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Ganglioside-magnetosome complex formation enhances uptake of gangliosides by cells
Bacterial magnetosomes, because of their nano-scale size, have a large surface-to-volume ratio and are able to carry large quantities of bioactive substances such as enzymes, antibodies, and genes. Gangliosides, a family of sialic acid-containing glycosphingolipids, function as distinctive cell surf...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Dove Medical Press
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4644171/ https://www.ncbi.nlm.nih.gov/pubmed/26609230 http://dx.doi.org/10.2147/IJN.S92228 |
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author | Guan, Feng Li, Xiang Guo, Jia Yang, Ganglong Li, Xiang |
author_facet | Guan, Feng Li, Xiang Guo, Jia Yang, Ganglong Li, Xiang |
author_sort | Guan, Feng |
collection | PubMed |
description | Bacterial magnetosomes, because of their nano-scale size, have a large surface-to-volume ratio and are able to carry large quantities of bioactive substances such as enzymes, antibodies, and genes. Gangliosides, a family of sialic acid-containing glycosphingolipids, function as distinctive cell surface markers and as specific determinants in cellular recognition and cell-to-cell communication. Exogenously added gangliosides are often used to study biological functions, transport mechanisms, and metabolism of their endogenous counterparts. Absorption of gangliosides into cells is typically limited by their tendency to aggregate into micelles in aqueous media. We describe here a simple strategy to remove proteins from the magnetosome membrane by sodium dodecyl sulfate treatment, and efficiently immobilize a ganglioside (GM(1) or GM(3)) on the magnetosome by mild ultrasonic treatment. The maximum of 11.7±1.2 µg GM(1) and 11.6±1.5 μg GM(3) was loaded onto 1 mg magnetosome, respectively. Complexes of ganglioside-magnetosomes stored at 4°C for certain days presented the consistent stability. The use of GM(1)-magnetosome complex resulted in the greatest enhancement of ganglioside incorporation by cells. GM(3)-magnetosome complex significantly inhibited EGF-induced phosphorylation of the epidermal growth factor receptor. Both of these effects were further enhanced by the presence of a magnetic field. |
format | Online Article Text |
id | pubmed-4644171 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Dove Medical Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-46441712015-11-25 Ganglioside-magnetosome complex formation enhances uptake of gangliosides by cells Guan, Feng Li, Xiang Guo, Jia Yang, Ganglong Li, Xiang Int J Nanomedicine Original Research Bacterial magnetosomes, because of their nano-scale size, have a large surface-to-volume ratio and are able to carry large quantities of bioactive substances such as enzymes, antibodies, and genes. Gangliosides, a family of sialic acid-containing glycosphingolipids, function as distinctive cell surface markers and as specific determinants in cellular recognition and cell-to-cell communication. Exogenously added gangliosides are often used to study biological functions, transport mechanisms, and metabolism of their endogenous counterparts. Absorption of gangliosides into cells is typically limited by their tendency to aggregate into micelles in aqueous media. We describe here a simple strategy to remove proteins from the magnetosome membrane by sodium dodecyl sulfate treatment, and efficiently immobilize a ganglioside (GM(1) or GM(3)) on the magnetosome by mild ultrasonic treatment. The maximum of 11.7±1.2 µg GM(1) and 11.6±1.5 μg GM(3) was loaded onto 1 mg magnetosome, respectively. Complexes of ganglioside-magnetosomes stored at 4°C for certain days presented the consistent stability. The use of GM(1)-magnetosome complex resulted in the greatest enhancement of ganglioside incorporation by cells. GM(3)-magnetosome complex significantly inhibited EGF-induced phosphorylation of the epidermal growth factor receptor. Both of these effects were further enhanced by the presence of a magnetic field. Dove Medical Press 2015-11-06 /pmc/articles/PMC4644171/ /pubmed/26609230 http://dx.doi.org/10.2147/IJN.S92228 Text en © 2015 Guan et al. This work is published by Dove Medical Press Limited, and licensed under Creative Commons Attribution – Non Commercial (unported, v3.0) License The full terms of the License are available at http://creativecommons.org/licenses/by-nc/3.0/. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed. |
spellingShingle | Original Research Guan, Feng Li, Xiang Guo, Jia Yang, Ganglong Li, Xiang Ganglioside-magnetosome complex formation enhances uptake of gangliosides by cells |
title | Ganglioside-magnetosome complex formation enhances uptake of gangliosides by cells |
title_full | Ganglioside-magnetosome complex formation enhances uptake of gangliosides by cells |
title_fullStr | Ganglioside-magnetosome complex formation enhances uptake of gangliosides by cells |
title_full_unstemmed | Ganglioside-magnetosome complex formation enhances uptake of gangliosides by cells |
title_short | Ganglioside-magnetosome complex formation enhances uptake of gangliosides by cells |
title_sort | ganglioside-magnetosome complex formation enhances uptake of gangliosides by cells |
topic | Original Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4644171/ https://www.ncbi.nlm.nih.gov/pubmed/26609230 http://dx.doi.org/10.2147/IJN.S92228 |
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