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This version published online on May 1, 2003
Endocrinology, doi:10.1210/en.2002-0107
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Submitted on December 4, 2002
Accepted on April 25, 2003

Identification of a glycogenolysis inhibiting peptide from the corpora cardiaca of locusts

Elke Clynen1*, Jurgen Huybrechts1, Geert Baggerman1, Jan Van Doorn1, Dick Van der Horst1, Arnold De Loof1, and Liliane Schoofs1

1 Laboratory for Developmental Physiology and Molecular Biology, K.U. Leuven, Leuven, Belgium; Department of Biochemical Physiology, Utrecht University, Utrecht, The Netherlands

* To whom correspondence should be addressed. E-mail: Elke.Clynen{at}bio.kuleuven.ac.be.

A mass spectrometric study of the peptidome of the neurohemal part of the corpora cardiaca of Locusta migratoria and Schistocerca gregaria shows that it contains several unknown peptides. We were able to identify the sequence of one of these peptides as pQSDLFLLSPK. This sequence is identical to the part of the Locusta insulin-related peptide (IRP) precursor that is situated between the signal peptide and the B-chain. We designated this peptide as IRP co-peptide. This IRP co-peptide is also present in the pars intercerebralis, which is likely to be the site of synthesis. It is identical in both Locusta migratoria and Schistocerca gregaria. It shows no effect on the hemolymph lipid concentration in vivo or muscle contraction in vitro. The IRP co-peptide is able to cause a decreased phosphorylase activity in locust fat body in vitro, opposite to the effect of the adipokinetic hormones and therefore possibly represents a glycogenolysis inhibiting peptide.
Key words: glycogen phosphorylase • insect metabolism • insulin-related peptide • Locusta migratoria • mass spectrometry • peptide precursor processing • Schistocerca gregaria






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