JBC Advanced Glycation Endproducts

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J. Biol. Chem., Vol. 258, Issue 20, 12210-12214, 10, 1983

Identification and activation of storage protein receptor of Sarcophaga peregrina fat body by 20-hydroxyecdysone

K Ueno, F Ohsawa and S Natori

Previous work showed that 20-hydroxyecdysone activates the fat body of Sarcophaga peregrina larvae to incorporate storage protein selectively from the hemolymph. In this study, storage protein receptors of the fat body membrane which were induced on pupation or on treatment of larval fat body with 20-hydroxyecdysone in vitro were identified. The binding of storage protein to its receptor required divalent cations, especially Ca2+, and the binding was very sensitive to pH. The storage protein receptor was inactivated when the fat body membrane was treated with trypsin. The storage protein receptor is probably a protein and it may be synthesized de novo or a cryptic form may be converted to the active form when the concentration of 20-hydroxyecdysone in the hemolymph reaches a physiological level.
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S. O. Chung, T. Kubo, and S. Natori
Molecular Cloning and Sequencing of Arylphorin-binding Protein in Protein Granules of the Sarcophaga Fat Body
J. Biol. Chem., March 3, 1995; 270(9): 4624 - 4631.
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