Open AccessSpatial Distribution of Intracellular Ion Concentrations in Aggregate‐Forming HeLa Cells Analyzed by μ‐XRF Imaging
Author(s) -
Gräfenstein Andreas,
Rumancev Christoph,
Pollak Roland,
Hämisch Benjamin,
Galbierz Vanessa,
Schroeder Walter H.,
Garrevoet Jan,
Falkenberg Gerald,
Vöpel Tobias,
Huber Klaus,
Ebbinghaus Simon,
Rosenhahn Axel
Publication year - 2022
Publication title -
chemistryopen
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.644
H-Index - 29
ISSN - 2191-1363
DOI - 10.1002/open.202200024
Subject(s) - intracellular , hela , huntingtin , chemistry , biophysics , potassium , amyloid (mycology) , fluorescence , biochemistry , microbiology and biotechnology , biology , cell , gene , inorganic chemistry , physics , organic chemistry , quantum mechanics , mutant
Protein aggregation is a hallmark of several severe neurodegenerative disorders such as Huntington's, Parkinson's, or Alzheimer's disease. Metal ions play a profound role in protein aggregation and altered metal‐ion homeostasis is associated with disease progression. Here we utilize μ‐X‐ray fluorescence imaging in combination with rapid freezing to resolve the elemental distribution of phosphorus, sulfur, potassium, and zinc in huntingtin exon‐1‐mYFP expressing HeLa cells. Using quantitative XRF analysis, we find a threefold increase in zinc and a 10‐fold enrichment of potassium that can be attributed to cellular stress response. While the averaged intracellular ion areal masses are significantly different in aggregate‐containing cells, a local intracellular analysis shows no different ion content at the location of intracellular inclusion bodies. The results are compared to corresponding experiments on HeLa cells forming pseudoisocyanine chloride aggregates. As those show similar results, changes in ion concentrations are not exclusively linked to huntingtin exon‐1 amyloid formation.