@article {886,
	title = {Identification and purification of sulfotransferases for 20-hydroxysteroid from the larval fat body of a fleshfly, Sarcophaga peregrina},
	volume = {67},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalKyoritsu College of Pharmacy, Minato-ku, Tokyo 105-8512, Japan.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=12951514},
	pages = {1780 - 1785},
	abstract = {Sulfotransferase (ST) activity for 20-hydroxyecdysone (20E) was identified in a larval fat body lysate of the fleshfly, Sarcophaga peregrina, but not in the hemolymph. The activity was highly sensitive to 2,6-dichloro-4-nitrophenol (DCNP) (IC50=0.61 microM), a specific inhibitor of phenol ST (P-ST), but insensitive to triethylamine, a hydroxysteroid ST inhibitor. These results suggest that 20E-specific ST enzymes belong to the P-ST family, despite the fact that 20E is a hydroxysteroid. In addition to 20E ST activity, a relatively high level of 2-naphthol ST activity was detected in the fat body lysate. The ST activity for both substrates transiently decreased to the 50\% of maximal levels, 6 hrs after induction of pupation. The ST enzymes were separated on a DEAE-cellulose column. The 20E-ST enzymes were eluted around 50 mM KCl as two separate peaks of close proximity and the P-ST was eluted at 0.1 M KCl. The 20E ST enzymes were further purified using 3{\textquoteright}-phosphoadenosine 5{\textquoteright}-phosphate (PAP)-agarose affinity column chromatography. Both of the eluted active fractions demonstrated 43-kDa proteins on SDS-polyacrylamide gel. Photoaffinity labeling with [35S]-3{\textquoteright}-phosphoadenosine 5{\textquoteright}-phosphosulfate (PAPS) showed 43-kDa bands in the fat body lysate, as well as in the purified fractions. These results suggest that the 43-kDa proteins catalyze 20E sulfation within the fat body of S. peregrina.},
	keywords = {Adenosine Diphosphate/pharmacology, Animals, Chromatography, DEAE-Cellulose, derivatives/metabolism, development, Diptera/*enzymology/growth \&amp, Ecdysterone/antagonists \&amp, Enzyme Inhibitors/chemistry/pharmacology, Fat Body/chemistry/*enzymology, Hemolymph/metabolism, inhibitors/*chemistry/isolation \&amp, inhibitors/isolation \&amp, Larva/chemistry/enzymology, Naphthols/isolation \&amp, Nitrophenols/pharmacology, Phosphoadenosine Phosphosulfate/analogs \&amp, Photoaffinity Labels/chemistry/metabolism, Pupa/metabolism, purification/*metabolism, purification/metabolism, Sulfates/metabolism, Sulfotransferases/antagonists \&amp, Sulfur Radioisotopes},
	author = {Matsumoto, E. and Matsui, M. and Tamura, H. O.}
}
@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.}
}
