Biochemically identified neuropeptides in a caddisfly (Trichoptera) and a pygmy mole cricket (Orthoptera: Caelifera: Tridactyloidea)

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F21%3A00541151" target="_blank" >RIV/60077344:_____/21:00541151 - isvavai.cz</a>

Výsledek na webu

<a href="https://onlinelibrary.wiley.com/doi/10.1002/arch.21778" target="_blank" >https://onlinelibrary.wiley.com/doi/10.1002/arch.21778</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/arch.21778" target="_blank" >10.1002/arch.21778</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Biochemically identified neuropeptides in a caddisfly (Trichoptera) and a pygmy mole cricket (Orthoptera: Caelifera: Tridactyloidea)

Popis výsledku v původním jazyce

One representative of the order Trichoptera, namely the caddisfly Chaetopteryx villosa, was investigated along with the pygmy mole cricket Xya capensis which is a representative of the most basal superfamily of the caeliferan Orthoptera, that is, the Tridactyloidea. From both clades neuropeptides have not been biochemically characterized before this study. Here, members of the adipokinetic hormone family (AKHs) are sequenced via liquid chromatography (LC)‐ion trap mass spectrometry from methanolic extracts from the corpora cardiaca of respective species. The corpora cardiaca were dissected, methanolic extracts prepared, peptides separated by liquid chromatography (LC), and AKHs detected and sequenced by ion trap mass spectrometry. Both species investigated contain an octapeptide AKH: the trichopteran species has the peptide with the sequence pGlu‐Leu‐Thr‐Phe‐Thr‐Pro‐ Ser‐Trp amide, the ambiguity of the isobaric amino acids Leu and Ile at position two was solved by comparing retention times on LC and by co‐elution with the synthetic Leu2‐form. This peptide is known as Aedae‐AKH and found in certain dipteran species and in an alderfly (Megaloptera). The tridactyloid species contains the peptide with the sequence pGlu‐Val‐Asn‐Phe‐Ser‐Pro‐Gly‐Trp amide which had first been identified in a member of the order Mantophasmatodea and is called Manto‐CC. Comparisons are made between the AKH complements of the sister groups Trichoptera and Lepidoptera and their possible relatedness and, on the other hand, between the AKH of X. capensis with those of closely related caeliferan superfamilies. The biology of the two studied species is used to speculate about a possible function of the elucidated hormones. Lastly, the use of a larval stage as starting material for structural neuropeptide information is discussed.

Název v anglickém jazyce

Biochemically identified neuropeptides in a caddisfly (Trichoptera) and a pygmy mole cricket (Orthoptera: Caelifera: Tridactyloidea)

Popis výsledku anglicky

One representative of the order Trichoptera, namely the caddisfly Chaetopteryx villosa, was investigated along with the pygmy mole cricket Xya capensis which is a representative of the most basal superfamily of the caeliferan Orthoptera, that is, the Tridactyloidea. From both clades neuropeptides have not been biochemically characterized before this study. Here, members of the adipokinetic hormone family (AKHs) are sequenced via liquid chromatography (LC)‐ion trap mass spectrometry from methanolic extracts from the corpora cardiaca of respective species. The corpora cardiaca were dissected, methanolic extracts prepared, peptides separated by liquid chromatography (LC), and AKHs detected and sequenced by ion trap mass spectrometry. Both species investigated contain an octapeptide AKH: the trichopteran species has the peptide with the sequence pGlu‐Leu‐Thr‐Phe‐Thr‐Pro‐ Ser‐Trp amide, the ambiguity of the isobaric amino acids Leu and Ile at position two was solved by comparing retention times on LC and by co‐elution with the synthetic Leu2‐form. This peptide is known as Aedae‐AKH and found in certain dipteran species and in an alderfly (Megaloptera). The tridactyloid species contains the peptide with the sequence pGlu‐Val‐Asn‐Phe‐Ser‐Pro‐Gly‐Trp amide which had first been identified in a member of the order Mantophasmatodea and is called Manto‐CC. Comparisons are made between the AKH complements of the sister groups Trichoptera and Lepidoptera and their possible relatedness and, on the other hand, between the AKH of X. capensis with those of closely related caeliferan superfamilies. The biology of the two studied species is used to speculate about a possible function of the elucidated hormones. Lastly, the use of a larval stage as starting material for structural neuropeptide information is discussed.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/GA17-22276S" target="_blank" >GA17-22276S: Nové metody pro metabolomickou analýzu obtížně stanovitelných metabolitů</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2021

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Archives of Insect Biochemistry and Physiology

ISSN

0739-4462

e-ISSN

1520-6327

Svazek periodika

106

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

e21778

Kód UT WoS článku

000628861700001

EID výsledku v databázi Scopus

2-s2.0-85102472943