메뉴 건너뛰기




Volumn 31, Issue 9, 2007, Pages 879-888

Preliminary characterization of hemolymph coagulation in Anopheles gambiae larvae

Author keywords

Anopheles gambiae; Coagulation; Drosophila; Insect immunity; Lipophorin; Phenoloxidase

Indexed keywords

BLOOD CLOTTING FACTOR; LIPOPHORIN; MONOPHENOL MONOOXYGENASE;

EID: 34247114978     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2006.12.006     Document Type: Article
Times cited : (22)

References (48)
  • 1
    • 0000330832 scopus 로고
    • Hemolymph coagulation
    • Rockstein M. (Ed), Academic Press, New York
    • Grégoire C. Hemolymph coagulation. In: Rockstein M. (Ed). Physiology of insecta vol. 5 (1974), Academic Press, New York 309-360
    • (1974) Physiology of insecta , vol.5 , pp. 309-360
    • Grégoire, C.1
  • 2
    • 0003348224 scopus 로고
    • Hemolymph clotting in insects
    • Brehélin M. (Ed), Springer, Berlin
    • Bohn H. Hemolymph clotting in insects. In: Brehélin M. (Ed). Immunity in invertebrates (1986), Springer, Berlin 188-207
    • (1986) Immunity in invertebrates , pp. 188-207
    • Bohn, H.1
  • 3
    • 1842800032 scopus 로고    scopus 로고
    • Coagulation in arthropods: defence, wound closure and healing
    • Theopold U., Schmidt O., Söderhäll K., and Dushay M.S. Coagulation in arthropods: defence, wound closure and healing. Trends Immunol 25 (2004) 289-294
    • (2004) Trends Immunol , vol.25 , pp. 289-294
    • Theopold, U.1    Schmidt, O.2    Söderhäll, K.3    Dushay, M.S.4
  • 4
    • 3042523021 scopus 로고    scopus 로고
    • Structure and function of coagulogen, a clottable protein in horseshoe crabs
    • Osaki T., and Kawabata S. Structure and function of coagulogen, a clottable protein in horseshoe crabs. Cell Mol Life Sci 61 (2004) 1257-1265
    • (2004) Cell Mol Life Sci , vol.61 , pp. 1257-1265
    • Osaki, T.1    Kawabata, S.2
  • 5
    • 0034694375 scopus 로고    scopus 로고
    • The proPO and clotting system in crustaceans
    • Sritunyalucksana K., and Söderhäll K. The proPO and clotting system in crustaceans. Aquaculture 191 (2000) 53-69
    • (2000) Aquaculture , vol.191 , pp. 53-69
    • Sritunyalucksana, K.1    Söderhäll, K.2
  • 6
    • 0033514933 scopus 로고    scopus 로고
    • The crayfish plasma clotting protein: a vitellogenin-related protein responsible for clot formation in crustacean blood
    • Hall M., Wang R., Antwerpen R.v., Sottrup-Jensen L., and Söderhäll K. The crayfish plasma clotting protein: a vitellogenin-related protein responsible for clot formation in crustacean blood. Proc Natl Acad Sci, USA 96 (1999) 1965-1970
    • (1999) Proc Natl Acad Sci, USA , vol.96 , pp. 1965-1970
    • Hall, M.1    Wang, R.2    Antwerpen, R.v.3    Sottrup-Jensen, L.4    Söderhäll, K.5
  • 7
    • 18044376633 scopus 로고    scopus 로고
    • Hemolymph coagulation in insect larvae and the role of phenoloxidase in Drosophila
    • Bidla G., Lindgren M.P.M., Theopold U., and Dushay M.S. Hemolymph coagulation in insect larvae and the role of phenoloxidase in Drosophila. Dev Comp Immunol 29 (2005) 669-679
    • (2005) Dev Comp Immunol , vol.29 , pp. 669-679
    • Bidla, G.1    Lindgren, M.P.M.2    Theopold, U.3    Dushay, M.S.4
  • 8
    • 1842665810 scopus 로고    scopus 로고
    • Isolation and characterization of hemolymph clotting factors in Drosophila melanogaster by a novel pull-out assay
    • Scherfer C., Karlsson C., Loseva O., Bidla G., Goto A., Havemann J., et al. Isolation and characterization of hemolymph clotting factors in Drosophila melanogaster by a novel pull-out assay. Curr Biol 14 (2004) 625-629
    • (2004) Curr Biol , vol.14 , pp. 625-629
