A novel adipokinetic peptide from the corpus cardiacum of the primitive caeliferan pygmy grasshopper Tetrix subulata (Caelifera, Tetrigidae)

GÄde, Gerd; Šimek, Petr; Marco, Heather G.

doi:10.1016/j.peptides.2015.01.008

Cited by 6 publications

(3 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Pygmy mole crickets are the most basal superfamily of the Caelifera with its closest relative to be found in the superfamily Tetrigoidea (Flook et al, 1999; Wipfler et al, 2019). The AKH complement from only one species of the family Tetrigidae, the pygmy grasshopper Tetrix subulata , is known (Gäde et al, 2015): two AKHs, code named Tetsu‐AKH and Schgr‐AKH‐II, were detected in T. subulata ; none of these peptides are identified in the current study in the pygmy mole cricket X. capensis . The T. subulata AKH peptides are only 75% similar to Manto‐CC of X. capensis exhibiting two amino acid substitutions (Table 1).…”

Section: Resultsmentioning

confidence: 52%

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

GÄde

Šimek

Marco

2021

Arch Insect Biochem Physiol

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Section: Resultsmentioning

confidence: 52%

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

GÄde

Šimek

Marco

2021

Arch Insect Biochem Physiol

Self Cite

View full text Add to dashboard Cite

show abstract

“…As we have now made it a habit to screen for the Hyp form of Pro-containing AKHs, we have also found a representative in the grasshopper, Tetrix subulata (a Hyp AKH with the recognition sequence TPG). It is known that T. subulata CC contain two peptides: Schgr-AKH-II, which has no Pro, and Tetsu-AKH, which does [55]. Evidence for low concentrations of [Hyp 6 ]-Tetsu-AKH was obtained in the current study (i.e., candidate peptide measured at expected mass and at earlier retention time than Tetsu-AKH, mass shift of the y 3 fragment ion m/z 358.19 > 374.18), whereas no oxidative modification was found Life 2023, 13, 2315 9 of 18 in Schgr-AKH-II (also not for Trp).…”

Section: Artifact or Natural Product?mentioning

confidence: 99%

Oxidation Products of Tryptophan and Proline in Adipokinetic Hormones—Artifacts or Post-Translational Modifications?

König,

Marco,

Gäde

2023

Life

Self Cite

View full text Add to dashboard Cite

Background: Adipokinetic hormones (AKHs) regulate important physiological processes in insects. AKHs are short peptides with blocked termini and Trp in position 8. Often, proline occupies position 6. Few post-translational modifications have been found, including hydroxyproline ([Hyp6]) and kynurenine. Our recent data suggest that the Hyp- and Kyn-containing AKHs occur more often than originally thought and we here investigate if they are natural or artifactual. Methods: From crude extracts of the corpora cardiaca (CC) of various insect species, AKHs were analyzed using liquid chromatography coupled to high-resolution mass spectrometry (LC-MS). Synthetic [Hyp6]-AKHs were tested in an in vivo metabolic assay. Freshly dissected Periplaneta americana and Blaberus atropos CCs (with precautions taken against oxidation) were analyzed. B. atropos CC were placed into a depolarizing saline and the released AKHs were measured. Results: Hyp was detected in several decapeptides from cockroaches. The modified form accompanied the AKH at concentrations below 7%. The [Hyp6]-AKHs of B. atropos were present in fresh CC preparations and were shown to be releasable from the CC ex vivo. Synthetic [Hyp6]-containing peptides tested positively in a hypertrehalosemic bioassay. Hydroxyprolination was also detected for Manto-CC from the termite Kalotermes flavicollis and for Tetsu-AKH of the grasshopper, Tetrix subulata. Oxidized Trp-containing forms of Nicve-AKH were found in species of the burying beetle genus Nicrophorus. Conclusions: Trp oxidation is known to occur easily during sample handling and is likely the reason for the present findings. For hydroxyprolination, however, the experimental evidence suggests endogenous processes.

show abstract

“…The primary structural characteristics of the AKH family peptides is a chain length of 8-10 amino acids, at least two posttranslational modifications (one at the N-terminus as a pyroglutamate residue and one at the C-terminus as a carboxyamide), an aromatic amino acid such as phenylalanine or tyrosine at position 4, a branched amino acid such as serine or threonine at position 5, always the aromatic tryptophan at position 8, and a glycine residue at position 9 (Gäde et al, 1997b). Additional posttranslational modifications, such as an unusual Trp-glycosylation, hydroxyproline, and phosphorylated-and sulphated-Thr, also occur (see Gäde, Šimek, & Marco, 2015).…”

mentioning

confidence: 99%

The adipokinetic hormone of Mantodea in comparison to other Dictyoptera

GÄde

Marco

2017

Arch Insect Biochem Physiol

Self Cite

View full text Add to dashboard Cite

Six species of the order Mantodea (praying mantises) are investigated for the presence and sequence of putative adipokinetic hormones (AKHs). The selected species span a wide evolutionary range of various families and subfamilies of the clade Mantodea. The corpora cardiaca of the different species are dissected, methanolic extracts prepared, peptides separated by liquid chromatography, and AKHs detected and sequenced by ion trap mass spectrometry. All six species investigated contain an octapeptide with the primary structure pGlu-Val-Asn-Phe-Thr-Pro-Asn-Trp amide, which is code-named Emppe-AKH and had been found earlier in three other species of Mantodea. Conspecific bioassays with the species Creoboter sp. (family Hymenopodidae) reveal an adipokinetic but not a hypertrehalosemic function of Emppe-AKH. Comparison with other members of the Dictyoptera (cockroaches, termites) show that Emppe-AKH is only found in certain termites, which have been recently placed into the Blattaria (cockroaches) as sister group to the family Cryptocercidae. Termites and cockroaches both show biodiversity in the sequence of AKHs, and some cockroach species even contain two AKHs. In contrast, all praying mantises-irrespective of their phylogenetic position-synthesize uniformly only one and the same octapeptide Emppe-AKH.

show abstract

A novel adipokinetic peptide from the corpus cardiacum of the primitive caeliferan pygmy grasshopper Tetrix subulata (Caelifera, Tetrigidae)

Cited by 6 publications

References 25 publications

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

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

Oxidation Products of Tryptophan and Proline in Adipokinetic Hormones—Artifacts or Post-Translational Modifications?

The adipokinetic hormone of Mantodea in comparison to other Dictyoptera

Contact Info

Product

Resources

About