Identification and Characterization of Receptors for Ion Transport Peptide (ITP) and ITP-like (ITPL) in the Silkworm Bombyx mori

Nagai, Chiaki; Mabashi-Asazuma, Hideaki; Nagasawa, Hiromichi; Nagata, Shinji

doi:10.1074/jbc.m114.590646

Cited by 67 publications

(75 citation statements)

References 47 publications

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“…It is probably not a coincidence that the tissues which express CHHBP in Eriocheir sinensis are the same as the main target tissues of CHH. Furthermore, in Bombyx mori, expression of the putative ITP receptors BNGR-A2 and BNGR-A34 was restricted to some, but not all of these tissues (Nagai et al, 2014), which is somewhat comparable to the expression profile of CHHBP.…”

Section: Discussionmentioning

confidence: 65%

“…These findings provide evidence that CHH is involved in glycogen metabolism in the hepatopancreas. Recently, Nagai and colleagues found that the Bombyx mori orphan neuropeptide G-protein-coupled receptors BNGR-A2 and BNGR-A34 act as ion transport peptide (ITP) receptors and show that BNGR-A24 is an ITP-like (ITPL) receptor (Nagai et al, 2014). However, in crustaceans, the CHH receptor in the hepatopancreas and downstream signal pathway that mediate these processes remain unidentified (Chung et al, 2010;Webster et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

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CHH binding protein (CHHBP): a newly identified receptor of crustacean hyperglycemic hormone (CHH)

Tian

Zhuang

et al. 2016

Journal of Experimental Biology

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Crustacean hyperglycemic hormone (CHH) is a neurohormone found only in arthropods that plays a pivotal role in the regulation of hemolymph glucose levels, molting and stress responses. Although it was determined that a membrane guanylyl cyclase (GC) acts as the CHH receptor in the Y-organ during ecdysteroidogenesis, the identity of the CHH receptor in the hepatopancreas has not been established. In this study, we identified CHH binding protein (CHHBP), as a potential receptor by screening the annotated unigenes from the transcriptome of Eriocheir sinensis, after removal of the eyestalk. Analysis of the binding affinity between CHH and CHHBP provided direct evidence that CHH interacts with CHHBP in a specific binding mode. Subsequent analysis showed that CHHBP is expressed primarily in the hepatopancreas where it localizes to the cell membrane. In addition, real-time PCR analysis showed that CHHBP transcript levels gradually increase in the hepatopancreas following eyestalk ablation. RNAimediated suppression of CHHBP expression resulted in decreased glucose levels. Furthermore, the reduction of blood glucose induced by CHHBP RNAi reached the same level as that observed in the eyestalk ablation group, suggesting that CHHBP is involved in glucose metabolism regulated by CHH. In addition, compared with the control group, injection of CHH was unable to rescue the decreased glucose levels in CHHBP RNAi crabs. CHH induced transport of 2-NBDG to the outside of cells, with indispensable assistance from CHHBP. Taken together, these findings suggest that CHHBP acts as one type of the primary signal processor of CHH-mediated regulation of cellular glucose metabolism.

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Section: Discussionmentioning

confidence: 65%

Section: Introductionmentioning

confidence: 99%

CHH binding protein (CHHBP): a newly identified receptor of crustacean hyperglycemic hormone (CHH)

Tian

Zhuang

et al. 2016

Journal of Experimental Biology

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“…melanogaster corazonin receptor, isoform A ( AAF49928 [ 72 ]); CCAPR, D . melanogaster crustacean cardioactive peptide receptor ( AAF56536 [ 72 ]); CHHR, Bombyx mori neuropeptide receptor A2 ( BAG68400 [ 76 , 77 ]); DH31R, D . melanogaster diuretic hormone 31 receptor, isoform A ( AAN16138 [ 72 ]); DH44R, D .…”

