Co‐activation of insulin‐like growth factor‐I receptors and protein kinase C results in parasympathetic neuronal survival

Crouch, Michael F.; Hendry, Ian A.

doi:10.1002/jnr.490280112

Cited by 19 publications

(4 citation statements)

References 28 publications

(34 reference statements)

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“…Ganglia were then triturated using a Pasteur pipette to disperse the individual cells. Neurons were cultured in DMEM in the presence of insulin (16 μmol/L) and phorbol ester (752 nmol/L) and incubated at 37°C (5% CO 2 in air) for 24 h. This stimulation protocol has been shown to cause maximal survival and neurite growth 26 . Neurons were subsequently fixed with 2% paraformaldehyde as described below.…”

Section: Methodsmentioning

confidence: 99%

The flightless I protein localizes to actin‐based structures during embryonic development

Davy¹,

Ball

Matthaei³

et al. 2000

Immunol Cell Biol

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SummaryThe product of the flightless I gene is predicted to provide a link between molecules of an as yet unidentified signal transduction pathway and the actin cytoskeleton. Previous work has shown that weak and severe mutations of the flightless I locus in Drosophila melanogaster cause disruption in the indirect flight muscles and in embryonic cellularization events, respectively, indicative of a regulatory role for the flightless I protein in cytoskeletal rearrangements. A C-terminal domain within flightless I with significant homology to the gelsolinlike family of actin-binding proteins has been identified, but evidence of a direct interaction between endogenous flightless I and actin remains to be shown. In the present study, chick, mouse and Drosophila melanogaster embryos have been examined and the localization of flightless I investigated in relation to the actin cytoskeleton. It is shown that flightless I localization is coincident with actin-rich regions in parasympathetic neurons harvested from chicks, in mouse blastocysts and in structures associated with cellularization in Drosophila melanogaster.

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Section: Methodsmentioning

confidence: 99%

The flightless I protein localizes to actin‐based structures during embryonic development

Davy¹,

Ball

Matthaei³

et al. 2000

Immunol Cell Biol

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“…Similarly, such synergy in the neuronal system has also been documented 6 . Chick ciliary parasympathetic neurones in culture respond to acidic fibroblast growth factor (aFGF) by surviving and extending neurites.…”

Section: Introductionmentioning

confidence: 86%

Insulin induces epidermal growth factor (EGF) receptor clustering and potentiates EGF‐stimulated DNA synthesis in Swiss 3T3 cells: A mechanism for costimulation in mitogenic synergy

et al. 2000

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In many cellular systems, activation with more than one ligand can produce a cellular response that is greater than the sum of the individual responses to the ligands. This synergy is sometimes referred to as coactivation. In Swiss 3T3 fibroblasts, activation of the epidermal growth factor (EGF) receptor produces a weak induction of DNA synthesis. Insulin has no stimulatory effect on this response. However, in combination, EGF and insulin synergize to cause a large induction of S phase. The underlying cellular biochemistry of this effect has been examined. The data indicate that phospholipase C activation is a major component of agonist‐induced DNA synthesis. In contrast, activation of p70 S6 kinase by single agonists was inversely related to their ability to stimulate DNA synthesis. Therefore, it was examined whether stimulation of Swiss 3T3 cells with insulin causes changes in the subcellular distribution of EGF receptors and phospholipase Cγ1 that could potentially explain the observed synergy or costimulation. It was found that insulin effectively induced the accumulation of EGF receptors on the actin arc of cells without activation of the EGF receptor. In contrast, EGF, when added for several hours, did not cause accumulation of the EGF receptor at this site. However, both EGF and insulin stimulated the accumulation of phospholipase Cγ1 at the actin arc, which was coincident with the EGF receptor in the case of insulin‐ stimulated cells. Therefore, it is suggested that the insulin‐induced coclustering of the EGF receptor with phospholipase Cγ1 at the actin arc may allow for greater efficiency of signal transduction, resulting in the synergy observed for these two hormones in stimulation of DNA synthesis.

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“…Other neurotrophic factors produced by cardiac myocytes include nerve growth factor (NGF) and insulinlike growth factor-1 (IGF-1) (Reiss et al 1994;Martinelli et al 2006). NGF has been shown to enhance the development of presynaptic terminals and modulate synaptic transmission between sympathetic neurons and cardiac myocytes (Lockhart et al 1997(Lockhart et al , 2000, and sympathetic neurons are known to respond to insulin-like growth factor-1 (IGF-1) as well (Crouch andHendry 1991: Karagiannis et al 1997). Preganglionic cholinergic neurons that innervate adrenal medulla require neurotrophin-4 (NT-4), a neurotrophic factor produced by adrenal chromaffin cells (Schober et al 1998).…”

Section: Introductionmentioning

confidence: 95%

Neurotrophic Factors in Autonomic Nervous System Plasticity and Dysfunction

Mattson

Wan

2008

Neuromol Med

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During development, neurotrophic factors are known to play important roles in regulating the survival of neurons in the autonomic nervous system (ANS) and the formation of their synaptic connectivity with their peripheral targets in the cardiovascular, digestive, and other organ systems. Emerging findings suggest that neurotrophic factors may also affect the functionality of the ANS during adult life and may, in part, mediate the effects of environmental factors such as exercise and dietary energy intake on ANS neurons and target cells. In this article, we describe the evidence that ANS neurons express receptors for multiple neurotrophic factors, and data suggesting that activation of those receptors can modify plasticity in the ANS. Neurotrophic factors that may regulate ANS function include brain-derived neurotrophic factor, nerve growth factor, insulin-like growth factors, and ciliary neurotrophic factor. The possibility that perturbed neurotrophic factor signaling is involved in the pathogenesis of ANS dysfunction in some neurological disorders is considered, together with implications for neurotrophic factor-based therapeutic interventions.

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Co‐activation of insulin‐like growth factor‐I receptors and protein kinase C results in parasympathetic neuronal survival

Cited by 19 publications

References 28 publications

The flightless I protein localizes to actin‐based structures during embryonic development

The flightless I protein localizes to actin‐based structures during embryonic development

Insulin induces epidermal growth factor (EGF) receptor clustering and potentiates EGF‐stimulated DNA synthesis in Swiss 3T3 cells: A mechanism for costimulation in mitogenic synergy

Neurotrophic Factors in Autonomic Nervous System Plasticity and Dysfunction

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