Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Guan, Feng, Li, Xiang, Guo, Jia, Yang, Ganglong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Dove Medical Press 2015
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
_version_ 1782400625914413056
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
work_keys_str_mv AT guanfeng gangliosidemagnetosomecomplexformationenhancesuptakeofgangliosidesbycells
AT lixiang gangliosidemagnetosomecomplexformationenhancesuptakeofgangliosidesbycells
AT guojia gangliosidemagnetosomecomplexformationenhancesuptakeofgangliosidesbycells
AT yangganglong gangliosidemagnetosomecomplexformationenhancesuptakeofgangliosidesbycells
AT lixiang gangliosidemagnetosomecomplexformationenhancesuptakeofgangliosidesbycells