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Direct electrochemical observation of glucosidase activity in isolated single lysosomes from a living cell
The protein activity in individual intracellular compartments in single living cells must be analyzed to obtain an understanding of protein function at subcellular locations. The current methodology for probing activity is often not resolved to the level of an individual compartment, and the results...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
National Academy of Sciences
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5910846/ https://www.ncbi.nlm.nih.gov/pubmed/29610324 http://dx.doi.org/10.1073/pnas.1719844115 |
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author | Pan, Rongrong Xu, Mingchen Burgess, James D. Jiang, Dechen Chen, Hong-Yuan |
author_facet | Pan, Rongrong Xu, Mingchen Burgess, James D. Jiang, Dechen Chen, Hong-Yuan |
author_sort | Pan, Rongrong |
collection | PubMed |
description | The protein activity in individual intracellular compartments in single living cells must be analyzed to obtain an understanding of protein function at subcellular locations. The current methodology for probing activity is often not resolved to the level of an individual compartment, and the results provide an extent of reaction that is averaged from a group of compartments. To address this technological limitation, a single lysosome is sorted from a living cell via electrophoresis into a nanocapillary designed to electrochemically analyze internal solution. The activity of a protein specific to lysosomes, β-glucosidase, is determined by the electrochemical quantification of hydrogen peroxide generated from the reaction with its substrate and the associated enzymes preloaded in the nanocapillary. Sorting and assaying multiple lysosomes from the same cell shows the relative homogeneity of protein activity between different lysosomes, whereas the protein activity in single lysosomes from different cells of the same type is heterogeneous. Thus, this study for the analysis of protein activity within targeted cellular compartments allows direct study of protein function at subcellular resolution and provides unprecedented information about the homogeneity within the lysosomal population of a single cell. |
format | Online Article Text |
id | pubmed-5910846 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | National Academy of Sciences |
record_format | MEDLINE/PubMed |
spelling | pubmed-59108462018-04-25 Direct electrochemical observation of glucosidase activity in isolated single lysosomes from a living cell Pan, Rongrong Xu, Mingchen Burgess, James D. Jiang, Dechen Chen, Hong-Yuan Proc Natl Acad Sci U S A Physical Sciences The protein activity in individual intracellular compartments in single living cells must be analyzed to obtain an understanding of protein function at subcellular locations. The current methodology for probing activity is often not resolved to the level of an individual compartment, and the results provide an extent of reaction that is averaged from a group of compartments. To address this technological limitation, a single lysosome is sorted from a living cell via electrophoresis into a nanocapillary designed to electrochemically analyze internal solution. The activity of a protein specific to lysosomes, β-glucosidase, is determined by the electrochemical quantification of hydrogen peroxide generated from the reaction with its substrate and the associated enzymes preloaded in the nanocapillary. Sorting and assaying multiple lysosomes from the same cell shows the relative homogeneity of protein activity between different lysosomes, whereas the protein activity in single lysosomes from different cells of the same type is heterogeneous. Thus, this study for the analysis of protein activity within targeted cellular compartments allows direct study of protein function at subcellular resolution and provides unprecedented information about the homogeneity within the lysosomal population of a single cell. National Academy of Sciences 2018-04-17 2018-04-02 /pmc/articles/PMC5910846/ /pubmed/29610324 http://dx.doi.org/10.1073/pnas.1719844115 Text en Copyright © 2018 the Author(s). Published by PNAS. https://creativecommons.org/licenses/by-nc-nd/4.0/ This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) . |
spellingShingle | Physical Sciences Pan, Rongrong Xu, Mingchen Burgess, James D. Jiang, Dechen Chen, Hong-Yuan Direct electrochemical observation of glucosidase activity in isolated single lysosomes from a living cell |
title | Direct electrochemical observation of glucosidase activity in isolated single lysosomes from a living cell |
title_full | Direct electrochemical observation of glucosidase activity in isolated single lysosomes from a living cell |
title_fullStr | Direct electrochemical observation of glucosidase activity in isolated single lysosomes from a living cell |
title_full_unstemmed | Direct electrochemical observation of glucosidase activity in isolated single lysosomes from a living cell |
title_short | Direct electrochemical observation of glucosidase activity in isolated single lysosomes from a living cell |
title_sort | direct electrochemical observation of glucosidase activity in isolated single lysosomes from a living cell |
topic | Physical Sciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5910846/ https://www.ncbi.nlm.nih.gov/pubmed/29610324 http://dx.doi.org/10.1073/pnas.1719844115 |
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