Insect tachykinin-related neuropeptides: Developmental changes in expression of callitachykinin isoforms in the central nervous system and intestine of the blowfly,Calliphora vomitoria

Kim, Min-Yung; Muren, J. Eric; Lundquist, C. Tomas; Nässel, Dick R.

doi:10.1002/(sici)1520-6327(1997)34:4<475::aid-arch6>3.0.co;2-r

Cited by 8 publications

(5 citation statements)

References 28 publications

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“…By comparison, the blowfly displays a larger number of LTK-LI neurons both in the brain and ventral nerve cord (30). The distribution of LTK-LI cells in the larval and adult midgut of Drosophila is very similar to that revealed in the blowfly Calliphora (47). In both fly species, the larval endocrine cells are fewer but substantially larger than their adult counterparts.…”

Section: Biological Activity Of the Drosophila Tachykinins-three Of Tmentioning

confidence: 99%

Expression and Functional Characterization of aDrosophila Neuropeptide Precursor with Homology to Mammalian Preprotachykinin A

Siviter¹,

Coast²,

Winther³

et al. 2000

Journal of Biological Chemistry

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141

166

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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 tachykininrelated 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 tachykininrelated 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.Substance P was the first peptide signaling molecule to be identified by virtue of its effects upon blood pressure and smooth muscle contraction (1) and is the archetypal member of the tachykinin family of peptides. Vertebrate tachykinins represent a large family of peptides that elicit a wide range of both central and peripheral responses (2-5). Although these peptides are structurally diverse, all contain a conserved C-terminal FXGLM-amide motif. Like other biologically active peptides, substance P is derived from a larger prohormone polypeptide (preprotachykinin A (PPT-A) 1 ) that also allows the production of several other biologically active peptides (neurokinin A, neuropeptide K, and neuropeptide ␥) (6). Three different isoforms of preprotachykinin can be produced as a result of alternative splicing of the PPT-A mRNA, which, in conjunction with alternative post-translational processing of the prohormone, allows the production of these peptides in a tissue-specific manner (7-9). A fifth mammalian tachykinin, neurokinin B, is derived from a separate gene product, preprotachykinin B (10).The tachykinin family is not confined to vertebrates, and a large number of tachykinins have now been isolated from a variety of invertebrate species such as the cockroach Leucophaea maderae (11, 12), the mosquito Culex salinarius (13), and the echiuroid worm Urechis unicinctus (14). In contrast to the vertebrate tachykinins, almost all of the invertebrate tachykinins contain a conserved C-terminal FXGXR-amide motif and, for this reason, have been termed tachykinin-related peptides (TRPs). Not...

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Section: Biological Activity Of the Drosophila Tachykinins-three Of Tmentioning

confidence: 99%

Expression and Functional Characterization of aDrosophila Neuropeptide Precursor with Homology to Mammalian Preprotachykinin A

Siviter¹,

Coast²,

Winther³

et al. 2000

Journal of Biological Chemistry

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141

166

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“…All of these seem to be colocalized in a small set of protocerebral neurons innervating the glandular lobe of the locust corpora cardiaca , but other cell systems have not yet been assayed. The two known isoforms of blowfly TRPs, callitachykinin-I and II, were found to be expressed in equimolar ratios in different parts of the nervous system and the midgut of Calliphora vomitoria and are likely to be colocalized in neurons and endocrine cells (Nä ssel et al, 1995;Kim et al, 1997). Hence, the recent findings are the first indications of differential distribution of TRP isoforms in invertebrates.…”

Section: Discussionmentioning

confidence: 94%

“…We know from immunocytochemistry with an antiserum to the locust TRP locustatachykinin-I (LomTK-I), which recognizes the conserved C-terminus of the known invertebrate TRPs (Lundquist et al, 1994;Nä ssel, 1996a,b, 1997;Christie et al, 1997;Kim et al, 1997), that both neuronal processes and endocrine cells of the midgut contain TRP-like material (Muren et al, 1995). It may be assumed that most, if not all, the known LemTRPs were detected in the midgut by immunocytochemistry with this antiserum.…”

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confidence: 99%

Differential distribution of isoforms ofLeucophaea tachykinin-related peptides (LemTRPs) in endocrine cells and neuronal processes of the cockroach midgut

et al. 1999

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“…Some FaRPs are potent inhibitors of proctolin-induced midgut motility (Lange and Orchard 1998). Other peptides expressed by gut endocrine cells in insects, for example the tachykinin-related peptides of Leucophaea maderae, induce spontaneous contractions of the hindgut (Winther et al 1998;Nässel 1999), and changes in immunoreactive (RIA) contents of the gut have been reported in Calliphora vomitoria larval and adult stages (Kim et al 1997). Indeed, more than 40 "kinin" peptides have been reported to stimulate hindgut activity (Schoofs et al 1994(Schoofs et al , 1997Nässel 1999) and, in many instances, Malpighian tubule secretion in insects (reviewed by Coast 1998).…”

Section: Introductionmentioning

confidence: 99%

Endocrine cells in the gut of the shore crab Carcinus maenas immunoreactive to crustacean hyperglycaemic hormone and its precursor-related peptide

Webster¹,

Dircksen²,

Chung³

2000

Cell and Tissue Research

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The distribution and morphology of gut endocrine cells, which are immunoreactive to crustacean hyperglycaemic hormone (CHH) and the corresponding precursor-related peptide (CPRP), have been described in the shore crab Carcinus maenas. The cells are uniquely distributed throughout the fore- and hindgut, but were never observed in the midgut or associated caeca. Expression of CHH and CPRP in the gut endocrine cells is generally restricted to premoult, although small numbers of immunoreactive cells were observed in intermoult and postmoult. A notable feature of the distribution of these slender cells was that, whilst they are distributed evenly over much of the fore- and hindgut, all extrinsic and intrinsic muscles of the gastric and pyloric stomach examined were surrounded by a ring(s) of cells, suggesting a mechanoreceptive function. Ultrastructural studies revealed that these cells contain numerous immunopositive, electron-dense granules. This suggests that they are "paraneurones", which secrete CHH and CPRP into the haemolymph during ecdysis, accounting for the ecdysial surge in CHH, which is implicated in water uptake and swelling prior to ecdysis.

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Insect tachykinin-related neuropeptides: Developmental changes in expression of callitachykinin isoforms in the central nervous system and intestine of the blowfly,Calliphora vomitoria

Cited by 8 publications

References 28 publications

Expression and Functional Characterization of aDrosophila Neuropeptide Precursor with Homology to Mammalian Preprotachykinin A

Expression and Functional Characterization of aDrosophila Neuropeptide Precursor with Homology to Mammalian Preprotachykinin A

Differential distribution of isoforms ofLeucophaea tachykinin-related peptides (LemTRPs) in endocrine cells and neuronal processes of the cockroach midgut

Endocrine cells in the gut of the shore crab Carcinus maenas immunoreactive to crustacean hyperglycaemic hormone and its precursor-related peptide

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