ADP-ribosylation of actin

Aktories, Klaus

doi:10.1007/bf01766487

Cited by 11 publications

(3 citation statements)

References 16 publications

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“…For example, ADP-ribosylation of actin catalyzed by bacterial toxins can lead to inhibition of actin assembly and to cytoskeletal rearrangements (32,40). More recent studies suggest a physiological role for ADP-ribosylation of G-actin (1,2). The present results suggest that ADP-ribosylation of monomeric G-actin may occur physiologically in human cervical epithelial cells in response to estrogen.…”

Section: Discussionsupporting

confidence: 49%

cGMP-dependent ADP depolymerization of actin mediates estrogen increase in cervical epithelial permeability

Gorodeski

2000

American Journal of Physiology-Cell Physiology

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Estrogen increases secretion of cervical mucus in women, and the effect depends on fragmentation of the cytoskeleton. The objective of the present study was to understand the molecular mechanism of estrogen action. Treatment of human cervical epithelial cells with 17beta-estradiol, sodium nitroprusside (SNP), or 8-bromoguanosine 3', 5'-cyclic monophosphate (8-Br-cGMP) increased cellular monomeric G-actin and decreased polymerized F-actin. The effects of estradiol were blocked by tamoxifen, by the guanylate cyclase inhibitor LY-83583, and by the cGMP-dependent protein kinase inhibitor KT-5823. The effects of SNP were blocked by LY-83583 and KT-5823, while the effects of 8-Br-cGMP were blocked only by KT-5823. Treatment with phalloidin decreased paracellular permeability and G-actin. Treatment with 17beta-estradiol, SNP, or 8-Br-cGMP attenuated SNP-induced phosphorylation of [(32)P]adenylate NAD in vitro: tamoxifen blocked the effect of estrogen; LY-83583 blocked the effect of SNP but not that of 8-Br-cGMP, while KT-5823 blocked effects of both SNP and 8-Br-cGMP. These results indicate that estrogen, nitric oxide (NO), and cGMP stimulate actin depolymerization. A possible mechanism is NO-induced, cGMP-dependent protein kinase augmentation of ADP-ribosylation of monomeric actin.

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Section: Discussionsupporting

confidence: 49%

cGMP-dependent ADP depolymerization of actin mediates estrogen increase in cervical epithelial permeability

Gorodeski

2000

American Journal of Physiology-Cell Physiology

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“…Like the retinal processes, those from DRG explants respond to NO from different donors, and this effect is not mediated by cGMP increases (Hess et al, 1993 ). Recent data suggests alternative mechanisms for motility modulation, possibly involving NO effects on Gactin ADP-ribosylation, which affects polymerization of actin filaments (Aktories, 1990), or NO-dependent modifications of major growth cone pro-teins including GAP-43 (Hess et al, 1993), Go (Hess et al, 1994), and SNAP-25 (Hess et al, 1993). No one mechanism yet has definitive support.…”

Section: Discussionmentioning

confidence: 99%

Exogenous nitric oxide causes collapse of retinal ganglion cell axonal growth cones in vitro

Renterı́a

Constantine‐Paton

1996

J. Neurobiol.

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We show that nitric oxide (NO) from applied NO-donating chemicals induces collapse of ganglion cell axonal growth cones extending from explants of tadpole retina in culture. Peroxynitrite, a neurotoxic product of NO and superoxide reaction, did not induce collapse, and oxyhemoglobin, which binds NO, blocked the highly effective collapsing activity of the NO donor S-nitrosocysteine. Membrane-permeable analogs of cyclic guanosine monophosphate had no collapsing activity. Inhibitors of NO synthase did not induce collapse. NO is a potential retrograde messenger through which postsynaptic neurons signal to their inputs to modify synaptic efficacy following NMDA receptor activation. Our results suggest a role for NO as such a messenger during development of the retinotectal projection.

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“…ADP-ribosylated actin acts as an actin capping protein inhibiting microfilament elongation at the barbed ends. Some other factors like clostridial toxins, for example botulinum C2 toxin, can also induce ADP-ribosylation of actin (for a review see Aktories, 1990). It is of interest that benzamide, which is an inhibitor of some ADP-ribosylating enzymes, causes dispersion of stress fibers rather than their stabilization.…”

Section: Resultsmentioning

confidence: 99%

Benzamide‐induced changes in the actin cytoskeleton in human skin fibroblasts.

Korohoda

Michalik

Pierzchalska

1994

Cell Biology International

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The incubation of human skin fibroblasts in the presence of 10 mM benzamide in Joklik's modification of Eagle's Minimal Essential Medium caused an extensive reorganization of actin filaments. The disappearance of stress fibers and changes in cell morphology were observed, whereas no changes in the microtubule architecture were noticed. The observed effects appeared fully reversible within 3 hours after the removal of benzamide. The results are discussed in relation to the two known activities of benzamide as an anaesthetic and an inhibitor of ADP-ribosylation.

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ADP-ribosylation of actin

Cited by 11 publications

References 16 publications

cGMP-dependent ADP depolymerization of actin mediates estrogen increase in cervical epithelial permeability

cGMP-dependent ADP depolymerization of actin mediates estrogen increase in cervical epithelial permeability

Exogenous nitric oxide causes collapse of retinal ganglion cell axonal growth cones in vitro

Benzamide‐induced changes in the actin cytoskeleton in human skin fibroblasts.

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