A Novel Peptide Mediates Aggregation and Migration of Hemocytes from an Insect

Current Biology

Volumn 19, Issue 9, 2009, Pages 779-785

  Nakatogawa, Shin ichi ^a   Oda, Yasunori ^b   Kamiya, Masakatsu ^a   Kamijima, Tatsuro ^a   Aizawa, Tomoyasu ^a   Clark, Kevin D ^c   Demura, Makoto ^a   Kawano, Keiichi ^a   Strand, Michael R ^c   Hayakawa, Yoichi ^b  

^a HOKKAIDO UNIVERSITY   (Japan)

^b SAGA UNIVERSITY   (Japan)

^c UNIVERSITY OF GEORGIA   (United States)

Author keywords

CELLBIO; CELLIMMUNO

Indexed keywords

CHEMOKINE;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; BLOOD CELL; CELL AGGREGATION; CELL MOTION; CHEMICAL STRUCTURE; GENETICS; IMMUNOHISTOCHEMISTRY; IMMUNOLOGY; METABOLISM; MOLECULAR GENETICS; MOTH; NUCLEOTIDE SEQUENCE; PHAGOCYTOSIS; PHYSIOLOGY;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CELL AGGREGATION; CELL MOVEMENT; CHEMOKINES; HEMOCYTES; IMMUNOHISTOCHEMISTRY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOTHS; PHAGOCYTOSIS;

HEXAPODA; LEPIDOPTERA; MYTHIMNA SEPARATA;

EID: 67349235127     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2009.03.050     Document Type: Article

References (36)

