Lipopolysaccharide‐caused fragmentation of individual microtubules in vitro observed by video‐enhanced differential interference contrast microscopy

Böhm, Konrad J.; Vater, W; Rußwurm, Stefan; Reinhart, Konrad; Unger, Eberhard

doi:10.1016/s0014-5793(98)00220-8

Cited by 9 publications

(2 citation statements)

References 17 publications

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“…With biochemical and electron microscopy analyses, it has been shown that LPS can bind to microtubules and inhibit the polymerization of microtubules in vitro in a LPS concentration-dependent process (35). At lower concentrations, LPS selectively displaced the microtubule-associated proteins from the polymerized microtubules, whereas at higher concentrations, LPS inhibited the polymerization of microtubules (5). In the present study, LPS exposure reduced microtubule polymerization rapidly, within 1 min (Fig.…”

Section: Discussionsupporting

confidence: 55%

Role of microtubules in LPS-induced macrophage inflammatory protein-2 production from rat pneumocytes

Isowa

Keshavjee

Liu

2000

American Journal of Physiology-Lung Cellular and Molecular Phys

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We have recently demonstrated that primary cultured rat pneumocytes produce macrophage inflammatory protein-2 (MIP-2) in response to lipopolysaccharide (LPS) stimulation. In this study, we found that brefeldin A, by blocking anterograde transport from the endoplasmic reticulum (ER) to the Golgi apparatus, decreased LPS-induced MIP-2 in the culture medium and increased its storage in cells. This suggests that MIP-2 is secreted via a pathway from the ER to the Golgi apparatus, a process commonly regulated by microtubules. We further found that LPS induced depolymerization of microtubules as early as 1 min after LPS stimulation, and it lasted at least for 4 h. Preventing depolymerization of microtubules with paclitaxel (Taxol; 10 nM to 10 microM) partially inhibited LPS-induced MIP-2 production, whereas the microtubule-depolymerizing agents colchicine (1-10 microM) and nocodazole (1-100 microM) increased LPS-induced MIP-2 protein production without affecting MIP-2 mRNA expression. These results suggest that in pneumocytes, LPS-induced microtubule depolymerization is involved in LPS-induced MIP-2 production and that secretion of MIP-2 from pneumocytes is via the ER-Golgi pathway.

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Section: Discussionsupporting

confidence: 55%

Role of microtubules in LPS-induced macrophage inflammatory protein-2 production from rat pneumocytes

Isowa

Keshavjee

Liu

2000

American Journal of Physiology-Lung Cellular and Molecular Phys

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“…LPS targeted to intracellular microtubule architecture results in microtubule disassembly [32]. LPS can also bind to tubulin to cause microtubule fragmentation and shortening [33]. In the present study, after 6 or 24 h exposure to LPS, the comprehensive profiling suggested that protein-coding genes were frequently enriched in GO:007023 (post-chaperonin tubulin folding change).…”

Section: Lps Is Toxic To Cultured Eukaryotic Cells and Inhibites In Vitro Microtubulementioning

confidence: 47%

mRNA and Long Non-coding RNA Expression Profiles in Rats Reveal Inflammatory Features in Sepsis-Associated Encephalopathy

2017

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Sepsis-associated encephalopathy (SAE) is related to cognitive sequelae in patients in the intensive care unit and can have serious impacts on quality of life after recovery. Although various pathogenic pathways are involved in SAE development, little is known concerning the global role of long non-coding RNAs (lncRNAs) in SAE. Herein, we employed transcriptome sequencing approaches to characterize the effects of lipopolysaccharide (LPS) on lncRNA expression patterns in brain tissue isolated from Sprague-Dawley rats with and without SAE. We performed high-throughput transcriptome sequencing after LPS was intraperitoneally injected and predicted targets and functions using bioinformatics tools. Subsequently, we explored the results in detail according to Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) analyses. LncRNAs were differentially expressed in brain tissue after LPS treatment. After 6 h of LPS exposure, expression of 400 lncRNAs were significantly changed, including an increase in 316 lncRNAs and a decrease in 84 lncRNAs. In addition, 155 mRNAs were differentially expressed, with 84 up-regulated and 71 down-regulated. At 24 h post-treatment, expression of 117 lncRNAs and 57 mRNAs was consistently elevated, while expression of 79 lncRNAs and 21 mRNAs was decreased (change >1.5-fold; p <0.05). We demonstrated for the first time that differentially expressed lncRNAs were predicted to be enriched in a post-chaperonin tubulin folding pathway (GO: 007023), which is closely related to the key step in the tubulin folding process. Interestingly, the predicted pathway (KEGG 04360: axon guidance) was significantly changed under the same conditions. These results reveal that LPS might influence the construction and polarization of microtubules, which exert predominant roles in synaptogenesis and related biofunctions in the rodent central nervous system (CNS). An inventory of LPS-modulated expression profiles from the rodent CNS is an important step toward understanding the function of mRNAs, including lncRNAs, and suggests that microtubule malformation and dysfunction may be involved in SAE pathogenesis.

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MICROTUBULE FORMATION AND KINESIN‐DRIVEN MICROTUBULE GLIDING IN VITRO IN THE PRESENCE OF LIPOPOLYSACCHARIDE

Böhm¹

1999

Cell Biology International

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Lipopolysaccharide (LPS) is a main trigger substance for the development of septic shock and multiple organ failure. We showed by turbidity measurements that LPS inhibits microtubule formation in a pH-dependent manner. Inhibition was found to be not only due to sequestration of MAP2 by LPS, but also of MAP1 and tau MAPs, indicating that LPS is able to react with a broad variety of MAPs. LPS-induced inhibition of microtubule formation could be compensated by additional tau or by addition of taxol. Dot blots revealed that LPS binds directly to tau, but seems not to bind to tubulin. As tau is expressed in various tissue types involved in multiorgan failure, it might be regarded as a further target for LPS action. In contrast, kinesin-dependent microtubule gliding was not affected by LPS. The toxin neither blocked the cargo (vesicle) nor the microtubule binding site of kinesin, suggesting a certain specificity of LPS-MAP interaction.

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Lipopolysaccharide‐caused fragmentation of individual microtubules in vitro observed by video‐enhanced differential interference contrast microscopy

Cited by 9 publications

References 17 publications

Role of microtubules in LPS-induced macrophage inflammatory protein-2 production from rat pneumocytes

Role of microtubules in LPS-induced macrophage inflammatory protein-2 production from rat pneumocytes

mRNA and Long Non-coding RNA Expression Profiles in Rats Reveal Inflammatory Features in Sepsis-Associated Encephalopathy

MICROTUBULE FORMATION AND KINESIN‐DRIVEN MICROTUBULE GLIDING IN VITRO IN THE PRESENCE OF LIPOPOLYSACCHARIDE

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