Anti-actin stains synapses

Toh, Ban Hock; Gallichio, H. A.; Jeffrey, Peter L.; Livett, Bruce G.; Muller, HK; Cauchi, Maurice N.; Clarke, Frank M.

doi:10.1038/264648a0

Cited by 66 publications

(19 citation statements)

References 9 publications

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“…β-Actin largely exists as a submembranous cytoskeleton in synaptic areas such as pre-synaptic nerve endings and post-synaptic dendrites (Ratner and Mahler 1983;Toh et al 1976). Playing a major role in neurite growth, cell adhesion, synapse information and exocytosis of neurotransmitters, β-actin was reported to be affected in the brains treated with MC-LR (Wang et al 2010).…”

Section: Cytoskeleton Disruptionmentioning

confidence: 99%

A review of neurotoxicity of microcystins

Chen

Fan

et al. 2016

Environ Sci Pollut Res

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Cyanobacterial blooms-produced microcystins are secondary metabolites which can accumulate in the food chain and contaminate water, thus posing a potential threat to the health of aquatic animals and even humans. Microcystin toxicity affects not only the liver but also the other organs, i.e., the brain. The serious neurotoxicity effects caused by microcystins then lead to various symptoms. This review focuses on the neurotoxicity of microcystins. Microcystins can cross bloodbrain barrier with the transport of Oatps/OATPs, causing neurostructural, functional, and behavioral changes. In this review, potential uptake mechanisms and neurotoxicity mechanisms are summarized, including neurotransmissions, neurochannels, signal transduction, oxidative stress, and cytoskeleton disruption. However, further researches are needed for detailed studies on signaling pathways and the downstream pathways of neurotoxicity of microcystins.

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Section: Cytoskeleton Disruptionmentioning

confidence: 99%

A review of neurotoxicity of microcystins

Chen

Fan

et al. 2016

Environ Sci Pollut Res

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“…This approach already has proved useful in demonstrating the association of a variety of proteins-such as tubulin (9), microtubule-associated protein (10), and calmodulin (11)-with PSDs in brain sections and, perhaps more significantly, in showing that other proteins belonging to neighboring structures are not associated with PSDs (8). Antiactin staining of brain sections for light microscopy has suggested an association of actin with synapses (12), but so far this has not been followed up at the ultrastructural level. Such a determination ofthe ultrastructural distribution of actin is ofparticular interest because of the variety of roles that have been suggested for synaptic actin.…”

mentioning

confidence: 99%

High actin concentrations in brain dendritic spines and postsynaptic densities.

Matus¹,

Ackermann²,

Pehling³

et al. 1982

Proc. Natl. Acad. Sci. U.S.A.

354

241

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Antibodies against actin were used to corroborate the presence ofactin as a major component protein ofisolated brain postsynaptic densities. The same antibodies also were used as an immunohistochemical stain to study the distribution of actin in sections of intact brain tissue. This showed two major sites where actin is concentrated: smooth muscle cells around blood vessels and postsynaptic sites. In the postsynaptic area the highest concentration of actin occurs in postsynaptic densities and there also is intense staining in the surrounding cytoplasm, especially within dendritic spines. Antiactin staining was much weaker in other parts of neurons and in glial cells. The high concentration of actin in dendritic spines may be related to shape changes that these structures have been found to undergo in response to prolonged afferent stimulation.

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“…Those authors have suggested that SMA serum contains antibody to actin, since its reactivity with smooth muscle is neutralized by prior absorption with platelet actin. The anti-actin specificity of SMA sera from patients with active chronic hepatitis has since been confirmed (Botazzo et al, 1976;Lidman et al, 1976;Toh et al, 1976d).…”

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confidence: 94%