Identification of Bombyx mori Akt and its phosphorylation by bombyxin stimulation
Autor(es): Nagata, Shinji; Hakuno, Fumihiko; Takahashi, Shin-Ichiro; Nagasawa, Hiromichi
Resumo: Akt, a Ser/Thr protein kinase involved in insulin signaling, was identified from the silkworm, Bombyx mori. Bombyx Akt (BomAkt) is composed of 493 amino acid residues including regions conserved in other Akts: the Pleckstrin homology and kinase domains, and a dual phosphorylation site essential for kinase activation. Commercially available antibodies against mammalian Akt and phosphoAkt were able to recognize BomAkt and phosphorylated BomAkt in HEK293 cells expressing BomAkt. Additionally, phosphorylation of BomAkt was detectable in insulin-like growth factor (IGF)-I stimulated-HEK293 cells expressing BomAkt. RT-PCR and immunoblotting analyses revealed that BomAkt is expressed ubiquitously in Bombyx larvae. Phosphorylation of BomAkt was observed both in the isolated fat body after exposure to bombyxin, an endogenous insulin-like peptide, and in the larval fat body by refeeding a diet after starvation. These results suggest that dietary intake may activate the insulin signaling pathway, including Akt, through bombyxin action in B. mori. (C) 2008 Elsevier Inc. All rights reserved.
Palavras-Chave: Akt; Bombyxin; Bombyx Mori; Feeding; Food Intake; Insulin-Like Signal; Molecular Cloning; Phosphorylation
Imprenta: Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology, v. 151, n. 3, p. 355-360, 2008
Identificador do objeto digital: 10.1016/j.cbpb.2008.08.002
Descritores: Aedes aegypti - RT-PCR
Data de publicação: 2008
