Journal
MOLECULAR AND CELLULAR ENDOCRINOLOGY
Volume 251, Issue 1-2, Pages 78-87Publisher
ELSEVIER IRELAND LTD
DOI: 10.1016/j.mce.2006.02.015
Keywords
signal transduction; phosphorylation; phospholipase C; insect molting; insect steroids; extracellular signal-regulated kinase (ERK)
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Funding
- NIGMS NIH HHS [GM63198-01] Funding Source: Medline
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The prothoracic gland is the primary source of ecdysteroid hormones in the immature insect. Ecdysteroids coordinate gene expression necessary for growth, molting and metamorphosis. Prothoracicotropic hormone (PTTH), a brain neuropeptide, regulates ecdysteroid synthesis in the prothoracie gland. PTTH stimulates ecdysteroid synthesis through a signal transduction cascade that involves at least four protein kinases: protein kinase A (PKA), p70 S6 kinase, an unidentified tyrosine kinase, and the extracellular signal-regulated kinase (ERK). In this report, the participation of protein kinase C (PKC) in PTTH signalling is demonstrated and characterized. PTTH stimulates PKC activity through a PLC and Ca2+-dependent pathway that is not cAMP regulated. Inhibition of PKC inhibits PTTH-stimulated ecdysteroidogenesis as well as PTTH-stimulated phosphorylation of ERK and its upstream regulator, MAP/ERK kinase (MEK). These observations reveal that the acute regulation of prothoracic gland steroidogenesis is dependent on a web of interacting kinase pathways, which probably converge on factors that regulate translation. (c) 2006 Elsevier Ireland Ltd. All rights reserved.
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