2007
DOI: 10.1002/arch.20180
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Different Ca2+ signalling cascades manifested by mastoparan in the prothoracic glands of the tobacco hornworm, Manduca sexta, and the silkworm, Bombyx mori

Abstract: Application of the tetradecapeptide mastoparan to the prothoracic glands (PGs) of the tobacco hornworm, Manduca sexta, and the silkworm, Bombyx mori, resulted in increases in intracellular Ca(2+) ([Ca(2+)](i)). In M. sexta, Gi proteins are involved in the mastoparan-stimulated increase in [Ca(2+)](i). However, there is no involvement of Gi proteins in the mastoparan-stimulated increase in [Ca(2+)](i) in prothoracic gland cells from B. mori. Unlike in M. sexta prothoracic glands, in B. mori prothoracic glands m… Show more

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Cited by 4 publications
(2 citation statements)
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“…The PTTH receptor is known as Torso, first characterized in Drosophila embryos (Casanova and Struhl, 1989; Li, 2005; Rewitz et al, 2009). Unlike insulin, PTTH increases intracellular levels of cyclic AMP, through a PTTH-stimulated increase in intracellular calcium and the activation of a calcium-sensitive adenylyl cyclase (Smith et al, 1984, 1985; Meller et al, 1988; Dedos et al, 2005, 2007; Fellner et al, 2005). Increased intracellular calcium also results in activation of mitogen-activated protein kinases (MAPkinases) including MEK and ERK (Rybczynski and Gilbert, 2003).…”
Section: Introductionmentioning
confidence: 99%
“…The PTTH receptor is known as Torso, first characterized in Drosophila embryos (Casanova and Struhl, 1989; Li, 2005; Rewitz et al, 2009). Unlike insulin, PTTH increases intracellular levels of cyclic AMP, through a PTTH-stimulated increase in intracellular calcium and the activation of a calcium-sensitive adenylyl cyclase (Smith et al, 1984, 1985; Meller et al, 1988; Dedos et al, 2005, 2007; Fellner et al, 2005). Increased intracellular calcium also results in activation of mitogen-activated protein kinases (MAPkinases) including MEK and ERK (Rybczynski and Gilbert, 2003).…”
Section: Introductionmentioning
confidence: 99%
“…Mastoparan activates trimeric G proteins [19,20] and increases intracellular Ca 2+ [21,22], which is important for the activation of the protein kinase Cα (PKCα) [23]. PKCα and PLD1 are co-localized [24,25] and are translocated to the plasma membrane upon Ca 2+ -mediated activation of PKCα [2628].…”
Section: Resultsmentioning
confidence: 99%