Insect ion transport peptides are derived from alternatively spliced genes and differentially expressed in the central and peripheral nervous system
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Updated: Jun 26, 2026

In vivo Interrogation of Central Nervous System Translatome by Polyribosome Fractionation
Published on: April 30, 2014
1Department of Zoology, Stockholm University, Svante Arrhenius väg 14, 10691 Stockholm, Sweden. dircksen@zoologi.su.se
Abstract:
Insect ionic and fluid homeostasis relies upon the Malpighian tubules (MT) and different hindgut compartments. Primary urine formed in MTs is finally modified by ion, solute and water reabsorptive processes primarily in the hindgut under the control of several large peptide hormones. One of these, the ion transport peptide (ITP), is a chloride transport-stimulating and acid secretion-inhibiting hormone similar to crustacean hyperglycaemic hormones (CHHs). In locusts, moths and fruit flies, ITP together with the slightly longer ITPL isoforms, inactive in hindgut bioassays, arise by alternative splicing from very similar itp genes. ITP and ITPL are differentially distributed in (1) pars lateralis/retrocerebral complex neurosecretory cells (NSCs) containing both splice forms, (2) interneurons with either one of the splice forms, (3) hindgut-innervating abdominal ITP neurons (in Drosophila only), and (4) intrinsic, putative sensory NSCs in peripheral neurohaemal perisympathetic/perivisceral organs or transverse nerves (usually containing ITPL). Both splice forms occur as hormones released into the haemolymph in response to feeding or stress stimuli. ITPL mainly released from the peripheral NSCs is discussed as a competitive inhibitor (as established in vitro) of ITP action on yet to be identified hindgut ITP receptors. Furthermore, some evidence has been provided for possible ecdysis-related functions of ITP and/or ITPL in moths. The comparative data on the highly similar gene, precursor and primary structures and similar differential distributions in insect and crustacean NSCs suggest that CHH/ITP and ITPL neuropeptide-producing cells and their gene products share common phylogenetic ancestry.
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