Title
New insights in Adipokinetic Hormone (AKH) precursor processing in **Locusta migratoria** obtained by capillary liquid chromatography-tandem mass spectrometry
Author
Faculty/Department
Faculty of Sciences. Biology
Publication type
article
Publication
Fayetteville, N.Y. ,
Subject
Chemistry
Biology
Pharmacology. Therapy
Source (journal)
Peptides. - Fayetteville, N.Y.
Volume/pages
23(2002) :4 , p. 635-644
ISSN
0196-9781
ISI
000174578700006
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Abstract
After translation, the AKH I and AKH II precursors form three dimeric constructs prior to further processing into the respective AKHs and three dimeric Adipokinetic Hormone Precursor Related Peptides or APRPS (two homodimers and one heterodimer). By capillary liquid chromatography-tandem mass spectrometry we demonstrate that the APRPs in Locusta migratoria are further processed to form two smaller neuropeptides: DAADFADPYSFL (residue 36 to 47 of the AKH I precursor) and YADPNADPMAFL (residue 34 to 45 of the AKH II precursor). The peptides are designated as Adipokinetic Hormone Joining Peptide I (AKH-JP I) and 2 (AKH-JP II) respectively. Within the AKH I and AKH II precursor molecules, the classic KK and RR processing sites separate the AKH-JPs from the AKH I and II respectively. At the carboxy terminus, both AKH-JP I and II are flanked by Tyr-Arg, a cleaving site not described before. Such an unusual cleavage site suggests the presence, in the corpora cardiaca, of specific convertases. The AKH-JP-II does not stimulate lipid release from the fat body nor does it stimulate glycogen phosphorylase activity, both key functions of AKH. (C) 2002 Elsevier Science Inc. All rights reserved.
E-info
https://repository.uantwerpen.be/docman/iruaauth/836b32/6819675.pdf
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