1. Lanot R., Zachary D., Holder F., and Meister M. Postembryonic hematopoiesis in Drosophila. Dev. Biol. 230 (2001) 243-257
2. Lavine M.D., and Strand M.R. Insect hemocytes and their role in cellular immune responses. Insect Biochem. Mol. Biol. 32 (2002) 1237-1242
3. Strand M.R. Insect hemocytes and their role in immunity. In: Beckage N.E. (Ed). Insect Immunology (2008), Academic Press, San Diego 25-48
4. Ribeiro C., and Brehelin M. Insect haemocytes: What type of cell is what?. J. Insect Physiol. 52 (2006) 417-429
5. Bangham J., Jiggins F., and Lemaitre B. Insect immunity, the post-genomic era. Immunity 25 (2006) 1-5
6. Ferrandon D., Imler J.-L., Hetru C., and Hoffmann J.A. The Drosophila systemic immune response: Sensing and signaling during bacterial and fungal infections. Nat. Rev. Immunol. 7 (2007) 862-874
7. Hultmark D., and Borge-Renberg K. Drosophila immunity: Is antigen processing the first step?. Curr. Biol. 17 (2007) R22-R24
8. Tepass U., Fessler L.I., Aziz A., and Hartenstein V. Embryonic origin of hemocytes and their relationship to cell death in Drosophila. Development 120 (1994) 1829-1837
9. Cho N.K., Keyes L., Johnson E., Heller J., Ryner L., Karim F., and Krasnow M.A. Developmental control of blood cell migration by the Drosophila VEGF pathway. Cell 108 (2002) 865-876
10. Brukner K.L., Kockel P., Duchek C.M., Luque P., Rorth P., and Perrimon N. The PDGF/VEGF receptor controls blood cell survival in Drosophila. Dev. Cell 7 (2004) 73-84
11. Wood W., Faria C., and Jacinto A. Distinct mechanisms regulate hemocyte chemotaxis during development and wound healing in Drosophila melanogaster. J. Cell Biol. 173 (2006) 405-416
12. Stramer B., Wood W., Galko M.J., Redd A., and Jacinto S.M. Live imaging of wound inflammation in Drosophila embryos reveals key roles for small GTPases during in vivo cell migration. J. Cell Biol. 168 (2005) 1829-1837
13. Babcock D.T., Brock A.R., Fish G.S., Wang Y., Perrin L., Krasnow M.A., and Galko M.J. Circulating blood cells function as a surveillance system for damaged tissue in Drososphila larvae. Proc. Natl. Acad. Sci. USA 105 (2008) 10017-10022
14. Hayakawa Y. Juvenile hormone esterase activity repressive factor in the plasma of parasitized insect larvae. J. Biol. Chem. 265 (1990) 10813-10816
15. Hayakawa Y., and Ohnishi A. Cell growth activity of growth-blocking peptide. Biochem. Biophys. Res. Commun. 250 (1998) 194-199
16. Strand M.R., Hayakawa Y., and Clark K.D. Plasmatocyte spreading peptide (PSP1) and growth blocking peptide (GBP) are multifunctional homologs. J. Insect Physiol. 46 (2000) 817-824
17. Hayakawa Y. Growth-blocking peptide: an insect biogenic peptide that prevents the onset of metamorphosis. J. Insect Physiol. 41 (1995) 1-6
18. Theopold U., Schmidt O., Soderhall K., and Dushay M.S. Coagulation in arthropods: defence, wound closure and healing. Trends Immunol. 25 (2004) 289-294
19. Galko M.J., and Krasnow M.A. Cellular and genetic analysis of wound healing in Drosophila larvae. PLoS Biol. 2 (2004) e239
20. Mace K.A., Joseph C.P., and McGinnis W. An epidermal barrier wound repair pathway in Drosophila is mediated by grainy head. Science 308 (2005) 381-385
21. Elrod-Erickson M., Mishra S., and Schneider D. Interactions between the cellular and humoral immune responses in Drosophila. Curr. Biol. 10 (2000) 781-784
22. Gardiner L.E.M., and Strand M.R. Hematopoiesis in larval Pseudoplusia includens and Spodoptera frugiperda. Arch. Insect Biochem. Physiol. 43 (2000) 147-164
23. Mellado M., Rodriguez-Frade J.M., Manes S., and Martinez A.C. Chemokine signaling and functional responses: The role of receptor dimerization and TK pathway activation. Annu. Rev. Immunol. 19 (2001) 397-421
24. Allen S.J., Crown S.E., and Handel T.M. Chemokine: Receptor structure, interactions, and antagonism. Annu. Rev. Immunol. 25 (2007) 787-820
25. Wang Y., Jiang H.B., and Kanost M.R. Biologial activity of Manduca sexta paralytic and plasmatocyte spreading peptide and primary structure of its hemolymph precursor. Insect Biochem. Mol. Biol. 12 (1999) 1075-1086
26. Clark K.D., Pech L., and Strand M.R. Isolation and identification of a plasmatocyte spreading peptide from hemolymph of the lepidopteran insect Pseudoplusia includens. J. Biol. Chem. 272 (1997) 23440-23447
27. Aizawa T., Hayakawa Y., Ohnishi A., Fujitani N., Clark K.D., Strand M.R., Miura K., Koganesawa N., Kumaki Y., Demura M., et al. Structure and activity of the insect cytokine growth-blocking peptide: Essential regions for mitogenic and hemocyte stimulating activities are separate. J. Biol. Chem. 276 (2001) 31813-31818
28. Clark K.D., Volkman B.F., Thoetkiattikul H., King D., Hayakawa Y., and Strand M.R. Alanine-scanning mutagenesis of plasmatocyte spreading peptide identifies critical residues for biological activity. J. Biol. Chem. 276 (2001) 18491-18496
29. Matumoto Y., Oda Y., Uryu M., and Hayakawa Y. Insect cytokine growth-blocking peptide triggers a termination system of cellular immunity by inducing its binding protein. J. Biol. Chem. 278 (2003) 38579-38585
30. Clark K.D., Volkman B.F., Thoetkiattikul H., Hayakawa Y., and Strand M.R. N-terminal residues of plasmatocyte spreading peptide possess specific determinants required for biological activity. J. Biol. Chem. 276 (2001) 37431-37435
31. Clark K.D., Garczynski S., Arora A., Crim J., and Strand M.R. Specific residues in plasmatocyte spreading peptide are required for receptor binding and functional antagonism of insect immune cells. J. Biol. Chem. 279 (2004) 33246-33252
32. Watanabe S., Tada M., Aizawa T., Toshida M., Sugaya T., Taguchi M., Kouno T., Nakamura T., Mizuguchi M., Demura M., et al. N-terminal mutational analysis of the interaction between growth-blocking peptide (GBP) and receptor of insect immune cells. Protein Pept. Lett. 13 (2006) 815-822
33. Moser B., Dewald B., Barella L., Schumacher C., Baggiolini M., and Clark-Lewis I. Interleukin-8 antagonists generated by N-terminal modification. J. Biol. Chem. 268 (1993) 7125-7128
34. Clark-Lewis I., Kim K.-S., Rajarathnam K., Gong J.-H., Dewald B., Baggiolini M., and Sykes B.D. Structure-activity relationships of chemokines. J. Leukoc. Biol. 57 (1995) 703-711
35. Hemmerich S., Paavola C., Bloom A., Bhakta S., Freedman R., Grunberger D., Krstenansky J., Lee S., McCarley D., Mulkins M., et al. Identification of residues in the monocyte chemotactic protein-1 that contact the MCP-1 receptor, CCR2. Biochemistry 38 (1999) 13013-13025
36. Dong C., Chua A., Ganguly B., Krensky A.M., and Clayberger C. Glycosylated recombinant human XCL1/lymphotactin exhibits enhanced biological activity. J. Immunol. Methods 302 (2005) 136-144