ISSN:
0739-4462
Keywords:
juvenile hormone-binding proteins
;
grasshopper
;
fat body
;
vitellogenin
;
Chemistry
;
Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
Notes:
In the analysis of insect juvenile hormone (JH) function, metamorphosis is complicated by ecdysone and JH acting concurrently. Although JH stimulation of vitellogenin synthesis by the fat body is by no means simple, it is possible to focus on the events leading to selective transcription of a single gene. The two-striped grasshopper Melanoplus bivittatus was used to study nuclear binding of JH during vitellogenesis and to investigate proteins binding JH that have been found in hemolymph and fat body. M. bivittatus reproduction is regulated by JH. The fat body nuclei increased in ploidy with time after eclosion, and, because the antiallatotropin precocene completely inhibited vitellogenin production, we assume that this grasshopper differs little from Locusta migratoria in which JH stimulates transcription of the vitellogenin gene. Proteins that bind JH with high affinity were identified with the hydroxyapatite assay. Characterization of the JH-binding proteins included ion exchange chromatography, gel filtration, and polyacrylamide gel electrophoresis. Four proteins of hemolymph and three proteins of fat body bound JH with high affinity, and binding was competitively inhibited by JHIII. Short-term tissue culture was used to follow [3H]JH-III uptake by fat body and to determine the intracellular distribution of the hormone. Proteins that bound JH were extracted from nuclei with KCI, and they increased in number from the time of adult emergence to the time of maximum vitellogenin secretion. The JH-binding proteins from nuclei might be receptors that help regulate the selective expression of genes for vitellogenin and for other proteins induced by JH.
Additional Material:
6 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/arch.940030704
