ArticleThe journal of venomous animals and toxins including tropical diseases2018
Cell migration inhibition activity of a non-RGD disintegrin from
Article in The journal of venomous animals and toxins including tropical diseases, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 15 citations in OpenAlex.
- Snake venom disintegrins update: insights about new findings.The journal of venomous animals and toxins including tropical diseases · 2023Review
- The Effects of αvβ3 Integrin Blockage in Breast Tumor and Endothelial Cells under Hypoxia In Vitro.International journal of molecular sciences · 2022Article
- Review
- Anticancer potential of nanogold conjugated toxin GNP-NN-32 fromThe journal of venomous animals and toxins including tropical diseases · 2020Article
- Cytotoxic and anticancer properties of the Malaysian mangrove pit viper (The journal of venomous animals and toxins including tropical diseases · 2020Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundIn recent decades, snake venom disintegrins have received special attention due to their potential use in anticancer therapy. Disintegrins are small and cysteine-rich proteins present in snake venoms and can interact with specific integrins to inhibit their activities in cell-cell and cell-ECM interactions. These molecules, known to inhibit platelet aggregation, are also capable of interacting with certain cancer-related integrins, and may interfere in important processes involved in carcinogenesis. Therefore, disintegrin from
methodsBased on previous studies, disintegrin was isolated by FPLC, through two chromatographic steps, both on reversed phase C-18 columns. The isolated disintegrin was structurally characterized by Tris-Tricine-SDS-PAGE, mass spectrometry and N-terminal sequencing. For the functional assays, MTT and wound-healing assays were performed in order to investigate cytotoxicity and effect on cell migration in vitro, respectively.
resultsDisintegrin presented a molecular mass of 7287.4 Da and its amino acid sequence shared similarity with the disintegrin domain of P-II metalloproteases. Using functional assays, the disintegrin showed low cytotoxicity (15% and 17%, at 3 and 6 μg/mL, respectively) after 24 h of incubation and in the wound-healing assay, the disintegrin (3 μg/mL) was able to significantly inhibit cell migration (24%,
conclusionThus, our results demonstrate that non-RGD disintegrin from
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