    • Scherfer, C.1    Karlsson, C.2    Loseva, O.3    Bidla, G.4    Goto, A.5    Havemann, J.6
  • 10
    • 0345161806 scopus 로고    scopus 로고
    • Generation of evolutionary novelty by functional shift
    • Ganfornina M.D., and Sanchez D. Generation of evolutionary novelty by functional shift. Bioessays 21 (1999) 432-439
    • (1999) Bioessays , vol.21 , pp. 432-439
    • Ganfornina, M.D.1    Sanchez, D.2
  • 11
    • 3142583725 scopus 로고    scopus 로고
    • Immune responses in Anopheles gambiae
    • Levashina E.A. Immune responses in Anopheles gambiae. Insect Biochem Mol Biol 34 (2004) 673-678
    • (2004) Insect Biochem Mol Biol , vol.34 , pp. 673-678
    • Levashina, E.A.1
  • 12
    • 3543017971 scopus 로고    scopus 로고
    • Innate immunity in the malaria vector Anopheles gambiae: comparative and functional genomics
    • Osta M.A., Christophides G.K., Vlachou D., and Kafatos F.C. Innate immunity in the malaria vector Anopheles gambiae: comparative and functional genomics. J Exp Biol 207 (2004) 2551-2563
    • (2004) J Exp Biol , vol.207 , pp. 2551-2563
    • Osta, M.A.1    Christophides, G.K.2    Vlachou, D.3    Kafatos, F.C.4
  • 13
    • 1642545494 scopus 로고    scopus 로고
    • Comparative and functional genomics of the innate immune system in the malaria vector Anopheles gambiae
    • Christophides G.K., Vlachou D., and Kafatos F.C. Comparative and functional genomics of the innate immune system in the malaria vector Anopheles gambiae. Immunol Rev 198 (2004) 127-148
    • (2004) Immunol Rev , vol.198 , pp. 127-148
    • Christophides, G.K.1    Vlachou, D.2    Kafatos, F.C.3
  • 15
    • 0030867913 scopus 로고    scopus 로고
    • Molecular immune responses of the mosquito Anopheles gambiae to bacteria and malaria parasites
    • Dimopoulos G., Richman A., Müller H.-M., and Kafatos F.C. Molecular immune responses of the mosquito Anopheles gambiae to bacteria and malaria parasites. Proc Natl Acad Sci, USA 94 (1997) 11508-11513
    • (1997) Proc Natl Acad Sci, USA , vol.94 , pp. 11508-11513
    • Dimopoulos, G.1    Richman, A.2    Müller, H.-M.3    Kafatos, F.C.4
  • 16
    • 19344365657 scopus 로고    scopus 로고
    • Cellular and genetic analysis of wound healing in Drosophila larvae
    • Galko M.J., and Krasnow M.A. Cellular and genetic analysis of wound healing in Drosophila larvae. PLoS Biol 2 (2004) E239
    • (2004) PLoS Biol , vol.2
    • Galko, M.J.1    Krasnow, M.A.2
  • 17
    • 0344925804 scopus 로고    scopus 로고
    • Drosophila hemolectin gene is expressed in embryonic and larval hemocytes and its knock down causes bleeding defects
    • Goto A., Kadowaki T., and Kitagawa Y. Drosophila hemolectin gene is expressed in embryonic and larval hemocytes and its knock down causes bleeding defects. Dev Biol 264 (2003) 582-591
    • (2003) Dev Biol , vol.264 , pp. 582-591
    • Goto, A.1    Kadowaki, T.2    Kitagawa, Y.3
  • 18
    • 0020674063 scopus 로고
    • Lipophorin as the plasma coagulen in Locusta migratoria
    • Gellissen G. Lipophorin as the plasma coagulen in Locusta migratoria. Naturwissenschaften 70 (1983) 45-46
    • (1983) Naturwissenschaften , vol.70 , pp. 45-46
    • Gellissen, G.1
  • 19
    • 0000741030 scopus 로고
    • Isolation and characterization of plasma coagulen (PC) of the cockroach Leucophaea madera (Blatteria)
    • Barwig B. Isolation and characterization of plasma coagulen (PC) of the cockroach Leucophaea madera (Blatteria). J Comp Physiol B 155 (1985) 135-143
    • (1985) J Comp Physiol B , vol.155 , pp. 135-143
    • Barwig, B.1
  • 20
    • 0032407614 scopus 로고    scopus 로고
