@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 {765,
	title = {Comparison of the effects of pyrokinins and related peptides identified from arthropods on pupariation behaviour in flesh fly (Sarcophaga bullata) larvae (Diptera: Sarcophagidae)},
	volume = {50},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalInstitute of Organic Chemistry and Biochemistry, Academy of Sciences, Flemingovo nam. 2, 166 10 Prague 6, Czech Republic. zdarek@uochb.cas.czenghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=15019526},
	pages = {233 - 239},
	abstract = {Peptides from the pyrokinin/PBAN family and some structurally related compounds identified in various arthropods were tested for acceleration of puparial contraction in flesh fly larvae. Modifications of behavioural patterns of pupariation were further studied for the active compounds using a behavioural analysis based on the recording of changes in tension of the cuticle. Nine peptides belonging to the pyrokinin/PBAN family (Lem-PK, Pea-PK-5, Lom-PK II, Hez-PBAN, Bom-DH-I), identified in five different insect species, two pyrokinin peptides derived from the genome of Drosophila melanogaster (capa-3, and hugin), and two pyrokinins identified from the white shrimp Penaeus vannamei were very active in the pupariation assay, with threshold doses within the range of 0.1-5.0 pmol larva(-1). High activity was also detected for a related peptide ETH1 from Drosophila. All of these peptides share a C-terminal PRLamide, which is essential and sufficient for the activity. Interestingly, two other structurally related peptides from Drosophila--ETH2 and capa-1--which feature conservative changes (Ile and Val, respectively) at the C-terminal Leu position, were inactive within a physiological range of concentrations. It is clear that the receptor mediating the acceleration of puparial contraction behaviour is sensitive to the introduction of greater steric bulk at the C-terminal Leu position. The peptides that accelerated pupariation showed very similar patterns of muscular and cuticular activity.},
	keywords = {Animals, Arthropods/chemistry, Biological Factors/analysis/physiology, development, Diptera/drug effects/*growth \&amp, Insect Hormones/*physiology, Insect Proteins/analysis/*physiology, Metamorphosis, Biological/drug effects/*physiology, Neuropeptides/classification/*physiology, Pupa/drug effects/growth \&amp},
	author = {Zd{\textquoteright}arek, J. and Verleyen, P. and Mares, M. and Doleckova, L. and Nachman, R. J.}
}
@article {652,
	title = {Involvement of EDTP, an egg-derived tyrosine phosphatase, in the early development of Drosophila melanogaster},
	volume = {138},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalGraduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Bunkyo-ku, Tokyo 113-0033. shinji-y@pharm.teikyo-u.ac.jpeng SI  - GENBANK/AB036800http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=16428301},
	pages = {721 - 728},
	abstract = {Previously, we purified a novel protein tyrosine phosphatase from eggs of the flesh fly, Sarcophaga peregrina. This protein tyrosine phosphatase, named egg-derived tyrosine phosphatase (EDTP), is expressed during oogenesis and early embryogenesis but is rapidly degraded in middle embryogenesis by lysosomal cathepsin L. Here, we demonstrate the requirement of EDTP in the development of the fruit fly, Drosophila melanogaster. Deletion of the Drosophila EDTP gene using transposase-catalyzed imprecise excision resulted in homozygous lethals during embryogenesis. Additionally, germline clones generated using the FLP-FRT-ovo(D) system showed severe defects in ovarian development during oogenesis. These results indicate that the Drosophila EDTP gene is crucial in oogenesis and embryogenesis.},
	keywords = {Animals, development, Drosophila melanogaster/*enzymology/growth \&amp, Drosophila Proteins/*physiology, Embryonic Development, Molecular Sequence Data, Mutation, Oogenesis, Protein Tyrosine Phosphatases/*physiology},
	author = {Yamaguchi, S. and Katagiri, S. and Sekimizu, K. and Natori, S. and Homma, K. J.}
}
@article {466,
