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A novel adipokinetic peptide from the corpus cardiacum of the primitive caeliferan pygmy grasshopper Tetrix subulata (Caelifera, Tetrigidae)
G. Gäde, P. Šimek, HG. Marco,
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Adipokines chemistry isolation & purification pharmacology MeSH
- Corpora Allata metabolism MeSH
- Insect Proteins chemistry isolation & purification pharmacology MeSH
- Grasshoppers chemistry MeSH
- Lipid Metabolism drug effects MeSH
- Molecular Weight MeSH
- Amino Acid Sequence MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
The basal caeliferan family Tetrigidae is investigated to identify neuropeptides belonging to the adipokinetic hormone (AKH) family. The pygmy grasshopper Tetrix subulata contains in its corpus cardiacum two octapeptides as revealed by liquid chromatography coupled to electrospray ionization mass spectrometry. The less abundant peptide is the well-known Schgr-AKH-II (pELNFSTGW amide) which is suggested to be the ancestral AKH of Caelifera and Ensifera. The second peptide, Tetsu-AKH (pEFNFTPGW amide), is novel and quite unusual with its third aromatic residue at position 2. It is thought to be autapomorphic for Caelifera. Tetsu-AKH has hyperlipemic activity in T. subulata and in Schistocerca gregaria.
Biology Centre The Czech Academy of Sciences CZ 37005 Ceske Budejovice Czech Republic
Department of Biological Sciences University of Cape Town Rondebosch ZA 7700 South Africa
References provided by Crossref.org
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- $a Gäde, Gerd $u Department of Biological Sciences, University of Cape Town, Rondebosch ZA-7700, South Africa. Electronic address: gerd.gade@uct.ac.za.
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- $a The basal caeliferan family Tetrigidae is investigated to identify neuropeptides belonging to the adipokinetic hormone (AKH) family. The pygmy grasshopper Tetrix subulata contains in its corpus cardiacum two octapeptides as revealed by liquid chromatography coupled to electrospray ionization mass spectrometry. The less abundant peptide is the well-known Schgr-AKH-II (pELNFSTGW amide) which is suggested to be the ancestral AKH of Caelifera and Ensifera. The second peptide, Tetsu-AKH (pEFNFTPGW amide), is novel and quite unusual with its third aromatic residue at position 2. It is thought to be autapomorphic for Caelifera. Tetsu-AKH has hyperlipemic activity in T. subulata and in Schistocerca gregaria.
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