The Drosophila hugin gene codes for myostimulatory and ecdysis-modifying neuropeptides

被引:88
作者
Meng, XJ
Wahlström, G
Immonen, T
Kolmer, M
Tirronen, M
Predel, R
Kalkkinen, N
Heino, TI
Sariola, H
Roos, C
机构
[1] Univ Helsinki, Dev Biol Program, Inst Biotechnol, Viikki Bioctr, FIN-00014 Helsinki, Finland
[2] Univ Helsinki, Inst Biomed Dev Biol, Biomed Helsinki, FIN-00014 Helsinki, Finland
[3] Natl Publ Hlth Inst, Dept Mol Med, FIN-00251 Helsinki, Finland
[4] Univ Jena, Inst Allgemeine Zool & Tierphys, D-07743 Jena, Germany
关键词
Drosophila hugin gene; neuropeptides; ecdysis; pyrokinin;
D O I
10.1016/S0925-4773(02)00175-2
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
In a genomic screen we isolated the Drosophila gene hugin (hug, cytology 87C1-2) by cross-hybridisation to a human glial cell line-derived neurotrophic factor cDNA. Upon cDNA sequence analysis and in vitro expression assays, the hugin gene was found to encode a signal peptide containing proprotein that was further processed in Schneider-2 cell s into peptides similar to known neuropeptides. Two of the peptides were similar to FXPRL-amides (pyrokinins) and to the ecdysis-triggering hormone, respectively. The former displayed myostimulatory activity in a bioassay on the cockroach hyperneural muscle preparation, as well as in the Drosophila heart muscle assay. Hugin is expressed during the later half of embryogenesis and during larval stages in a subgroup of neurosecretory cells of the suboesophageal ganglion. Ubiquitous ectopic hugin expression resulted in larval death predominantly at or shortly after ecdysis from second to third instar, suggesting that at least one of the posttranslational cleavage products affects molting of the larva by interfering with the regulation of ecdysis. (C) 2002 Elsevier Science Ireland Ltd. All rights reserved.
引用
收藏
页码:5 / 13
页数:9
相关论文
共 58 条
[1]  
Bailey T L, 1994, Proc Int Conf Intell Syst Mol Biol, V2, P28
[2]  
Baker JD, 1999, J EXP BIOL, V202, P3037
[3]   Neuropeptides and their precursors in the fruitfly, Drosophila melanogaster [J].
Broeck, JV .
PEPTIDES, 2001, 22 (02) :241-254
[4]   Pyrokinin/PBAN-like peptides in the central nervous system of Drosophila melanogaster [J].
Choi, MY ;
Rafaeli, A ;
Jurenka, RA .
CELL AND TISSUE RESEARCH, 2001, 306 (03) :459-465
[5]   A SEQUENCE ASSEMBLY AND EDITING PROGRAM FOR EFFICIENT MANAGEMENT OF LARGE PROJECTS [J].
DEAR, S ;
STADEN, R .
NUCLEIC ACIDS RESEARCH, 1991, 19 (14) :3907-3911
[6]   PROCESSING SPECIFICITY AND BIOSYNTHESIS OF THE DROSOPHILA-MELANOGASTER CONVERTASES DFURIN1, DFURIN1-CRR, DFURIN1-X, AND DFURIN2 [J].
DEBIE, I ;
SAVARIA, D ;
ROEBROEK, AJM ;
DAY, R ;
LAZURE, C ;
VANDEVEN, WJM ;
SEIDAH, NG .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (03) :1020-1028
[7]   A cDNA, from Agrotis ipsilon, that encodes the pheromone biosynthesis activating neuropeptide (PBAN) and other FXPRL peptides [J].
Duportets, L ;
Gadenne, C ;
Couillaud, F .
PEPTIDES, 1999, 20 (08) :899-905
[8]   THE BIOSYNTHESIS OF NEUROPEPTIDES - PEPTIDE ALPHA-AMIDATION [J].
EIPPER, BA ;
STOFFERS, DA ;
MAINS, RE .
ANNUAL REVIEW OF NEUROSCIENCE, 1992, 15 :57-85
[9]  
Ewer J, 1997, J EXP BIOL, V200, P869
[10]  
Freeman MR, 1999, DEVELOPMENT, V126, P4591