Ganglioside-magnetosome complex formation enhances uptake of gangliosides by cells

Feng Guan,1 Xiang Li,1 Jia Guo,1 Ganglong Yang,1 Xiang Li2 1The Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, 2Wuxi Medical School, Jiangnan University, Wuxi, People’s Republic of China Abstract: Bacterial magnetosomes, because...

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Autores principales: Guan F, Li X, Guo J, Yang G
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Publicado: Dove Medical Press 2015
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spelling oai:doaj.org-article:dce3d5f33cea456e8f53882e5a01fa5e2021-12-02T05:04:30ZGanglioside-magnetosome complex formation enhances uptake of gangliosides by cells1178-2013https://doaj.org/article/dce3d5f33cea456e8f53882e5a01fa5e2015-11-01T00:00:00Zhttps://www.dovepress.com/ganglioside-magnetosome-complex-formation-enhances-uptake-of-gangliosi-peer-reviewed-article-IJNhttps://doaj.org/toc/1178-2013Feng Guan,1 Xiang Li,1 Jia Guo,1 Ganglong Yang,1 Xiang Li2 1The Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, 2Wuxi Medical School, Jiangnan University, Wuxi, People’s Republic of China Abstract: 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 (GM1 or GM3) on the magnetosome by mild ultrasonic treatment. The maximum of 11.7±1.2 µg GM1 and 11.6±1.5 µg GM3 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 GM1-magnetosome complex resulted in the greatest enhancement of ganglioside incorporation by cells. GM3-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. Keywords: bacterial magnetosome, nanoparticle, cellular uptake, ganglioside, inhibitionGuan FLi XGuo JYang GLi XDove Medical PressarticleMedicine (General)R5-920ENInternational Journal of Nanomedicine, Vol 2015, Iss default, Pp 6919-6930 (2015)
institution DOAJ
collection DOAJ
language EN
topic Medicine (General)
R5-920
spellingShingle Medicine (General)
R5-920
Guan F
Li X
Guo J
Yang G
Li X
Ganglioside-magnetosome complex formation enhances uptake of gangliosides by cells
description Feng Guan,1 Xiang Li,1 Jia Guo,1 Ganglong Yang,1 Xiang Li2 1The Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, 2Wuxi Medical School, Jiangnan University, Wuxi, People’s Republic of China Abstract: 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 (GM1 or GM3) on the magnetosome by mild ultrasonic treatment. The maximum of 11.7±1.2 µg GM1 and 11.6±1.5 µg GM3 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 GM1-magnetosome complex resulted in the greatest enhancement of ganglioside incorporation by cells. GM3-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. Keywords: bacterial magnetosome, nanoparticle, cellular uptake, ganglioside, inhibition
format article
author Guan F
Li X
Guo J
Yang G
Li X
author_facet Guan F
Li X
Guo J
Yang G
Li X
author_sort Guan F
title Ganglioside-magnetosome complex formation enhances uptake of gangliosides by cells
title_short 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_sort ganglioside-magnetosome complex formation enhances uptake of gangliosides by cells
publisher Dove Medical Press
publishDate 2015
url https://doaj.org/article/dce3d5f33cea456e8f53882e5a01fa5e
work_keys_str_mv AT guanf gangliosidemagnetosomecomplexformationenhancesuptakeofgangliosidesbycells
AT lix gangliosidemagnetosomecomplexformationenhancesuptakeofgangliosidesbycells
AT guoj gangliosidemagnetosomecomplexformationenhancesuptakeofgangliosidesbycells
AT yangg gangliosidemagnetosomecomplexformationenhancesuptakeofgangliosidesbycells
AT lix gangliosidemagnetosomecomplexformationenhancesuptakeofgangliosidesbycells
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