Comparison of Active Conformations of the Insectatachykinin/tachykinin and Insect Kinin/Tyr‐W‐MIF‐1 Neuropeptide Family Pairs

Nachman, Ronald J.; Moyna, Guillermo; Williams, Howard J.; Zabrocki, Janusz; Zadina, James E.; Coast, Geoffrey M.; Broeck, Jozef Vanden

doi:10.1111/j.1749-6632.1999.tb07908.x

Cited by 41 publications

(22 citation statements)

References 29 publications

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“…At this time, it is not possible to establish phylogenetic relationships for tachykinins and related peptides. However, several experimental data, such as the ability of SP to activate invertebrate tachykinin receptors, suggest that tachykinins and related peptides also originate from a common, ancestral gene (Nachman et al, 1999;Siviter et al, 2000).…”

Section: Alternative Tachykinin Receptor Usagementioning

confidence: 98%

Tachykinins and tachykinin receptors: a growing family

et al. 2004

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Section: Alternative Tachykinin Receptor Usagementioning

confidence: 98%

Tachykinins and tachykinin receptors: a growing family

et al. 2004

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“…Three of these peptide sequences (TAP-1, TAP-2, and TAP-5) have a C-terminal Gly residue and therefore have the potential to be processed to amidated peptides, as shown in Table I. TAP-5 has a structure at the C terminus similar to a recently isolated tachykinin-related peptide from another dipteran, Stomoxys calcitrans (37). All the other TAPs are novel sequences showing little homology to known bioactive peptides.…”

Section: Identification Of a Tachykinin Prohormone Gene In D Melanogmentioning

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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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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“…Like all vertebrate tachykinins, and a few invertebrate isoforms sequenced from salivary tissues (e.g. eledoisin), these two peptides contain the carboxy (C)-terminal amino acid motif -FXGLMamide, where X represents a variable amino acid (Nachman et al, 1999;Nässel, 1999;Vanden Broeck et al, 1999;Severini et al, 2002). In invertebrates, a plethora of peptides containing the C-terminal amino acid motif -FX I GX II Ramide have been identified and collectively termed tachykinin-related peptides or TRPs (Nachman et al, 1999;Nässel, 1999;Vanden Broeck et al, 1999).…”

mentioning

confidence: 99%

“…eledoisin), these two peptides contain the carboxy (C)-terminal amino acid motif -FXGLMamide, where X represents a variable amino acid (Nachman et al, 1999;Nässel, 1999;Vanden Broeck et al, 1999;Severini et al, 2002). In invertebrates, a plethora of peptides containing the C-terminal amino acid motif -FX I GX II Ramide have been identified and collectively termed tachykinin-related peptides or TRPs (Nachman et al, 1999;Nässel, 1999;Vanden Broeck et al, 1999). Comparisons of sequence homology, tissue distribution, chemical/ conformational requirements for receptor interaction and physiological function suggest a common evolutionary origin for both the vertebrate-and invertebrate-type peptides (Nachman et al, 1999;Nässel, 1999;Vanden Broeck et al, 1999;Severini et al, 2002).…”

mentioning

confidence: 99%

Identification and characterization of a tachykinin-containing neuroendocrine organ in the commissural ganglion of the crabCancer productus

Messinger

Kutz

et al. 2005

Journal of Experimental Biology

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SUMMARY A club-shaped, tachykinin-immunopositive structure first described nearly two decades ago in the commissural ganglion (CoG) of three species of decapod crustaceans has remained enigmatic, as its function is unknown. Here, we use a combination of anatomical, mass spectrometric and electrophysiological techniques to address this issue in the crab Cancer productus. Immunohistochemistry using an antibody to the vertebrate tachykinin substance P shows that a homologous site exists in each CoG of this crab. Confocal microscopy reveals that its structure and organization are similar to those of known neuroendocrine organs. Based on its location in the anterior medial quadrant of the CoG, we have named this structure the anterior commissural organ (ACO). Matrix-assisted laser desorption/ionization Fourier transform mass spectrometry shows that the ACO contains the peptide APSGFLGMRamide,commonly known as Cancer borealis tachykinin-related peptide Ia(CabTRP Ia). Using the same technique, we show that CabTRP Ia is also released into the hemolymph. As no tachykinin-like labeling is seen in any of the other known neuroendocrine sites of this species (i.e. the sinus gland, the pericardial organ and the anterior cardiac plexus), the ACO is a prime candidate to be the source of CabTRP Ia present in the circulatory system. Our electrophysiological studies indicate that one target of hemolymph-borne CabTRP Ia is the foregut musculature. Here, no direct CabTRP Ia innervation is present, yet several gastric mill and pyloric muscles are nonetheless modulated by hormonally relevant concentrations of the peptide. Collectively,our findings show that the C. productus ACO is a neuroendocrine organ providing hormonal CabTRP Ia modulation to the foregut musculature. Homologous structures in other decapods are hypothesized to function similarly.

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Comparison of Active Conformations of the Insectatachykinin/tachykinin and Insect Kinin/Tyr‐W‐MIF‐1 Neuropeptide Family Pairs

Cited by 41 publications

References 29 publications

Tachykinins and tachykinin receptors: a growing family

Tachykinins and tachykinin receptors: a growing family

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

Identification and characterization of a tachykinin-containing neuroendocrine organ in the commissural ganglion of the crabCancer productus

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