Lancaster EPrints

Expression and functional characterisation of a Drosophila neuropeptide precursor with homology to mammalian preprotachykinin.

Siviter, Richard J. and Coast, Geoffrey M. and Winther, Åsa M. and Nachman, Ronald J. and Taylor, C. A. M. and Shirras, Alan D. and Coates, David and Isaac, R. Elwyn and Nässel, Dick R. (2000) Expression and functional characterisation of a Drosophila neuropeptide precursor with homology to mammalian preprotachykinin. Journal of Biological Chemistry, 275 (30). pp. 23273-23280. ISSN 1083-351X

Full text not available from this repository.

Abstract

Peptides structurally related to mammalian tachykinins have recently been isolated from the brain and intestine of several insect species, where they are believed to function as both neuromodulators and hormones. Further evidence for the signaling role of insect tachykinin-related peptides was provided by the cloning and characterization of cDNAs for two tachykinin receptors from Drosophila melanogaster. However, no endogenous ligand has been isolated for the Drosophila tachykinin receptors to date. Analysis of the Drosophila genome allowed us to identify a putative tachykinin-related peptide prohormone (prepro-DTK) gene. A 1.5-kilobase pair cDNA amplified from a Drosophila head cDNA library contained an 870-base pair open reading frame, which encodes five novel Drosophila tachykinin-related peptides (called DTK peptides) with conserved C-terminal FXGXR-amide motifs common to other insect tachykinin-related peptides. The tachykinin-related peptide prohormone gene (Dtk) is both expressed and post-translationally processed in larval and adult midgut endocrine cells and in the central nervous system, with midgut expression starting at stage 17 of embryogenesis. The predicted Drosophila tachykinin peptides have potent stimulatory effects on the contractions of insect gut. These data provide additional evidence for the conservation of both the structure and function of the tachykinin peptides in the brain and gut during the course of evolution.

Item Type: Article
Journal or Publication Title: Journal of Biological Chemistry
Subjects: Q Science > QH Natural history > QH301 Biology
Departments: Faculty of Health and Medicine > Biomedical & Life Sciences
Faculty of Science and Technology > Lancaster Environment Centre
ID Code: 9347
Deposited By: Dr Alan Shirras
Deposited On: 05 Jun 2008 11:29
Refereed?: Yes
Published?: Published
Last Modified: 09 Apr 2014 22:16
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/9347

Actions (login required)

View Item