    • Two major proteins from locust plasma are involved in coagulation and are specifically precipitated by laminarin, a beta-1,3-glucan
    • Duvic B., and Brehélin M. Two major proteins from locust plasma are involved in coagulation and are specifically precipitated by laminarin, a beta-1,3-glucan. Insect Biochem Mol Biol 28 (1998) 959-967
    • (1998) Insect Biochem Mol Biol , vol.28 , pp. 959-967
    • Duvic, B.1    Brehélin, M.2
  • 21
    • 0035983328 scopus 로고    scopus 로고
    • Insect hemolymph clotting: evidence for interaction between the coagulation system and the prophenoloxidase activating cascade
    • Li D., Scherfer C., Korayem A.M., Zhao Z., Schmidt O., and Theopold U. Insect hemolymph clotting: evidence for interaction between the coagulation system and the prophenoloxidase activating cascade. Insect Biochem Mol Biol 32 (2002) 919-928
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 919-928
    • Li, D.1    Scherfer, C.2    Korayem, A.M.3    Zhao, Z.4    Schmidt, O.5    Theopold, U.6
  • 22
    • 2542508922 scopus 로고    scopus 로고
    • A hemocyte-like cell line established from the malaria vector Anopheles gambiae expresses six prophenoloxidase genes
    • Müller H.M., Dimopoulos G., Blass C., and Kafatos F.C. A hemocyte-like cell line established from the malaria vector Anopheles gambiae expresses six prophenoloxidase genes. J Biol Chem 274 (1999) 11727-11735
    • (1999) J Biol Chem , vol.274 , pp. 11727-11735
    • Müller, H.M.1    Dimopoulos, G.2    Blass, C.3    Kafatos, F.C.4
  • 23
    • 1642463826 scopus 로고    scopus 로고
    • The prophenoloxidase-activating system in invertebrates
    • Cerenius L., and Söderhäll K. The prophenoloxidase-activating system in invertebrates. Immunol Rev 198 (2004) 116-126
    • (2004) Immunol Rev , vol.198 , pp. 116-126
    • Cerenius, L.1    Söderhäll, K.2
  • 24
    • 0031177932 scopus 로고    scopus 로고
    • Molecular cloning of cDNAs for two pro-phenol oxidase subunits from the malaria vector, Anopheles gambiae
    • Jiang H., Wang Y., Korochkina S.E., Benes H., and Kanost M.R. Molecular cloning of cDNAs for two pro-phenol oxidase subunits from the malaria vector, Anopheles gambiae. Insect Biochem Mol Biol 27 (1997) 693-699
    • (1997) Insect Biochem Mol Biol , vol.27 , pp. 693-699
    • Jiang, H.1    Wang, Y.2    Korochkina, S.E.3    Benes, H.4    Kanost, M.R.5
  • 25
    • 26244443507 scopus 로고    scopus 로고
    • Purification and primary structural characterization of prophenoloxidases from Aedes aegypti larvae
    • Li J.S., Ruyl Kim S., Christensen B.M., and Li J. Purification and primary structural characterization of prophenoloxidases from Aedes aegypti larvae. Insect Biochem Mol Biol 35 (2005) 1269-1283
    • (2005) Insect Biochem Mol Biol , vol.35 , pp. 1269-1283
    • Li, J.S.1    Ruyl Kim, S.2    Christensen, B.M.3    Li, J.4
  • 26
    • 0026512098 scopus 로고
    • Effect of particle lipid content on the structure of insect lipophorins
    • Ryan R.O., Kay C.M., Oikawa K., Liu H., Bradley R., and Scraba D.G. Effect of particle lipid content on the structure of insect lipophorins. J Lipid Res 33 (1992) 55-63
    • (1992) J Lipid Res , vol.33 , pp. 55-63
    • Ryan, R.O.1    Kay, C.M.2    Oikawa, K.3    Liu, H.4    Bradley, R.5    Scraba, D.G.6
  • 27
    • 0002513065 scopus 로고
    • Limited proteolysis of prophenoloxidase during activation by microbial products in insect plasma and effect of phenoloxidase on electrophoretic mobilities of plasma proteins
