Mechanisms of microcystin-LR-induced cytoskeletal disruption in animal cells

Zhou, Mi; Tu, Wei-wei; Xu, Jin

doi:10.1016/j.toxicon.2015.05.005

Cited by 81 publications

(57 citation statements)

References 139 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Douglas et al [49] reported that through the inhibition of PP1/2A, MC-LR may be implicated in the regulation of the activity of DNAdependent protein kinase (DNA-PK), which is required for DNA double strand break repair by the process of nonhomologous end joining (NHEJ). Moreover, the well-known effects of MC-LR on cytoskeletal disruption, metabolic disorder, cell cycle arrest, abnormal cell proliferation and cell death have been related to PP1/PP2A activity and the increased phosphorylation of certain proteins [48,50].…”

Section: Protein Phosphatasesmentioning

confidence: 99%

“…The cytoskeleton is a well-organized network of intracellular filaments and consists of three major components: microfilaments (MFs), microtubules (MTs) and intermediate filaments (IFs) [50]. These elements not only provide cellular architecture to maintain cell shape, cell division, migration, adhesion and contraction/relaxation, but also play a central role in signal transduction.…”

Section: Cytoskeleton Disruptionmentioning

confidence: 99%

See 1 more Smart Citation

Mechanisms of Microcystin-induced Cytotoxicity and Apoptosis

Chen¹,

Xie

2016

MRMC

View full text Add to dashboard Cite

Abstract:In recent years, cyanobacterial blooms have dramatically increased and become an ecological disaster worldwide. Cyanobacteria are also known to produce a wide variety of toxic secondary metabolites, i.e. cyanotoxins. Microcystins (MCs), a group of cyclic heptapeptides, are considered to be one of the most common and dangerous cyanobacterial toxins. MCs can be incorporated into the cells via organic anion transporting polypeptides (Oatps). It's widely accepted that inhibition of protein phosphatases (PPs) and induction of oxidative stress are the main toxic mechanisms of MCs. MCs are able to induce a variety of toxic cellular effects, including DNA damage, cytoskeleton disruption, mitochondria dysfunction, endoplasmic reticulum (ER) disturbance and cell cycle deregulation, all of which can contribute to apoptosis/programmed cell death. This review aimed to summarize the increasing data regarding the intracellular biochemical and molecular mechanisms of MC-induced toxicity and cell death.

show abstract

Section: Protein Phosphatasesmentioning

confidence: 99%

Section: Cytoskeleton Disruptionmentioning

confidence: 99%

Mechanisms of Microcystin-induced Cytotoxicity and Apoptosis

Chen¹,

Xie

2016

MRMC

View full text Add to dashboard Cite

show abstract

“…At a high dose, MCs cause massive changes in cell morphology through cytoskeletal rearrangements and oxidative stress, leading to loss of cell-to-cell adhesion and cell death [175][176][177]. In a chronic model of low level exposure, constant mild PP2A inhibition leads to reprogramming of the cell, runaway cell growth, and tumor production, analogous to the effects of endogenous human protein CIP2A (cancerous inhibitor of PP2A) associated with breast and lung cancer [178][179][180][181].…”

Section: Effects On Other Tissues From Oral Exposure To Mcsmentioning

confidence: 99%

Cyanobacterial Toxins of the Laurentian Great Lakes, their Toxicological Effects, and Numerical Limits in Drinking Water

