Paraquat induces irreversible actin cytoskeleton disruption in cultured human lung cells

Cappelletti, Graziella; Incani, Cristina; Maci, Rosalba

doi:10.1007/bf00756765

Cited by 23 publications

(14 citation statements)

References 26 publications

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“…The fat body is analogous to the mammalian liver and white adipose tissue, and is implicated in extending lifespan by altered IIS (7). Break-up of the fat body actin cytoskeleton by exposure to paraquat (51) further implies that vital physiological functions (52) are lost. Thus, our results indicate that excess mortality of vg Ϫ bees was linked to cellular damage that included a severe oxidative insult to the fat body.…”

Section: Figmentioning

confidence: 99%

Reproductive protein protects functionally sterile honey bee workers from oxidative stress

Seehuus

Norberg

Gimsa

et al. 2006

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

519

468

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Research on aging shows that regulatory pathways of fertility and senescence are closely interlinked. However, evolutionary theories on social species propose that lifelong care for offspring can shape the course of senescence beyond the restricted context of reproductive capability. These observations suggest that control circuits of aging are remodeled in social organisms with continuing care for offspring. Here, we studied a circuit of aging in the honey bee (Apis mellifera). The bee is characterized by the presence of a long-lived reproductive queen caste and a shorter-lived caste of female workers that are life-long alloparental care givers. We focus on the role of the conserved yolk precursor gene vitellogenin that, in Caenorhabditis elegans, shortens lifespan as a downstream element of the insulin͞insulin-like growth factor signaling cascade. Vitellogenin protein is synthesized at high levels in honey bee queens and is abundant in long-lived workers. We establish that vitellogenin gene activity protects worker bees from oxidative stress. Our finding suggests that one mechanistic explanation for patterns of longevity in bees is that a reproductive regulatory pathway has been remodeled to extend life. This perspective is of considerable relevance to research on longevity regulation that builds largely on inference from solitary model species.aging ͉ social evolution ͉ vitellogenin ͉ carbonylation ͉ RNA interference

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Section: Figmentioning

confidence: 99%

Reproductive protein protects functionally sterile honey bee workers from oxidative stress

Seehuus

Norberg

Gimsa

et al. 2006

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

519

468

View full text Add to dashboard Cite

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“…Therefore, the discrepancy between our results and their work is probably dependent on the difference in the cells examined. Cappelletti et al [20] also found differences in the cells examined following PQ-induced actin cytoskeleton disruption. On the other hand, we showed that the cells exposed to low levels of NOC18, 20-50 ~tM, improved MTT reduction activity.…”

Section: Discussionmentioning

confidence: 90%

The role of nitric oxide in paraquat-induced cytotoxicity in the human A549 lung carcinoma cell line

Tomita

Okuyama

Ishikawa

et al. 2001

Free Radical Research

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Paraquat (PQ) is a well-known pneumotoxicant that exerts its toxic effect by elevating intracellular levels of superoxide. In addition, production of pro-inflammatory cytokines has possibly been linked to PQ-induced inflammatory processes through reactive oxygen species (ROSs) and nitric oxide (NO). However, the role of NO in PQ-induced cell injury has been controversial. To explore this problem, we examined the effect of NO on A549 cells by exposing them to the exogenous NO donor NOC18 or to cytokines; tumor necrosis factor-alpha, interleukin-1 beta and interferon-gamma, as well as PQ. Although the exogenous NO donor on its own had no effect on the release of lactate dehydrogenase (LDH), remarkable release was observed when the cells were exposed to high concentrations of NOC18 and PQ. This cellular damage caused by 1 mM NOC18 plus 0.2 mM PQ was ascertained by phase contrast microscopy. On the other hand, NO derived from 25-50 microM NOC18 added into the medium improved the MTT reduction activity of mitochondria, suggesting a beneficial effect of NO on the cells. Incubation of A549 cells with cytokines increased in inducible NO synthase (iNOS) expression and nitrite accumulation, resulting in LDH release. PQ further potentiated this release. The increase in nitrite levels could be completely prevented by NOS inhibitors, while the leakage of LDH was not attenuated by the inhibition of NO production with them. On the other hand, ROS scavenging enzymes, superoxide dismutase and catalase, inhibited the leakage of LDH, whereas they had no effect on the increase in the nitrite level. These results indicate that superoxide, not NO, played a key role in the cellular damage caused by PQ/cytokines. Our in vitro models demonstrate that NO has both beneficial and deleterious actions, depending on the concentrations produced and model system used.