    • Ashida C., and Yoshida Y. Limited proteolysis of prophenoloxidase during activation by microbial products in insect plasma and effect of phenoloxidase on electrophoretic mobilities of plasma proteins. Insect Biochem 18 (1988) 11-19
    • (1988) Insect Biochem , vol.18 , pp. 11-19
    • Ashida, C.1    Yoshida, Y.2
  • 28
  • 29
    • 33645400827 scopus 로고    scopus 로고
    • Recognition and inactivation of LPS by lipophorin particles
    • Ma G., Hay D., Li D., Asgari S., and Schmidt O. Recognition and inactivation of LPS by lipophorin particles. Dev Comp Immunol 30 (2006) 619-626
    • (2006) Dev Comp Immunol , vol.30 , pp. 619-626
    • Ma, G.1    Hay, D.2    Li, D.3    Asgari, S.4    Schmidt, O.5
  • 31
    • 33646839951 scopus 로고    scopus 로고
    • Regulation of lipid metabolism genes, lipid carrier protein Lipophorin, and its receptor during immune challenge in the mosquito Aedes aegypti
    • Cheon H.M., Shin S.W., Bian G., Park J.H., and Raikhel A.S. Regulation of lipid metabolism genes, lipid carrier protein Lipophorin, and its receptor during immune challenge in the mosquito Aedes aegypti. J Biol Chem 281 (2006) 8426-8435
    • (2006) J Biol Chem , vol.281 , pp. 8426-8435
    • Cheon, H.M.1    Shin, S.W.2    Bian, G.3    Park, J.H.4    Raikhel, A.S.5
  • 32
    • 21844450491 scopus 로고    scopus 로고
    • Functional genomic analysis of midgut epithelial responses in Anopheles during Plasmodium invasion
    • Vlachou D., Schlegelmilch T., Christophides G.K., and Kafatos F.C. Functional genomic analysis of midgut epithelial responses in Anopheles during Plasmodium invasion. Curr Biol 15 (2005) 1185-1195
    • (2005) Curr Biol , vol.15 , pp. 1185-1195
    • Vlachou, D.1    Schlegelmilch, T.2    Christophides, G.K.3    Kafatos, F.C.4
  • 34
    • 23844501112 scopus 로고    scopus 로고
    • The hemolymph proteome of Anopheles gambiae
    • Paskewitz S.M., and Shi L. The hemolymph proteome of Anopheles gambiae. Insect Biochem Mol Biol 35 (2005) 815-824
    • (2005) Insect Biochem Mol Biol , vol.35 , pp. 815-824
    • Paskewitz, S.M.1    Shi, L.2
  • 35
    • 28844452777 scopus 로고    scopus 로고
    • The roles of two clip domain serine proteases in innate immune responses of the malaria vector Anopheles gambiae
    • Volz J., Osta M.A., Kafatos F.C., and Muller H.M. The roles of two clip domain serine proteases in innate immune responses of the malaria vector Anopheles gambiae. J Biol Chem 280 (2005) 40161-40168
    • (2005) J Biol Chem , vol.280 , pp. 40161-40168
    • Volz, J.1    Osta, M.A.2    Kafatos, F.C.3    Muller, H.M.4
  • 36
    • 0018384686 scopus 로고
    • A comparative synopsis of the structure and function of the blood cells of insects and other invertebrates
    • Ratcliffe N.A., and Rowley A.F. A comparative synopsis of the structure and function of the blood cells of insects and other invertebrates. Dev Comp Immunol 3 (1979) 189-221
    • (1979) Dev Comp Immunol , vol.3 , pp. 189-221
    • Ratcliffe, N.A.1    Rowley, A.F.2
  • 37
    • 0017105720 scopus 로고
    • The granular cells of Galleria mellonella during clotting and phagocytic reactions in vitro
    • Rowley A.F., and Ratcliffe N.A. The granular cells of Galleria mellonella during clotting and phagocytic reactions in vitro. Tissue Cell 8 (1976) 437-446
    • (1976) Tissue Cell , vol.8 , pp. 437-446
    • Rowley, A.F.1    Ratcliffe, N.A.2
  • 39
    • 0021770429 scopus 로고
    • Structural studies on lipophorin, an insect lipoprotein
    • Shapiro J.P., Keim P.S., and Law J.H. Structural studies on lipophorin, an insect lipoprotein. J Biol Chem 259 (1984) 3680-3685
    • (1984) J Biol Chem , vol.259 , pp. 3680-3685
    • Shapiro, J.P.1    Keim, P.S.2    Law, J.H.3