Miller

Beversdorf

Weirich

et al. 2017

Preprint

View full text Add to dashboard Cite

Cyanobacteria are ubiquitous phototrophic bacteria that inhabit diverse environments across the planet. They dominate many eutrophic lakes impacted by excess nitrogen (N) and phosphorus (P) forming dense accumulations of biomass known as cyanobacterial harmful algal blooms or cyanoHABs. Their dominance in eutrophic lakes is attributed to a variety of unique adaptations including N and P concentrating mechanisms, N fixation, colony formation that inhibits predation, vertical movement via gas vesicles, and the production of toxic or otherwise bioactive molecules. While some of these molecules have been explored for their medicinal benefits, others are potent toxins harmful to humans, animals, and other wildlife known as cyanotoxins. In humans these cyanotoxins affect various tissues, including the liver, central and peripheral nervous system, kidneys, and reproductive organs among others. They induce acute effects at low doses in the parts-per-billion range and some are tumor promoters linked to chronic diseases such as liver and colorectal cancer. The occurrence of cyanoHABs and cyanotoxins in lakes presents challenges for maintaining safe recreational aquatic environments and the production of potable drinking water. CyanoHABs are a growing problem in the North American (Laurentian) Great Lakes basin. This review summarizes information on the occurrence of cyanoHABs in the Great Lakes, toxicological effects of cyanotoxins, and appropriate numerical limits on cyanotoxins in finished drinking water.

show abstract

“…It inhibits the activity of the serine/threonine protein phosphatase PP1 and PP2A, interrupts signaling transduction, induces oxidative stress, and disrupts Na + /K + ATPase pumps (Alexandre and Vitor, 2010). Many published papers have described that microcystins could cause dysfunction in mitochondrion, endoplasmic reticulum, and cytoskeleton etc (Rogers et al, 2011;Zhang et al, 2013;Zhou et al, 2015). The expression of many proteins of these organelles has been affected due to MCLR exposure (Chen et al, 2013;Rymuszka, 2013).…”

Section: Introductionmentioning

confidence: 99%

“…The expression of many proteins of these organelles has been affected due to MCLR exposure (Chen et al, 2013;Rymuszka, 2013). The structure and function of ribosome are tightly connected with other cellular organelles such as mitochondrion, endoplasmic reticulum, and cytoskeleton (Zhou et al, 2015;Zhao et al, 2015), but the impact of ribosomal structure and function by microcystins is still unknown, especially the change of ribosomal protein expression.…”

Section: Introductionmentioning

confidence: 99%

Systematic identification of seven ribosomal protein genes in bighead carp and their expression in response to microcystin-LR

et al. 2016

View full text Add to dashboard Cite

-Microcystin-LR (MCLR) is one of the most toxic cyanotoxins produced in algal blooms. The toxic effects of MCLR on the expression of some organelles genes (mitochondrion, endoplasmic reticulum, and cytoskeleton etc) have been widely investigated, but little is known how it impacts on the expression of ribosomal genes. In this study we identified seven ribosomal protein genes RPS6, RPS12, RPS24, RPS27a, RPL12, RPL27 and RPL29 in bighead carp (Aristichthys nobilis), whose expression was regulated by MCLR. The amino acid sequences of those 7 genes shared more than 90% identity with corresponding sequences from zebrafish, and were well conserved throughout evolution. The 3D structure prediction showed that the structures of these ribosomal proteins were conserved, but had species specificity. Q-PCR analysis revealed that expression of seven genes changed dramatically at 3 hr, then went back to a moderate change-level at 24 hr in almost all tested tissues (liver, kidney, intestine, heart, spleen and gill) post MCLR injection, but in brain expression of the seven genes stayed same as the normal level. This study will help us to know not only about the evolution and functions of ribosomal proteins in anti-MCLR response in bighead carp, but also about the MCLR toxicity and its impact on aquaculture and human health.

show abstract

Mechanisms of microcystin-LR-induced cytoskeletal disruption in animal cells

Cited by 81 publications

References 139 publications

Mechanisms of Microcystin-induced Cytotoxicity and Apoptosis

Mechanisms of Microcystin-induced Cytotoxicity and Apoptosis

Cyanobacterial Toxins of the Laurentian Great Lakes, their Toxicological Effects, and Numerical Limits in Drinking Water

Systematic identification of seven ribosomal protein genes in bighead carp and their expression in response to microcystin-LR

Contact Info

Product

Resources

About