Preliminary characterization of hemolymph coagulation in Anopheles gambiae larvae

被引:21
作者
Agianian, Bogos
Lesch, Christine
Loseva, Olga
Dushay, Mitchell S.
机构
[1] Uppsala Univ, Dept Comparat Physiol, S-75236 Uppsala, Sweden
[2] European Mol Biol Lab, D-69117 Heidelberg, Germany
[3] Democritus Univ Thrace, Dept Mol Biol & Genet, Alexandroupolis 68100, Greece
[4] Stockholm Univ, Dept Mol Biol & Funct Genom, S-10691 Stockholm, Sweden
[5] Stockholm Univ, Dept Genet Microbiol & Toxicol, S-10691 Stockholm, Sweden
[6] Sodertorns Hogskola, Dept Life Sci, S-14189 Huddinge, Sweden
关键词
Anopheles gambiae; Drosophila; coagulation; lipophorin; phenoloxidase; insect immunity; MALARIA VECTOR; GALLERIA-MELLONELLA; IMMUNE-RESPONSES; FUNCTIONAL GENOMICS; PLASMA COAGULOGEN; GRANULAR CELLS; AEDES-AEGYPTI; LIPOPHORIN; PROPHENOLOXIDASE; SYSTEM;
D O I
10.1016/j.dci.2006.12.006
中图分类号
S9 [水产、渔业];
学科分类号
0908 ;
摘要
Hemolymph coagulation is a first response to injury, impeding infection, and ending bleeding. Little is known about its molecular basis in insects, but clotting factors have been identified in the fruit fly Drosophila melanogaster. Here, we have begun to study coagulation in the aquatic larvae of the malaria vector mosquito Anopheles gambiae using methods developed for Drosophila. A delicate clot was seen by light microscopy, and pullout and proteomic analysis identified phenoloxidase and apolipophorin-I as major candidate clotting factors. Electron microscopic analysis confirmed clot formation and revealed it contains fine molecular sheets, most likely a result of lipophorin assembly. Phenoloxidase appears to be more critical in clot formation in Anopheles than in Drosophila. The Anopheles larval clot thus differs in formation, structure, and composition from the clot in Drosophila, confirming the need to study coagulation in different insect species to learn more about its evolution and adaptation to different lifestyles. (C) 2007 Published by Elsevier Ltd.
引用
收藏
页码:879 / 888
页数:10
相关论文
共 49 条
[11]   Two major proteins from locust plasma are involved in coagulation and are specifically precipitated by laminarin, a β-1,3-glucan [J].
Duvic, B ;
Brehelin, M .
INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY, 1998, 28 (12) :959-967
[12]   Cellular and genetic analysis of wound healing in Drosophila larvae [J].
Galko, MJ ;
Krasnow, MA .
PLOS BIOLOGY, 2004, 2 (08) :1114-1126
[13]  
Ganfornina MD, 1999, BIOESSAYS, V21, P432, DOI 10.1002/(SICI)1521-1878(199905)21:5<432::AID-BIES10>3.0.CO
[14]  
2-T
[15]   LIPOPHORIN AS THE PLASMA COAGULOGEN IN LOCUSTA-MIGRATORIA [J].
GELLISSEN, G .
NATURWISSENSCHAFTEN, 1983, 70 (01) :45-46
[16]   Drosophila hemolectin gene is expressed in embryonic and larval hemocytes and its knock down causes bleeding defects [J].
Goto, A ;
Kadowaki, T ;
Kitagawa, Y .
DEVELOPMENTAL BIOLOGY, 2003, 264 (02) :582-591
[17]  
Gregoire C., 1974, The Physiology of Insecta, V5, P309, DOI DOI 10.1016/B978-0-12-591605-9.50014-7
[18]   MOSQUITO HEMOCYTES - A REVIEW [J].
HALL, DW .
DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY, 1983, 7 (01) :1-12
[19]   The crayfish plasma clotting protein:: A vitellogenin-related protein responsible for clot formation in crustacean blood [J].
Hall, M ;
Wang, RG ;
van Antwerpen, R ;
Sottrup-Jensen, L ;
Söderhäll, K .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (05) :1965-1970
[20]   Cellular-mediated reactions to foreign organisms inoculated into the hemocoel of Anopheles albimanus (Diptera: Culicidae) [J].
Hernández-Martínez, S ;
Lanz, H ;
Rodríguez, MH ;
González-Ceron, L ;
Tsutsumi, V .
JOURNAL OF MEDICAL ENTOMOLOGY, 2002, 39 (01) :61-69