Section: Resultsmentioning

confidence: 99%

Neuropeptidergic Signaling in the American Lobster Homarus americanus: New Insights from High-Throughput Nucleotide Sequencing

et al. 2015

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Peptides are the largest and most diverse class of molecules used for neurochemical communication, playing key roles in the control of essentially all aspects of physiology and behavior. The American lobster, Homarus americanus, is a crustacean of commercial and biomedical importance; lobster growth and reproduction are under neuropeptidergic control, and portions of the lobster nervous system serve as models for understanding the general principles underlying rhythmic motor behavior (including peptidergic neuromodulation). While a number of neuropeptides have been identified from H. americanus, and the effects of some have been investigated at the cellular/systems levels, little is currently known about the molecular components of neuropeptidergic signaling in the lobster. Here, a H. americanus neural transcriptome was generated and mined for sequences encoding putative peptide precursors and receptors; 35 precursor- and 41 receptor-encoding transcripts were identified. We predicted 194 distinct neuropeptides from the deduced precursor proteins, including members of the adipokinetic hormone-corazonin-like peptide, allatostatin A, allatostatin C, bursicon, CCHamide, corazonin, crustacean cardioactive peptide, crustacean hyperglycemic hormone (CHH), CHH precursor-related peptide, diuretic hormone 31, diuretic hormone 44, eclosion hormone, FLRFamide, GSEFLamide, insulin-like peptide, intocin, leucokinin, myosuppressin, neuroparsin, neuropeptide F, orcokinin, pigment dispersing hormone, proctolin, pyrokinin, SIFamide, sulfakinin and tachykinin-related peptide families. While some of the predicted peptides are known H. americanus isoforms, most are novel identifications, more than doubling the extant lobster neuropeptidome. The deduced receptor proteins are the first descriptions of H. americanus neuropeptide receptors, and include ones for most of the peptide groups mentioned earlier, as well as those for ecdysis-triggering hormone, red pigment concentrating hormone and short neuropeptide F. Multiple receptors were identified for most peptide families. These data represent the most complete description of the molecular underpinnings of peptidergic signaling in H. americanus, and will serve as a foundation for future gene-based studies of neuropeptidergic control in the lobster.

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“…Pyrokinin receptor Pyrokinin and ITP [189,190] Bombyx Tachykinin receptor TK and ITPL [189,191] Drosophila PK-1 receptor Capa-PK (PK-1) and limostatin [192]…”

Section: Bombyxmentioning

confidence: 99%

Recent advances in neuropeptide signaling in Drosophila, from genes to physiology and behavior

Nässel

Zandawala

2019

Preprint

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This review focuses on neuropeptides and peptide hormones, the largest and most diverse class of neuroactive substances, known in Drosophila and other animals to play roles in almost all aspects of daily life, as well as in developmental processes. We provide an update on novel neuropeptides and receptors identified in the last decade, and highlight progress in analysis of neuropeptide signaling in Drosophila. Especially exciting is the huge amount of work published on novel functions of neuropeptides and peptide hormones in Drosophila, largely due to the rapid developments of powerful genetic methods, imaging techniques and innovative assays. We critically discuss the roles of peptides in olfaction, taste, foraging, feeding, clock function/sleep, aggression, mating/reproduction, learning and other behaviors, as well as in regulation of development, growth, metabolic and water homeostasis, stress responses, fecundity, and lifespan. We furthermore provide novel information on neuropeptide distribution and organization of peptidergic systems, as well as the phylogenetic relations between Drosophila neuropeptides and those of other phyla, including mammals. As will be shown, neuropeptide signaling is phylogenetically ancient, and not only are the structures of the peptides, precursors and receptors conserved over evolution, but also many functions of neuropeptide signaling in physiology and behavior.

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Identification and Characterization of Receptors for Ion Transport Peptide (ITP) and ITP-like (ITPL) in the Silkworm Bombyx mori

Cited by 67 publications

References 47 publications

CHH binding protein (CHHBP): a newly identified receptor of crustacean hyperglycemic hormone (CHH)

CHH binding protein (CHHBP): a newly identified receptor of crustacean hyperglycemic hormone (CHH)

Neuropeptidergic Signaling in the American Lobster Homarus americanus: New Insights from High-Throughput Nucleotide Sequencing

Recent advances in neuropeptide signaling in Drosophila, from genes to physiology and behavior

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