Lepidopteran Peptides of the Allatostatin Superfamily

Duve, Hanne; Johnsen, Anders H.; Maestro, José L.; Scott, Alan G.; Winstanley, Doreen; Davey, Marlene; East, Peter D.; Thorpe, Alan

doi:10.1016/s0196-9781(97)00188-5

Cited by 70 publications

(61 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition, the peptide ARGYDFGL-NH 2 , which was isolated from C. pomonella (Duve et al, 1997b) and is closely related to helicostatin 5 (ARAYDFGL-NH 2 ), also was used (see Table 1). Allatotropin (98% purity) was purchased from Sigma (St. Louis, MO).…”

Section: Peptidesmentioning

confidence: 99%

“…Furthermore, this peptide was identified from tissue extracts of fifth-instar larvae of C. pomonella, and, significantly, it was shown to inhibit all visible forms of spontaneous contractile activity of the foregut (Duve et al, 1997a). Subsequently, several other family members of the allatostatin superfamily have been isolated and identified from extracts of whole larvae of C. pomonella and also of the noctuid moth Helicoverpa armigera (Duve et al, 1997b), from which latter species the allatostatin gene also has been identified (Davey, 1997;Davey et al, 1999). In situ hybridisation studies on H. armigera supported the immunocytochemical findings in C. pomonella by showing that the allatostatin gene is expressed in four neurones of the frontal ganglion (Davey, 1997).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Regulation of lepidopteran foregut movement by allatostatins and allatotropin from the frontal ganglion

1999

Self Cite

View full text Add to dashboard Cite

Section: Peptidesmentioning

confidence: 99%

mentioning

confidence: 99%

Regulation of lepidopteran foregut movement by allatostatins and allatotropin from the frontal ganglion

1999

Self Cite

View full text Add to dashboard Cite

“…Matrix-assisted laser desorption/ ionization-Fourier transform mass spectrometry identified the peptides responsible for the immunoreactivities as GYRKPPFNGSIFamide (Gly hemolymph circulation, digestion and water and ion transport (e.g. Duve et al, 1994;Lee et al, 1998;Zudaire et al, 1998;Winther and Nässel, 2001). Although crustaceans are closely related to insects, and neuroendocrine regulation is an important component of control systems in both taxa, the endocrine role of the gut epithelium has not been widely studied in crustaceans (Mykles, 1979;Chung et al, 1999;Webster et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Midgut epithelial endocrine cells are a rich source of the neuropeptides APSGFLGMRamide (Cancer borealis tachykinin-related peptide Ia) and GYRKPPFNGSIFamide (Gly1-SIFamide) in the crabs Cancer borealis, Cancer magister and Cancer productus

Christie

Kutz-Naber

Stemmler

et al. 2007

Journal of Experimental Biology

View full text Add to dashboard Cite

-SIFamide) and APSGFLGMRamide [Cancer borealis tachykinin-related peptide Ia (CabTRP Ia)], respectively, both of which are known neuropeptides of Cancer species. Although the function of these midgut-derived peptides remains unknown, we found that both Gly 1 -SIFamide and CabTRP Ia were released when the midgut was exposed to highpotassium saline. In addition, CabTRP Ia was detectable in the hemolymph of crabs that had been held without food for several days, but not in that of fed animals, paralleling results that were attributed to TRP release from midgut endocrine cells in insects. Thus, one function that midgutderived CabTRP Ia may play in Cancer species is paracrine/hormonal control of feeding-related behavior, as has been postulated for TRPs released from homologous cells in insects.

show abstract

“…The elongated form, bostatin-2, is identical to the moth peptides helicostatin-2, and cydiastatin-2 (21), the cockroach peptide Dippu-AST-2 (22), and only one amino acid residue different (Ser-3 3 Thr-3) from the locust peptide Scg-AST-2 (23), and the honey bee peptide Apime-AST (12). Bostatin-4 is identical to the moth peptides helicostatin-4 and cydiastatin-4 and to an A-type allatostatin isolated or identified from locusts, flies, and cockroaches (10,12,21,23,24). All other bostatins are novel peptide structures.…”

