@article {541,
	title = {Rapid cold-hardening increases membrane fluidity and cold tolerance of insect cells},
	volume = {52},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalaDepartment of Zoology, Miami University, Oxford, OH 45056, USA. leere@muohio.eduenghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=16626678},
	pages = {459 - 463},
	abstract = {The rapid cold-hardening (RCH) response not only confers dramatic protection against cold-shock (non-freezing) injury, but also "instantaneously" enhances organismal performance. Since cold-shock injury is associated with damage to the cell membrane, we investigated the relationship between RCH and changes in cold tolerance and membrane fluidity at the cellular level. None of the adult flies (Sarcophaga bullata) in the cold-shocked treatment group survived direct transfer to -8 degrees C for 2 h; in contrast, 64.5\% of flies in the RCH group survived exposure to -8 degrees C. Differences between the treatment groups also were reflected at the cellular level; only 21.3\% of fat body cells in the cold-shocked group survived compared to 68.5\% in the RCH group. Using 31P solid-state NMR spectroscopy, we determined that membrane fluidity increased concurrently with rapid cold-hardening of fat body cells. This result suggests that membrane characteristics may be modified very rapidly to protect cells against cold-shock injury.},
	keywords = {*Cold Temperature, *Membrane Fluidity, *Tephritidae, Adaptation, Physiological, Animals, Cell Survival, Fat Body/*cytology, Magnetic Resonance Spectroscopy},
	author = {Lee, R. E., Jr. and Damodaran, K. and Yi, S. X. and Lorigan, G. A.}
}
@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.}
}