	title = {Characterisation of functional and insecticidal properties of a recombinant cathepsin L-like proteinase from flesh fly (Sarcophaga peregrina), which plays a role in differentiation of imaginal discs},
	volume = {37},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalSchool of Biological and Biomedical Sciences, Durham University, South Road, Durham, UK.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=17517336},
	pages = {589 - 600},
	abstract = {ScathL is a cathepsin L-like cysteine proteinase from Sarcophaga peregrina (flesh fly), which is involved in differentiation of imaginal discs, through proteolysis of components of basement membranes. An expression system based on the methylotrophic yeast Pichia pastoris was used to produce recombinant ScathL. Although the expression construct contained the full proprotein coding sequence for ScathL, the proprotein was only detected in culture supernatant at early stages of expression by Western blotting. The purified recombinant protein contained only a polypeptide similar to mature ScathL, as a result of autocatalytic processing. After activation by reducing agents, the enzyme hydrolysed the cathepsin L substrate Z-Phe-Arg-AMC, with optimal activity at pH 5.5. ScathL showed decreasing activity with increasing ionic strength above 0.3M NaCl, and lost activity irreversibly at pH \&gt; or = 7.5. The enzyme showed limited activity towards protein substrates, digesting only to large fragments. ScathL was insecticidal towards larvae of the tomato moth, Lacanobia oleracera, following injection into the haemolymph. It caused melanisation, although no evidence of extensive proteolysis in haemolymph or gut was observed. Production of a inactive mutant form of ScathL showed that enzyme activity was necessary for the complete proprotein processing observed during production as a recombinant protein, and for insecticidal activity.},
	keywords = {Amino Acid Sequence, Animals, Cysteine Endopeptidases/genetics/isolation \&amp, development, Diptera/*enzymology/growth \&amp, Enzyme Activation, Hemolymph/metabolism, Hydrogen-Ion Concentration, Insecticides/pharmacology, Larva/drug effects, Lepidoptera/drug effects, Mutation, Pichia/genetics, purification/*metabolism/pharmacology, purification/metabolism/pharmacology, Recombinant Proteins/genetics/isolation \&amp, Salts/metabolism},
	author = {Philip, J. M. and Fitches, E. and Harrison, R. L. and Bonning, B. and Gatehouse, J. A.}
}
@article {468,
	title = {Purification of a cysteine protease inhibitor from larval hemolymph of the tobacco hornworm (Manduca sexta) and functional expression of the recombinant protein},
	volume = {37},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalLaboratory of Food Molecular Functionality, College of Agriculture, Ibaraki University, 3-21-1 Chuo, Ami-machi, Inashiki-gun, Ibaraki 300-0393, Japan.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=17681235},
	pages = {960 - 968},
	abstract = {A cysteine protease inhibitor (CPI) with an apparent molecular mass of 11.5kDa was purified from larval hemolymph of the tobacco hornworm (Manduca sexta) by gel filtration on Sephadex G-50 followed by hydrophobic and ion-exchange column chromatographies. The purified cysteine proteinase inhibitor, denoted as MsCPI, strongly inhibited the plant cysteine protease, papain, with a K(i) value of 5.5 x 10(-9)M. Nucleotide sequence analysis of a partial cDNA encoding MsCPI indicated that MsCPI consists of 105 amino acid residues in a sequence that is similar to sarcocystatin A from Sarcophaga peregrina. However, northern blotting and PCR analyses using the specific primers of MsCPI suggested that the mRNA encoding MsCPI had a size of more than 12 kilobases, which included at least six tandemly repeated MsCPI segments. MsCPI was expressed in Escherichia coli and the recombinant protein effectively inhibited cysteine proteases from plants as well as from animals such as cathepsins B (K(i), 6.8 nM), H (3.0 nM), and L (0.87 nM). There was no inhibition exhibited toward trypsin, chymotrypsin, subtilisin, pepsin or themolysin.},
