ArticleCell biochemistry and biophysics2020
Fumonisin B1 Affects the Biophysical Properties, Migration and Cytoskeletal Structure of Human Umbilical Vein Endothelial Cells.
Article in Cell biochemistry and biophysics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Aflatoxins and Fumonisins: Assessment Methods, Biomarkers of Exposure, Modified Forms, Co-Exposure, and Impact on Human Health.Molecules (Basel, Switzerland) · 2026Review
- Fumonisin B1 Exerts Immunosuppressive Effects Through Cytoskeleton Remodeling and Function Attenuation of Mature Dendritic Cells.International journal of molecular sciences · 2025Article
- Article
- Current Knowledge of Individual and Combined Toxicities of Aflatoxin B1 and Fumonisin B1 In Vitro.Toxins · 2023Review
- Fumonisin BToxins · 2021Article
- Grape Seed Proanthocyanidin Ameliorates FBToxins · 2021Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Fumonisin B1 (FB1) is an important mycotoxin in nature and is a serious threat to human and animal health, but its specific target and molecular mechanism of the toxicity and potential carcinogenicity remain unclear. In this study, we first detected the effects of FB1 on the cell viability, biophysical properties, migration ability, and reactive oxygen species (ROS) of human umbilical vein endothelial cells (HUVECs). Subsequently, changes in the cytoskeletal structure and its binding proteins were analyzed by immunofluorescence and real-time PCR, respectively. The results showed that FB1 could inhibit the viability of HUVECs in a dose-dependent manner. After treatment of HUVECs with FB1, the hypotonic resistance, cell surface charges, cell membrane fluidity, and migration ability were weakened, whereas the ROS levels were significantly increased. Moreover, the cytoskeletal structure of the HUVECs was significantly changed, and the mRNA expression of some important actin-binding proteins was altered. Therefore, this study revealed that FB1 can affect the migration and cytoskeletal structure of HUVECs, which provides a new perspective for further understanding the molecular mechanisms of FB1 toxicity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.