Journal article
Identification of Phe-Gly-Leu-amide type allatostatin-7 in Reticulitermes flavipes: Its localization in tissues and relation to juvenile hormone synthesis
Peptides (New York, N.Y. : 1980), Vol.30(3), pp.495-506
03/01/2009
DOI: 10.1016/j.peptides.2008.06.020
PMID: 18652864
Abstract
The allatostatins (ASTs), with a Tyr/Phe-Xaa-Phe-Gly-Leu/Ile-amide C-terminus, are neuropeptides that occur in many orders of insects, but are known to inhibit juvenile hormone (JH) synthesis by corpora allata (CA) only in cockroaches, crickets, and termites. 5 AST peptides with similar sequences to those of 6 species of cockroaches have been isolated and sequenced from extract of brain tissue of the termite
Reticulitermes flavipes. The amino acid sequence of a 6th peptide,
R. flavipes AST-7, determined by LC–MS/MS following HPLC fractionation of brain extract, is S-P-S-S-G-N-Q-R-L-Y-G-F-G-L-NH
2. The 8 terminal amino acids are identical to AST-7 of the cockroach
Diploptera punctata.
R. flavipes and
D. punctata AST-7s inhibited JH synthesis by CA of both species equally and their affinity for antibody against
D. punctata AST-7 is similar. Immunoreactivity of termite tissue with this antibody indicates neuro- and myomodulatory activity of the peptide in addition to its demonstrated allatostatic function. The density of AST immunostaining in axons within the CA of
R. flavipes and the rate of JH synthesis by similar glands were negatively correlated. This is evidence that when AST is abundant in the glands it is being released in vivo to limit JH production.
Details
- Title: Subtitle
- Identification of Phe-Gly-Leu-amide type allatostatin-7 in Reticulitermes flavipes: Its localization in tissues and relation to juvenile hormone synthesis
- Creators
- Karen L. Elliott - University of IowaKuen Kuen Chan - Department of Biology, University of Iowa, Dubuque Street, Iowa Avenue, Iowa City, IA 52242, United StatesLynn Teesch - University of IowaOmar Clor - University of IowaBarbara Stay - University of Iowa
- Resource Type
- Journal article
- Publication Details
- Peptides (New York, N.Y. : 1980), Vol.30(3), pp.495-506
- Publisher
- Elsevier Inc
- DOI
- 10.1016/j.peptides.2008.06.020
- PMID
- 18652864
- ISSN
- 0196-9781
- eISSN
- 1873-5169
- Language
- English
- Date published
- 03/01/2009
- Academic Unit
- Core Research Facilities; Biology; Medicine Administration
- Record Identifier
- 9984622754702771
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