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 Pieris brassicae; this provides insight into structure-activity specificity and could be useful for further investigations into possible biorational insecticide development.

• Klíčová slova
• Lepidoptera, adipokinetic hormone, biological assays, butterflies and moths, mass spectrometry, neuropeptides, primary structure,
• Publikační typ
• časopisecké články MeSH

Insect adipokinetic hormones (AKHs) are short peptides produced in the corpora cardiaca and are responsible for mobilizing energy stores from the fat body to the hemolymph. Three related peptides, AKH1, AKH2, and AKH/corazonin-related peptide (ACP) as well as three AKH receptors have been reported in Bombyx mori. AKH1 and AKH2 are specific for the AKHR1 receptor, whereas ACP interacts with the other two AKHRs. To assess the effect of the two silkworm AKHs and ACP in the regulation of energy homeostasis we examined the expression pattern of the three peptides and their receptors as well as their effect on the level of carbohydrates and lipids in the hemolymph. Our results support the hypothesis that only AKH1 and AKH2 peptides together with the AKHR1 receptor are involved in the maintenance of energy homeostasis. Because Bombyx AKHR1 (BmAKHR1) seems to be a true AKHR we generated its mutation. The BmAKHR1 mutant larvae display significantly lower carbohydrate and lipid levels in the hemolymph and reduced sensitivity to starvation. Our study clarifies the role of BmAKHR1 in energy homeostasis.

• Klíčová slova
• BMSK0010951, Bommo-AKH1, Bommo-AKH2, NM_001043584, TALEN, silkworm, targeted mutagenesis,
• MeSH
• bourec růst a vývoj   metabolismus   MeSH
• energetický metabolismus MeSH
• hemolymfa metabolismus   MeSH
• hmyzí hormony genetika   metabolismus   MeSH
• hmyzí proteiny genetika   metabolismus   MeSH
• kyselina pyrrolidonkarboxylová analogy a deriváty   metabolismus   MeSH
• larva metabolismus   MeSH
• lipidy analýza   MeSH
• mutageneze MeSH
• neuropeptidy genetika   metabolismus   MeSH
• oligopeptidy genetika   metabolismus   MeSH
• protein - isoformy genetika   metabolismus   MeSH
• receptory glukagonu genetika   metabolismus   MeSH
• regulace genové exprese MeSH
• sacharidy analýza   MeSH
• signální transdukce * MeSH
• zvířata MeSH
• Check Tag
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• adipokinetic hormone MeSH Prohlížeč
• corazonin protein, insect MeSH Prohlížeč
• hmyzí hormony MeSH
• hmyzí proteiny MeSH
• kyselina pyrrolidonkarboxylová MeSH
• lipidy MeSH
• neuropeptidy MeSH
• oligopeptidy MeSH
• protein - isoformy MeSH
• receptory glukagonu MeSH
• sacharidy MeSH

The male accessory glands (AG) and gonoducts of moths develop during metamorphosis and are essential for successful fertilization of females. We found that these reproductive organs are innervated by a sex-specific cluster of peptidergic neurons in the posterior 9th neuromere of the terminal abdominal ganglion (TAG). This cluster of ~20 neurons differentiate during metamorphosis to innervate the accessory glands and sperm ducts. Using immunohistochemistry and in situ hybridization (ISH) we showed that these neurons express four neuropeptide precursors encoding calcitonin-like diuretic hormone (CT-DH), allatotropin (AT) and AT-like peptides (ATLI-III), allatostatin C (AST-C), and myoinhibitory peptides (MIPs). We used contraction bioassay in vitro to determine roles of these neuropeptides in the gonoduct and accessory gland activity. Spontaneous contractions of the seminal vesicle and AG were stimulated in a dose depended manner by CT-DH and AT, whereas AST-C and MIP elicited dose dependent inhibition. Using quantitative RT-PCR we confirmed expression of receptors for these neuropeptides in organs innervated by the male specific cluster of neurons. Our results suggest a role of these neuropeptides in regulation of seminal fluid movements during copulation.

• MeSH
• biologická proměna fyziologie   MeSH
• bourec metabolismus   MeSH
• hmyzí hormony metabolismus   MeSH
• hmyzí proteiny metabolismus   MeSH
• neurony metabolismus   MeSH
• neuropeptidy metabolismus   MeSH
• pohlavní dimorfismus * MeSH
• zvířata MeSH
• Check Tag
• mužské pohlaví MeSH
• ženské pohlaví MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• allatotropin MeSH Prohlížeč
• hmyzí hormony MeSH
• hmyzí proteiny MeSH
• neuropeptidy MeSH