@article {386,
	title = {Rapid cold hardening elicits changes in brain protein profiles of the flesh fly, Sarcophaga crassipalpis},
	volume = {17},
	year = {Submitted},
	note = {Rapid cold hardening (RCH) refers to the enhanced cold tolerance acquired by a brief exposure to a moderately low temperature. Although ecological aspects of this response have been well documented in insects, less is known about the physiological and biochemical mechanisms elicited by RCH. In this study we used two-dimensional electrophoresis to detect differences in brain protein abundance in pharate adults of the flesh fly Sarcophaga crassipalpis, in response to a 2 h RCH exposure at 0 degrees C. Fourteen high abundance proteins that responded to RCH were selected for mass spectrometric identification. Three proteins that increased in abundance during RCH included ATP synthase subunit alpha, a small heat shock protein (smHsp), and tropomyosin-1 isoforms 33/34. Eleven proteins that decreased in abundance or were missing following RCH included several proteins involved in energy metabolism, protein degradation, transcription, actin binding, and cytoskeleton organization. That several proteins increased in abundance during RCH underscores the dynamics of the RCH mechanism and suggests that more than one physiological response likely contribute to RCH. The increase in ATP synthase suggests an elevation of ATP during RCH, and the smHsp increase suggests that at least one of the Hsps is actually mobilized during RCH, rather than after RCH as previously assumed01-10-200906-02-2012Normal},
	pages = {565 - 572},
	author = {Li, A. and Denlinger, D. L.}
}
@article {282,
	title = {Neuropeptide-like precursor 4 is uniquely expressed during pupal diapause in the flesh fly},
	volume = {30},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalDepartment of Entomology, Ohio State University, Columbus, OH 43210, USA.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=19007830},
	pages = {518 - 521},
	abstract = {Suppression subtractive hybridization comparing brains from diapausing and nondiapausing pupae of the flesh fly, Sarcophaga crassipalpis, suggested that the gene encoding neuropeptide-like precursor 4 (Nplp4) was uniquely expressed during diapause. We have sequenced the full-length cDNA encoding Nplp4 and used Northern blots to further evaluate linkage to diapause. The open reading frame of this cDNA encodes a 61-amino acid residue precursor protein containing a predicted 18 residue signal peptide, one 22-amino acid and one 2-amino acid propeptides, and a 19-amino acid neuropeptide. The amino acid sequence of the precursor protein shows 64\% identity to Drosophila melanogaster Nplp4; homologues of this precursor protein are not known from species other than these two flies. Nplp4 mRNA levels were quite low in nondiapausing (long day) pupae, but in contrast the gene was highly upregulated in diapausing (short day) pupae. Expression increased at the onset of diapause, remained high throughout diapause, and then decreased 2 days after diapause was terminated. Although the function of this precursor protein and the neuropeptide it yields remain unknown, this close association with diapause suggests a potential role for Nplp4 in initiating and maintaining diapause in the flesh fly.},
	keywords = {Amino Acid Sequence, Animals, Diptera/genetics, Gene Expression Regulation, Developmental, Molecular Sequence Data, Neuropeptides/*genetics, Protein Precursors/*genetics, Pupa/metabolism, Sequence Alignment},
	author = {Li, A. and Rinehart, J. P. 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.}
}
