopus 로고
    • Cysteine proprotease colocalizes with vitellogenin in compound granules of the cockroach fat body
    • Yin L., Nordin J.H., Lucches P., Giorgi F. Cysteine proprotease colocalizes with vitellogenin in compound granules of the cockroach fat body. Cell Tissue Res. 2001, 304:391-399.
    • (2001) Cell Tissue Res. , vol.304 , pp. 391-399
    • Yin, L.1    Nordin, J.H.2    Lucches, P.3    Giorgi, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.