	keywords = {Amino Acid Sequence, Animals, Cathepsins/drug effects/isolation \&amp, Cloning, Molecular, Conserved Sequence, Cysteine Proteinase Inhibitors/genetics/*isolation \&amp, development, DNA Primers, Escherichia coli/genetics, Hemolymph/*chemistry, Humans, inhibitors, Larva, Manduca/*growth \&amp, Molecular Sequence Data, Papain/antagonists \&amp, Polymerase Chain Reaction, purification/metabolism, purification/pharmacology, Recombinant Proteins/isolation \&amp, Sequence Alignment, Sequence Homology, Amino Acid},
	author = {Miyaji, T. and Kouzuma, Y. and Yaguchi, J. and Matsumoto, R. and Kanost, M. R. and Kramer, K. J. and Yonekura, M.}
}
@article {363,
	title = {Diapause hormone in the corn earworm, Helicoverpa zea: optimum temperature for activity, structure-activity relationships, and efficacy in accelerating flesh fly pupariation},
	volume = {29},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalDepartment of Entomology, Ohio State University, 318 West 12th Avenue, Columbus, OH 43210, USA.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=18206265},
	pages = {196 - 205},
	abstract = {Diapause hormone (DH) effectively terminated pupal diapause in Helicoverpa zea. This effect was temperature-dependent, with an optimum of 21 degrees C. The dose-response curve indicated an ED50 of DH for diapause termination of approximately 100 pmol. The core sequence and essential amino acids were determined by bioassays using modified and truncated DH analogs. A C-terminal hepta-peptide, LWFGPRLa, was the core sequence required for diapause termination. Activity was lost when Alanine was substituted for any of the amino acids in the hepta-peptide, with the exception of Glycine. A fragment series of analogs suggested that the amide and Arginine were the most important components needed for terminating diapause. Leucine, Tryptophan, and Phenylalanine at the N-terminus of the hepta-peptide were also critical for activity. The C-terminal Leucine was less important: deletion resulted in decreased activity, although it could not be substituted by Alanine. The fact that a portion of the DH sequence is similar to the pyrokinin that accelerates fly pupariation prompted us to also evaluate the capability of DH to accelerate development in the flesh fly, Sarcophaga bullata. The threshold dose of DH essential to accelerate fly pupariation was 5 pmol for immobilization/retraction and longitudinal contraction and 10 pmol for tanning, approximately one or two orders of magnitude lower than the effective dose required for diapause termination in H. zea. Tensiometric measurements revealed that DH affected neuromuscular patterns of pupariation behavior and associated cuticular changes in a manner similar to that of the fly pyrokinins and their analogs.},
	keywords = {*Temperature, Amino Acid Substitution, Animals, development, Diptera/*growth \&amp, Dose-Response Relationship, Drug, Larva/drug effects/growth \&amp, Lepidoptera/*growth \&amp, Muscle Contraction/drug effects, Neuropeptides/chemistry/*pharmacology, Peptide Fragments/pharmacology, Pupa/drug effects/growth \&amp, Structure-Activity Relationship},
	author = {Zhang, Q. and Zd{\textquoteright}arek, J. and Nachman, R. J. and Denlinger, D. L.}
}
@article {364,
	title = {A case of myiasis in a patient with psoriasis from Turkey},
	volume = {57},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalEge University Faculty of Medicine Department of Parasitology, Izmir, Turkey. hande.dagci@ege.edu.trenghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=18243777},
	pages = {239 - 241},
	abstract = {Myiasis infestations caused by the larvae of flies mostly belonging to Cyclorapha suborders are frequently encountered in Turkey, which is located in the subtropical zone. The skin is a common site for myiasis, and the infestations are likely to develop in infected tissues and poorly attended wounds of the skin. The case, a 30-year-old male patient, was diagnosed with psoriasis 18 years ago. He had psoriatic scales on his right big toe and was receiving corticosteroid and immunosuppressive drugs. A total of 11 fly larvae were removed from the infected right first toe of the patient. Structures of the stigmas seen in the cross-sections taken from the final segments of these larvae were examined and determined as Sarcophaga spp. larvae. Patients with infected tissues should be extremely cautious about their wound hygiene and take required fly control measures especially during summer as flies can find a suitable environment for sustenance.},