  • 40
    • 0024318973 scopus 로고
    • A strategy for solubilizing delipidated apolipoprotein with lysophosphatidylcholine and reconstitution with phosphatidylcholine
    • Kawooya J.K., Wells M.A., and Law J.H. A strategy for solubilizing delipidated apolipoprotein with lysophosphatidylcholine and reconstitution with phosphatidylcholine. Biochemistry 28 (1989) 6658-6667
    • (1989) Biochemistry , vol.28 , pp. 6658-6667
    • Kawooya, J.K.1    Wells, M.A.2    Law, J.H.3
  • 41
    • 0017418680 scopus 로고
    • The encapsulation of foreign tissue implants in Galleria mellonella larvae
    • Schmit A.R., and Ratcliffe N.A. The encapsulation of foreign tissue implants in Galleria mellonella larvae. J Insect Physiol 23 (1977) 175-184
    • (1977) J Insect Physiol , vol.23 , pp. 175-184
    • Schmit, A.R.1    Ratcliffe, N.A.2
  • 42
    • 0018140445 scopus 로고
    • A histological study of wound healing and hemocyte function in the wax-moth Galleria mellonella
    • Rowley A.F., and Ratcliffe N.A. A histological study of wound healing and hemocyte function in the wax-moth Galleria mellonella. J Morphol 157 (1978) 181-200
    • (1978) J Morphol , vol.157 , pp. 181-200
    • Rowley, A.F.1    Ratcliffe, N.A.2
  • 43
    • 0029833464 scopus 로고    scopus 로고
    • Granular cells are required for encapsulation of foreign targets by insect haemocytes
    • Pech L.L., and Strand M.R. Granular cells are required for encapsulation of foreign targets by insect haemocytes. J Cell Sci 109 (1996) 2053-2060
    • (1996) J Cell Sci , vol.109 , pp. 2053-2060
    • Pech, L.L.1    Strand, M.R.2
  • 44
    • 0020615861 scopus 로고
    • Mosquito hemocytes: a review
    • Hall D.W. Mosquito hemocytes: a review. Dev Comp Immunol 7 (1983) 1-12
    • (1983) Dev Comp Immunol , vol.7 , pp. 1-12
    • Hall, D.W.1
  • 45
    • 0036364092 scopus 로고    scopus 로고
    • Cellular-mediated reactions to foreign organisms inoculated into the hemocoel of Anopheles albimanus (Diptera: Culicidae)
    • Hernandez-Martinez S., Lanz H., Rodriguez M.H., Gonzalez-Ceron L., and Tsutsumi V. Cellular-mediated reactions to foreign organisms inoculated into the hemocoel of Anopheles albimanus (Diptera: Culicidae). J Med Entomol 39 (2002) 61-69
    • (2002) J Med Entomol , vol.39 , pp. 61-69
    • Hernandez-Martinez, S.1    Lanz, H.2    Rodriguez, M.H.3    Gonzalez-Ceron, L.4    Tsutsumi, V.5
  • 46
    • 0344630287 scopus 로고    scopus 로고
    • The role of reactive oxygen species on Plasmodium melanotic encapsulation in Anopheles gambiae
    • Kumar S., Christophides G.K., Cantera R., Charles B., Han Y.S., Meister S., et al. The role of reactive oxygen species on Plasmodium melanotic encapsulation in Anopheles gambiae. Proc Natl Acad Sci, USA 100 (2003) 14139-14144
    • (2003) Proc Natl Acad Sci, USA , vol.100 , pp. 14139-14144
    • Kumar, S.1    Christophides, G.K.2    Cantera, R.3    Charles, B.4    Han, Y.S.5    Meister, S.6
  • 47
    • 8644286464 scopus 로고    scopus 로고
    • A glue-like Drosophila salivary protein is expressed in hemocytes: evidence for a function in hemolymph coagulation
    • Korayem A., Fabbri M., Takahashi K., Scherfer C., Lindgren M., Schmidt O., et al. A glue-like Drosophila salivary protein is expressed in hemocytes: evidence for a function in hemolymph coagulation. Insect Biochem Mol Biol 34 (2004) 1297-1304
    • (2004) Insect Biochem Mol Biol , vol.34 , pp. 1297-1304
    • Korayem, A.1    Fabbri, M.2    Takahashi, K.3    Scherfer, C.4    Lindgren, M.5    Schmidt, O.6
  • 48


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.