References
- Andersen SO (2005) Cuticular sclerotization and tanning. In: Gilbert LI, Iatrou K, Gill SS (Eds.), Comprehensive Molecular Insect Science vol. 4. Elsevier, Amsterdam, pp. 145-170.
- Arakane Y, Lomakin J, Beeman RW, Muthukrishnan S, Gehrke SH, Kanost MR, et al. (2009) Molecular and functional analyses of amino acid decarboxylases involved in cuticle tanning in Tribolium castaneum. J Biol Chem 284, 16584-16594. https://doi.org/10.1074/jbc.M901629200
- Asano T, Ashida M (2001a) Transepithelially transported prophenoloxidase in the cuticle of the silkworm, Bombyx mori: identification of its methionyl residues oxidized to methionine sulfoxides. J Biol Chem 276, 11113-11125. https://doi.org/10.1074/jbc.m008425200
- Asano T, Ashida M (2001b) Cuticular pro-phenoloxidase of the silkworm, Bombyx mori: purification and demonstration of its transport from hemolymph. J Biol Chem 276, 11100-11112. https://doi.org/10.1074/jbc.m008426200
- Ashida M, Brey PT (1995) Role of the integument in insect defense: pro-phenol oxidase cascade in the cuticular matrix. Proc Natl Acad Sci U. S. A. 92, 10698-10702. https://doi.org/10.1073/pnas.92.23.10698
- Cambi A, Koopman M, Figdor CG (2005) How C-type lectins detect pathogens. Cell Microbiol 7, 481-488. https://doi.org/10.1111/j.1462-5822.2005.00506.x
- Cerenius L, Soderhall K (2004) The prophenoloxidase-activating system in invertebrates. Immunol Rev 198, 116-126. https://doi.org/10.1111/j.0105-2896.2004.00116.x
- Cerenius L, Lee BL, Soderhall K (2008) The proPO-system: pros and cons for its role in invertebrate immunity. Trends Immunol 29, 263-271. https://doi.org/10.1016/j.it.2008.02.009
- Dodd RB, Drickamer K (2001) Lectin-like proteins in model organisms: implications for evolution of carbohydrate-binding activity. Glycobiology 11, 71R-79R. https://doi.org/10.1093/glycob/11.5.71R
- Futahashi R, Fujiwara H (2005) Melanin-synthesis enzymes coregulate stage-specific larval cuticular markings in the swallowtail butterfly, Papilio xuthus. Dev Genes Evol 215, 519-529. https://doi.org/10.1007/s00427-005-0014-y
- Gorman MJ, An C, Kanost MR (2007) Characterization of tyrosine hydroxylase from Manduca sexta. Insect Biochem Mol Biol 37, 1327-1337. https://doi.org/10.1016/j.ibmb.2007.08.006
- Gorman MJ, Arakane Y (2010) Tyrosine hydroxylase is required for cuticle sclerotization and pigmentation in Tribolium castaneum. Insect Biochem Mol Biol 40, 267-273. https://doi.org/10.1016/j.ibmb.2010.01.004
- Hashimoto K, Yamano Y, Morishima I (2008) Induction of tyrosine hydroxylase gene expression by bacteria in the fat body of erisilkworm, Samia cynthia ricini. Comp Biochem Physiol B 149, 501-506. https://doi.org/10.1016/j.cbpb.2007.11.010
- Hiruma K, Riddiford LM (2009) The molecular mechanisms of cuticular melanization: the ecdysone cascade leading to dopa decarboxylase expression in Manduca sexta. Insect Biochem Mol Biol 39, 245-253. https://doi.org/10.1016/j.ibmb.2009.01.008
- Hopkins TL, Kramer KJ (1992) Insect cuticle sclerotization. Ann Rev Entomol 37, 273-302.
