@article {987,
	title = {Activation of the Sarcophaga lectin gene promoter in transgenic Drosophila},
	volume = {50},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalDepartment of Cell Biochemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, Bunkyo-ku, Tokyo, Japan.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=12111973},
	pages = {131 - 138},
	publisher = {Copyright 2002 Wiley-Liss, Inc.},
	abstract = {We established transgenic Drosophila strains in which the lacZ gene was expressed under the control of the 5{\textquoteright}-upstream regulatory region of the Sarcophaga lectin gene promoter (3.1 kbp). The reporter gene was expressed in the fat bodies of the transgenic larvae when they were immunized by body pricking or treatment with Escherichia coli, which was the same as the Sarcophaga lectin gene expression in Sarcophaga larvae. However, the same reporter gene was found to be expressed constitutively in the digestive tracts of the transgenic larvae even without immunization.},
	keywords = {*Depsipeptides, *Insect Proteins, *Lectins, C-Type, *Peptides, *Promoter Regions, Genetic, *Transcriptional Activation, Animals, Animals, Genetically Modified, Anti-Bacterial Agents/immunology, beta-Galactosidase/genetics, Cell Line, Diptera/genetics/*metabolism, Drosophila melanogaster/genetics/immunology, Escherichia coli/immunology, Genes, Reporter, Lectins/*genetics, Staphylococcus aureus/immunology, Tissue Distribution, Transgenes},
	author = {Tanji, T. and Kobayashi, A. and Natori, S.}
}
@article {648,
	title = {Gene expression of heat-shock proteins (Hsp23, Hsp70 and Hsp90) during and after larval diapause in the blow fly Lucilia sericata},
	volume = {51},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalDepartment of Bio- and Geosciences, Graduate School of Science, Osaka City University, Sumiyoshi, Osaka 558-8585, Japan.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=15993128},
	pages = {641 - 647},
	abstract = {Genes encoding heat-shock protein 23 (Hsp23), Hsp70 and Hsp90 were cloned from Lucilia sericata to examine whether their expression is related to the regulation of its larval diapause. The level of all three Hsps mRNAs was consistently low irrespective of diapause status. These results indicate that expression of Hsp23, Hsp70 and Hsp90 is not regulated in response to diapause, in contrast to the flesh fly Sarcophaga crassipalpis that shows upregulation of Hsp23 and Hsp70 and downregulation of Hsp90 during its pupal diapause. On the other hand, Hsp90 transcripts were regulated developmentally in nondiapause larvae of L. sericata, i.e., they were at low levels after cessation of feeding but were considerably upregulated a day before pupariation, suggesting that Hsp90 is involved in a developmental process that occurs between the cessation of feeding and pupariation. When diapause larvae were transferred to all of the conditions that terminate diapause and allow postdiapause development, Hsp90 transcripts were promptly upregulated. These results indicate that Hsp90 may serve as an early marker to predict diapause termination in this species.},
	keywords = {Animals, Diptera/*metabolism, Gene Expression Regulation, Developmental/*physiology, Heat-Shock Proteins/*biosynthesis, Hot Temperature, Insect Proteins/*biosynthesis, Larva/metabolism, Photoperiod, Tissue Distribution, Transcription, Genetic/physiology},
	author = {Tachibana, S. and Numata, H. and Goto, S. G.}
}