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“…In fact, S100A1 may be a molecule that directly links the cytoskeleton and cell growth. The observations that increases in microtubule stability can reverse neuronal cell death associated with Alzheimer's disease (29) as well as neurotoxic agents such as acrylamide and carbon disulfide (30), glutamate (31), and N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (32) suggest that S100A1 may be a suitable pharmacological target for treating neurological disorders. S100A1 antagonists may also be useful agents for the treatment of cancers such as renal carcinoma because these cancers express high levels of S100A1 (see Ref.…”

Section: Discussionmentioning

confidence: 99%

S100A1 Regulates Neurite Organization, Tubulin Levels, and Proliferation in PC12 Cells

Zimmer

Cornwall

Reynolds

et al. 1998

Journal of Biological Chemistry

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As a first step in determining what cellular processes are regulated by the calcium-modulated protein S100A1 isoform in neurons, the effects of ablated S100A1 expression on neurite organization and microtubule/tubulin levels in PC12 cells were examined. A mammalian expression vector containing the rat S100A1 cDNA in the antisense orientation with respect to a cytomegalovirus promoter was constructed and transfected into PC12 cells. Indirect immunofluorescence microscopy confirmed decreased S100A1 protein levels in all three stable transfectants (pAntisense clones) that expressed exogenous S100A1 antisense mRNA. In response to nerve growth factor, pAntisense clones extended significantly more neurites than control cells (4.01 ؎ 0.16 versus 2.93 ؎ 0.16 neurites/cell). This increase in neurite number was accompanied by an increase in total ␣-tubulin levels in untreated (4.0 ؎ 0.6 versus 1.76 ؎ 0.4 ng of ␣-tubulin/mg of total protein) and nerve growth factortreated pAntisense clones (4.15 ؎ 0.4 versus 2.04 ؎ 0.5 ng of ␣-tubulin/mg of total protein) when compared with control cells. At high cell densities, pAntisense clones exhibited a significant decrease in anchorage-dependent growth. In soft agar, pAntisense clones formed significantly more colonies (153 ؎ 8%) than control cells (116 ؎ 5%). However, the pAntisense soft agar colonies were significantly smaller than those observed in control cells (40.6 ؎ 3.0 versus 59.5 ؎ 1.2 m). These data suggest that cell density inhibits both anchorage-independent and -dependent growth of pAntisense clones. In summary, ablation of S100A1 expression in PC12 cells results in increased tubulin levels, altered neurite organization, and decreased cell growth. Thus, S100A1 may directly link the cytoskeleton and calcium signal transduction pathways to cell proliferation.The S100 protein family is a group of calcium-binding proteins that exhibit a high degree of conservation in amino acid sequence, secondary structure, and genomic organization (1-3). To date, there are 18 members of the S100 family, 13 of which are clustered in region q21 of human chromosome 1 (see Refs. 4 and 5). A new nomenclature that reflects the genomic organization of these proteins has recently been adopted, and S100␣ is now designated S100A1 and S100␤ is designated S100B (6). S100A1 and S100B were the original members of this family and have been implicated in a diverse group of cellular functions including cell-cell communication, cell growth, cell structure, energy metabolism, contraction, and intracellular calcium signal transduction (see Refs. 1 and 3).Because each S100 monomer contains two EF-hand high affinity calcium binding domains, they have been included in the S100-troponin-calmodulin superfamily of calcium-modulated proteins. These proteins have no known enzymatic activity and function by modulating the activity of other proteins termed target proteins. Calmodulin appears to be the "workhorse" in calcium signaling and to be responsible for generating the main events triggered by changes in intracell...

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Paraquat induces irreversible actin cytoskeleton disruption in cultured human lung cells

Cited by 23 publications

References 26 publications

Reproductive protein protects functionally sterile honey bee workers from oxidative stress

Reproductive protein protects functionally sterile honey bee workers from oxidative stress

The role of nitric oxide in paraquat-induced cytotoxicity in the human A549 lung carcinoma cell line

S100A1 Regulates Neurite Organization, Tubulin Levels, and Proliferation in PC12 Cells

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