@article {469,
	title = {High temperature and hexane break pupal diapause in the flesh fly, Sarcophaga crassipalpis, by activating ERK/MAPK},
	volume = {53},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalDepartment of Entomology, Ohio State University, 400 Aronoff Laboratory, 318 West 12th Avenue, Columbus, OH 43210, USA. fujiwara.6@osu.eduenghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=17681525},
	pages = {1276 - 1282},
	abstract = {Pupal diapause in the flesh fly, Sarcophaga crassipalpis, can be terminated by exposure to high temperatures or, artificially, with a topical application of organic solvents. To analyze the molecular mechanisms involved in diapause termination we explored the possibility that the mitogen-activated protein kinases (MAPK) are involved in this response. Levels of phospho-ERK increased within 10 min after hexane application. Extracellular signal-regulated kinase (ERK) was also activated when pupae were transferred from 20 to 25 degrees C, thus suggesting that ERK activation is a likely component of the signal transduction pathway used to initiate development in response to diapause-terminating signals. 20-Hydroxyecdysone and cyclic GMP terminate diapause in this fly, and the juvenile hormone analog methoprene shortens the diapause, but none of these agents activated ERK. ERK was readily activated in isolated abdomens treated with hexane, thus we conclude that ERK is directly activated by the hexane treatment. ERK activation was evident in the brain, epidermis, midgut and fat body, but not in the ventral nerve mass or ring gland, thus suggesting that ERK does not act directly on the ring gland to promote ecdysteroid synthesis but exerts its effect through stimulation of the brain.},
	keywords = {*Hot Temperature, Animals, Cloning, Molecular, Diptera/drug effects/*physiology, DNA, Complementary/genetics, Dose-Response Relationship, Drug, Ecdysterone/pharmacology, Enzyme Activation/drug effects, Extracellular Signal-Regulated MAP Kinases/genetics/*metabolism, Gene Expression Regulation, Hexanes/*pharmacology, Methoprene/pharmacology, Nucleotides, Cyclic/pharmacology, Pupa/drug effects/physiology, Signal Transduction/physiology},
	author = {Fujiwara, Y. and Denlinger, D. L.}
}
@article {284,
	title = {Rapid elevation of Inos and decreases in abundance of other proteins at pupal diapause termination in the flesh fly Sarcophaga crassipalpis},
	volume = {1794},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalDepartment of Entomology, The Ohio State University, Columbus, OH 43210, USA.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=19118649},
	pages = {663 - 668},
	abstract = {We analyzed changes in brain proteins 24 h after pupal diapause termination in Sarcophaga crassipalpis by a combination of 2-dimensional gel electrophoresis and mass spectrometry. The proteome analysis revealed significant changes in 20 proteins, 11 of which represented \&gt;or=2.5-fold changes. Three proteins were present only in the brains of diapausing pupae. Among the most abundant proteins that showed a change, 1 was more abundant, 7 were less abundant, and 2 were absent following diapause termination. The protein that increased in abundance following diapause termination showed highest identity to myo-inositol-1-phosphate synthase (Inos). Proteins that decreased at diapause termination included those showing highest identities to fatty acid binding protein, CG2331-PA, twinstar, catalase, and a histone. Proteins absent at diapause termination included ribosomal protein L17A and one unnamed protein. An increase of Inos protein level was confirmed using Western blot analysis. Attempts to terminate diapause by injection of several Inos-related metabolites failed, thus suggesting that the elevation of Inos at diapause termination is downstream of the physiological regulation that initiates development.},
	keywords = {Adaptation, Physiological, Animals, Brain/metabolism, Databases, Protein, development/*metabolism/physiology, Diptera/*metabolism/physiology, Electrophoresis, Gel, Two-Dimensional, Gene Expression Profiling, Gene Expression Regulation, Inositol/metabolism/pharmacology, Insect Proteins/*metabolism, Mass Spectrometry, Myo-Inositol-1-Phosphate Synthase/*metabolism, Pupa/growth \&amp},
	author = {Li, A. and Michaud, M. R. and Denlinger, D. L.}
}