Section: Resultsmentioning

confidence: 99%

Molecular Cloning of a Functional Allatostatin Gut/Brain Receptor and an Allatostatin Preprohormone from the Silkworm Bombyx mori

Secher

Lenz

Cazzamali

et al. 2001

Journal of Biological Chemistry

View full text Add to dashboard Cite

The cockroach-type or A-type allatostatins are inhibitory insect neuropeptides with the C-terminal sequence Tyr/Phe-X-Phe-Gly-Leu-NH 2 . Here, we have cloned an A-type allatostatin receptor from the silkworm Bombyx mori (BAR). BAR is 361 amino acid residues long, has seven transmembrane domains, shows 60% amino acid residue identity with the first Drosophila allatostatin receptor (DAR-1), and 48% identity with the second Drosophila allatostatin receptor (DAR-2). The BAR gene has two introns and three exons. These two introns coincide with and have the same intron phasing as two introns in the DAR-1 and DAR-2 genes, showing that the three receptors are not only structurally but also evolutionarily related. Furthermore, we have cloned a Bombyx allatostatin preprohormone that contains eight different Atype allatostatins. Chinese hamster ovary cells permanently transfected with BAR DNA react on the addition of 4 ؋ 10 ؊9 M Bombyx A-type allatostatins with a second messenger cascade (measured as bioluminescence), showing that BAR is a functional A-type allatostatin receptor. Southern blots suggest that Bombyx has at least one other BAR-related gene in addition to the BAR gene described in this paper. Northern blots and quantitative reverse transcriptase-polymerase chain reaction of different larval tissues show that BAR mRNA is mainly expressed in the gut and to a much lesser extent in the brain. To our knowledge, this is the first report on the molecular cloning and functional expression of an insect gut/brain peptide hormone receptor.Insects constitute a large group of animals (more than 70% of all animal species are insects) and are ecologically and economically extremely important, because most flowering plants depend on insects for their pollination (honeybees alone pollinate 20 billion dollars worth of crop yearly in the United States). But insects can also be severe pests in agriculture, destroying 30% of our potential annual harvest, and can be vectors for major diseases such as malaria, sleeping disease, and yellow fever. Despite the importance of insects, however, their molecular endocrinology is not well understood. This will certainly change after the recent publication of the Drosophila genome (1, 2), which represents a breakthrough for our understanding of virtually all aspects of insects. For the insect molecular endocrinology field, e.g. one can anticipate that the major future advances will occur by "mining" of the "Drosophila Genome Project" data base and cloning of important key proteins involved in insect endocrinology (3-9).Although most initial findings will be made in Drosophila, one can expect that these discoveries also will have their impacts on our understanding of the molecular endocrinology of other insects. Although Drosophila offers many important advantages for studying the molecular biology and genetics of an insect (a sequenced genome; the presence of numerous mutants, including knock-out mutants (7); and the possibility of creating transgenic animals), it is relatively small, which m...

show abstract

Lepidopteran Peptides of the Allatostatin Superfamily

Cited by 70 publications

References 19 publications

Regulation of lepidopteran foregut movement by allatostatins and allatotropin from the frontal ganglion

Regulation of lepidopteran foregut movement by allatostatins and allatotropin from the frontal ganglion

Midgut epithelial endocrine cells are a rich source of the neuropeptides APSGFLGMRamide (Cancer borealis tachykinin-related peptide Ia) and GYRKPPFNGSIFamide (Gly1-SIFamide) in the crabs Cancer borealis, Cancer magister and Cancer productus

Molecular Cloning of a Functional Allatostatin Gut/Brain Receptor and an Allatostatin Preprohormone from the Silkworm Bombyx mori

Contact Info

Product

Resources

About