	keywords = {Adult, Animals, Arthritis, Psoriatic/*complications, development, Diptera/growth \&amp, Humans, Larva/growth \&amp, Male, Myiasis/*complications/parasitology/pathology, Skin Diseases, Parasitic/*complications/parasitology/pathology, Toes/*parasitology/pathology, Turkey},
	author = {Dagci, H. and Zeyrek, F. and Gerzile, Y. K. and Sahin, S. B. and Yagci, S. and Uner, A.}
}
@article {280,
	title = {Mendelian inheritance of pupal diapause in the flesh fly, Sarcophaga bullata},
	volume = {100},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalDepartment of Entomology, The Ohio State University, 318 West 12th Avenue, Columbus, OH 43210, USA.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=18836144},
	pages = {251 - 255},
	abstract = {Pupal diapause (dormancy) in the flesh fly, Sarcophaga bullata, is induced by short-day photoperiods and low temperature. In this study, the inheritance mode of diapause was investigated by crossing a nondiapausing (nd) strain of S. bullata with 2 diapausing strains having different diapause capacities. The results consistently indicated that diapause incidence is inherited in a simple Mendelian pattern, thus a single gene or a small gene cluster linked to the photoperiodic clock controls the seasonal response of diapause. The fact that the nd strain lacked daily rhythmicity in adult eclosion and showed altered expression of 2 circadian clock genes suggests that the photoperiodic and circadian clocks are related through a shared molecular component in S. bullata.},
	keywords = {Animals, Crosses, Genetic, development, Diptera/*genetics/*growth \&amp, Female, Inheritance Patterns/*genetics, Linkage (Genetics), Male, Metamorphosis, Biological/*genetics/physiology, Models, Genetic},
	author = {Han, B. and Denlinger, D. L.}
}
@article {289,
	title = {Preparation and preliminary biological screening of cholic acid-juvenoid conjugates},
	volume = {74},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalInstitute of Experimental Botany, Academy of Sciences of the Czech Republic, Prague, Czech Republic. jurcek@ueb.cas.czenghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=19394354},
	pages = {779 - 785},
	abstract = {Steroidal compounds have been utilized as carriers and for modification of physico-chemical properties of model biologically active secondary alcohols - juvenoids. Juvenoids are juvenile hormone analogues - environmentally safe insecticides, possessing significant biological activity towards different arthropods groups in focus on insect pest species. Structure modification of juvenoids plays important role to control the rate of liberation and decomposition of juvenoid in digestive system and can also play important role in the mode of action towards selected insect. This study presents an approach to the synthesis of steroidal monomers and dimers carrying one and two molecules of a juvenoid in their structures. The prepared compounds were tested for their inhibition activity on reproduction of the blowfly Neobellieria (Sarcophaga) bullata. These steroid-juvenoid conjugates showed promising possibilities in synthesis of new unique biochemical insecticides. Preliminary biological test results of prepared compounds are presented.},
	keywords = {Animals, Cell Proliferation/drug effects, Cholic Acid/*chemistry, development, Dimerization, Diptera/cytology/drug effects/growth \&amp, Epithelial Cells/cytology/drug effects, Female, Juvenile Hormones/*chemical synthesis/chemistry/*pharmacology, Larva/drug effects/growth \&amp, Male, Pesticides/*chemical synthesis/chemistry/*pharmacology, Reproduction/drug effects},
	author = {Jurcek, O. and Wimmer, Z. and Svobodova, H. and Bennettova, B. and Kolehmainen, E. and Drasar, P.}
}
