Action of juvenile hormone on the follicle cells ofRhodnius prolixus: Evidence for a novel regulatory mechanism involving protein kinase C

Sevala, Veeresh L.; Davey, K. G.

doi:10.1007/bf01957476

Cited by 89 publications

(52 citation statements)

References 11 publications

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“…These hormones control the synthesis of yolk protein and its receptors (Raikhel and Dhadiala 1992); the patency of follicular cells (Sevala andDavey 1989, Raikhel andO'Lea 1991); and uptake of yolk proteins (Stoffolano et al 1992). The great complexity and variety of cells that compose insect ovaries suggest the participation of local mediators that also control and coordinate oogenesis.…”

Section: Eicosanoids As Local Regulators Of Oogenesismentioning

confidence: 99%

Oogenesis and egg development in triatomines: a biochemical approach

Atella

Gondim

Machado

et al. 2005

An. Acad. Bras. Ciênc.

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In triatomines, as well as in other insects, accumulation of yolk is a process in which an extra-ovarian tissue, the fat body, produces yolk proteins that are packed in the egg. The main protein, synthesized by the fat body, which is accumulated inside the oocyte, is vitellogenin. This process is also known as vitellogenesis. There are growing evidences in triatomines that besides fat body the ovary also produces yolk proteins. The way these yolk proteins enter the oocyte will be discussed. Yolk is a complex material composed of proteins, lipids, carbohydrates and other minor components which are packed inside the oocyte in an organized manner. Fertilization triggers embryogenesis, a process where an embryo will develop. During embryogenesis the yolk will be used for the construction of a new individual, the first instar nymph. The challenge for the next decade is to understand how and where these egg proteins are used up together with their non-protein components, in pace with the genetic program of the embryo, which enables cell differentiation (early phase of embryogenesis) and embryo differentiation (late phase) inside the egg.

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Section: Eicosanoids As Local Regulators Of Oogenesismentioning

confidence: 99%

Oogenesis and egg development in triatomines: a biochemical approach

Atella

Gondim

Machado

et al. 2005

An. Acad. Bras. Ciênc.

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“…By analogy to the established roles of JH III in insect reproduction (11,12), and in an attempt to unify common themes in arthropod endocrinology, it has been suggested that MF has a key role in reproduction (13). MF biosynthesis and circulating titer have been shown to be positively correlated with ovarian maturation in some crustaceans (3,14), and morphological changes in ovarian follicle cells reminiscent of JHstimulated patency in insects (15), have been observed in crustaceans following injection of JH mimics (16). A further role of MF as an ecdysiotropin has been suggested, since MO homogenates profoundly stimulate molting in vivo (17,18), and MF stimulates ecdysteroid synthesis in vitro (19).…”

Section: It Is Established That the Mandibular Organs (Mo)mentioning

confidence: 99%

Structure and Significance of Mandibular Organ-inhibiting Hormone in the Crab, Cancer pagurus

Wainwright

Webster

Wilkinson

et al. 1996

Journal of Biological Chemistry

166

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Current evidence indicates that methyl farnesoate is the crustacean equivalent of the juvenile hormones of insects. This putative hormone is produced by the mandibular organs and is negatively regulated by a neuropeptide produced and secreted by the X-organ-sinus gland complex of the eyestalk. To identify this neuropeptide, a bioassay was developed which measures the inhibition of methyl farnesoate synthesis by mandibular organs exposed to fractionated sinus gland extracts from the crab, Cancer pagurus. Two neuropeptides, named mandibular organ-inhibiting hormones (MOIH-1 and -2) repressed methyl farnesoate synthesis. MOIH-1 was fully sequenced by automated Edman degradation of endoproteinase-derived fragments and further characterized by mass spectrometry. This peptide consisted of 78 residues (M r 9235.6), with unblocked termini and three intrachain disulfide bridges. MOIH-2 appeared to be almost identical to MOIH-1 with the exception of a Gln for Lys substitution at position 33. Comparison with previously sequenced crustacean neuropeptides shows that these MOIHs are members of the ever expanding crustacean hyperglycemic hormone family, with significant sequence similarity to molt-inhibiting hormones (MIHs). It is possible that these two structurally similar peptides (MIH, MOIH) may control mutually exclusive physiological phenomena (somatic and gonadal growth), suggesting a complex hormonal integration of these processes in crustaceans.

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“…The lipidsoluble nature of JH has suggested action directly on the genome through nuclear receptors similar to the action of ecdysteroids and the vertebrate steroid/thyroid/ retinoid hormones (Jones, 1995;Gilbert et al, 2000). However, the action of JH through the cell membrane was also documented (Yamamoto et al, 1988;Sevala and Davey, 1989). Many attempts have been made to identify nuclear JH receptors.…”

Section: Introductionmentioning

confidence: 99%

Interaction of proteins involved in ecdysone and juvenile hormone signal transduction

Bitra

Palli

2008

Arch Insect Biochem Physiol

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Ecdysteroids and juvenile hormones (JH) regulate a variety of developmental, physiological, behavioral, and metabolic processes. Ecdysteroids function through a heterodimeric complex of two nuclear receptors, ecdysone receptor (EcR) and ultraspiracle (USP). An 85 kDa protein identified in Drosophila melanogaster methoprene‐tolerant (Met) mutant binds to JH III with high affinity, and the mutant flies are resistant to juvenile hormone analog (JHA), methoprene. Reporter assays using the yeast two‐hybrid system were performed in order to study the molecular interactions between EcR, USP and Met. As expected, EcR fused to the B42 activation domain and USP fused to the LexA DNA binding domain interacted with each other and supported induction of the reporter gene in the presence of stable ecdysteroid analog, RG‐102240 or steroids, muristerone A and ponasterone A. The USP:USP homodimers supported expression of the reporter gene in the absence of ligand, and there was no significant increase in the reporter activity after addition of a JHA, methoprene. Similarly, Met:Met homodimers as well as Met:EcR and Met:USP heterodimers induced reporter activity in the absence of ligand and addition of ecdysteroid or JH analogs did not increase the reporter activity regulated by either homodimers or heterodimers of Met protein. Two‐hybrid assays in insect cells and in vitro pull‐down assays confirmed the interaction of Met with EcR and USP. These data suggest that the proteins that are involved in signal transduction of ecdysteroids (EcR and USP) and juvenile hormones (Met) interact to mediate cross‐talk between these two important hormones. Arch. Insect Biochem. Physiol. 2008. © 2008 Wiley‐Liss, Inc.

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Action of juvenile hormone on the follicle cells ofRhodnius prolixus: Evidence for a novel regulatory mechanism involving protein kinase C

Cited by 89 publications

References 11 publications

Oogenesis and egg development in triatomines: a biochemical approach

Oogenesis and egg development in triatomines: a biochemical approach

Structure and Significance of Mandibular Organ-inhibiting Hormone in the Crab, Cancer pagurus

Interaction of proteins involved in ecdysone and juvenile hormone signal transduction

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