ArticleFrontiers in physiology2020
Unique Members of the Adipokinetic Hormone Family in Butterflies and Moths (Insecta, Lepidoptera).
Article in Frontiers in physiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- Structural Diversity of Adipokinetic Hormones in the Coleopteran Suborder Polyphaga (Excluding Cucujiformia).Archives of insect biochemistry and physiology · 2025Article
- Sex and stress modulate pupal defense response in tobacco hornworm.Current zoology · 2023Article
- The proline effect and the tryptophan immonium ion assist in de novo sequencing of adipokinetic hormones.Scientific reports · 2023Article
- Mass Spectrometric Proof of Predicted Peptides: Novel Adipokinetic Hormones in Insects.Molecules (Basel, Switzerland) · 2022Article
- In Silico Screening for Pesticide Candidates against the Desert LocustLife (Basel, Switzerland) · 2022Article
- The Adipokinetic Peptides of Hemiptera: Structure, Function, and Evolutionary Trends.Frontiers in insect science · 2022Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lepidoptera is amongst one of the four most speciose insect orders and ecologically very successful because of their ability to fly. Insect flight is always aerobic and exacts a high metabolic demand on the animal. A family of structurally related neuropeptides, generically referred to as adipokinetic hormones (AKHs), play a key role in triggering the release of readily utilizable fuel metabolites into the hemolymph from the storage forms in the fat body. We used mass spectrometry to elucidate AKH sequences from 34 species of Lepidoptera and searched the literature and publicly available databases to compile (in a phylogenetic context) a comprehensive list of all Lepidoptera sequences published/predicted from a total of 76 species. We then used the resulting set of 15 biochemically characterized AKHs in a physiological assay that measures lipid or carbohydrate mobilization in three different lepidopteran species to learn about the functional cross-activity (receptor-ligand interactions) amongst the different butterfly/moth families. Our results include novel peptide structures, demonstrate structural diversity, phylogenetic trends in peptide distribution and order-specificity of Lepidoptera AKHs. There is almost an equal occurrence of octa-, nona-, and decapeptides, with an unparalleled emphasis on nonapeptides than in any insect order. Primitive species make Peram-CAH-II, an octapeptide found also in other orders; the lepidopteran signature peptide is Manse-AKH. Not all of the 15 tested AKHs are active in
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