- Jiang H, Kanost MR (2000) The clip-domain family of serine proteinases in arthropods. Insect Biochem Mol Biol 30, 95-105. https://doi.org/10.1016/S0965-1748(99)00113-7
- Kanost MR, Jiang H, Yu ZQ (2004) Innate immune responses of a lepidopteran insect, Manduca sexta. Immunol Rev 198, 97-105. https://doi.org/10.1111/j.0105-2896.2004.0121.x
- Kim BY, Jin BR (2017) The dual roles of Bombyx mori immulectin in cuticular melanization and innate immunity. J Aisa-Pac Entomol 20, 761-766. https://doi.org/10.1016/j.aspen.2017.05.002
- Koizumi N, Morozumi A, Imamura M, Tanaka E, Iwahana H, Sato R (1997) Lipopolysaccharide-binding proteins and their involvement in the bacterial clearance from the hemolymph of the silkworm Bombyx mori. Eur J Biochem 248, 217-224. https://doi.org/10.1111/j.1432-1033.1997.t01-1-00217.x
- Koizumi N, Imai Y, Morozumi A, Imamura M, Kadotani T, Yaoi K, et al. (1999a) Lipopolysaccharide-binding protein of Bombyx mori participates in a hemocyte-mediated defense reaction against gram-negative bacteria. J Insect Physiol 45, 853-859. https://doi.org/10.1016/S0022-1910(99)00069-4
- Koizumi N, Imamura M, Kadotani T, Yaoi K, Iwahana H, Sato R (1999b) The lipopolysaccharide-binding protein participating in a hemocyte nodule formation in the silkworm Bombyx mori is a novel member of the C-type lectin superfamily with two different tandem carbohydrate-recognition domains. FEBS Lett 443, 139-143. https://doi.org/10.1016/S0014-5793(98)01701-3
- Lee KS, Kim BY, Jin BR (2015) Differential regulation of tyrosine hydroxylase in cuticular melanization and innate immunity in the silkworm Bombyx mori. J Asia-Pac Entomol 18, 765-770. https://doi.org/10.1016/j.aspen.2015.09.008
- Lee KS, Kim BY, Choo YM, Jin BR (2018) Dual role of the serine protease homolog BmSPH-1 in the development and immunity of the silkworm Bombyx mori. Dev Comp Immunol 85, 170-176. https://doi.org/10.1016/j.dci.2018.04.011
- Lemaitre B, Hoffmann J (2007) The host defense of Drosophila melanogaster. Annu Rev Immunol 25, 697-743. https://doi.org/10.1146/annurev.immunol.25.022106.141615
- Liu C, Yamamoto K, Cheng TC, Kadono-Okuda K, Narukawa J, Liu SP, et al. (2010) Repression of tyrosine hydroxylase is responsible for the sex-linked chocolate mutation of the silkworm, Bombyx mori. Proc Natl Acad Sci U. S. A. 107, 12980-12985. https://doi.org/10.1073/pnas.1001725107
- Rao XJ, Shahzad T, Liu S, Wu P, He YT, Sun WJ, et al. (2015) Identification of C-type lectin-domain proteins (CTLDPs) in silkworm Bombyx mori. Dev Comp Immunol 53, 328-338. https://doi.org/10.1016/j.dci.2015.07.005
- Riley PA (1997) Melanin. Int J Biochem Cell Biol 29, 1235-1239. https://doi.org/10.1016/S1357-2725(97)00013-7
- Kramer KJ, Hopkins TL (1987) Tyrosine metabolism for insect cuticle tanning. Arch Insect Biochem Physiol 6, 279-301. https://doi.org/10.1002/arch.940060406
- Takase H, Watanabe A, Yoshizawa Y, Kitami M, Sato R (2009) Identification and comparative analysis of three novel C-type lectins from the silkworm with functional implications in pathogen recognition. Dev Comp Immunol 33, 789-800. https://doi.org/10.1016/j.dci.2009.01.005
- True JR, Edwards KA, Yamamoto D. Carroll SB (1999) Drosophila wing melanin patterns from by vein-dependent elaboration of enzymatic prepatterns. Curr Biol 9, 1382-1391. https://doi.org/10.1016/S0960-9822(00)80083-4
- Watanabe A, Miyazawa S, Kitami M, Tabunoki H, Ueda K, Sato R (2006) Characterization of a novel C-type lectin, Bombyx mori multibinding protein, from the B. mori hemolymph: mechanism of wide-range microorganism recognition and role in immunity. J Immunol 177, 4594-4604. https://doi.org/10.4049/jimmunol.177.7.4594
- Wright TRF (1987) The genetics of biogenic amine metabolism, sclerotization, and melanization in Drosophila melanogaster. Adv Genet 24, 127-222.
- Yu XQ, Jiang H, Wang Y, Kanost MR (2003) Nonproteolytic serine proteinase homologs are involved in prophenoloxidase activation in the tobacco hornworm, Manduca sexta. Insect Mol Biol 33, 197-208. https://doi.org/10.1016/S0965-1748(02)00191-1
- Zhan S, Guo Q, Li M, Li M, Li J, Miao X, et al. (2010) Disruption of an N-acetyltransferase gene in the silkworm reveals a novel role in pigmentation. Development 137, 4083-4090 https://doi.org/10.1242/dev.053678
- Zou FM, Lee KS, Kim BY, Kim HJ, Gui ZZ, Zhang GZ, et al. (2015) Differential and spatial regulation of the prophenoloxidase (proPO) and proPO-activating enzyme in cuticular melanization and innate immunity in Bombyx mori pupae. J Asia-Pac Entomol 18, 757-764. https://doi.org/10.1016/j.aspen.2015.09.007