Subcellular distribution of S100 proteins in tumor cells and their relocation in response to calcium activation View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1999-06

AUTHORS

Andrea Mueller, Thomas Bächi, Matthias Höchli, Beat W. Schäfer, C. W. Heizmann

ABSTRACT

S100 proteins, a subgroup of the EF-hand Ca2+-binding protein family, regulate a variety of cellular processes via interaction with different target proteins. Several pathological disorders, including cancer, are linked to altered Ca2+ homeostasis and might involve the multifunctional S100 proteins, which are expressed in a cell- and tissue-specific manner. The present work demonstrates a distinct intracellular localization of S100A6, S100A4, and S100A2 in two tumor cell lines derived from metastatic epithelial breast adenocarcinoma (MDA-MB231) and cervical carcinoma (HeLa). Treatment of the cells by thapsigargin, the ionophore A23187, or cyclic ADP-ribose, to increase [Ca2+]i via different pathways, led to relocation of S100A6 and S100A4 but only partially of the nuclear S100A2, as demonstrated by confocal laser scanning microscopy. These findings support the hypothesis that S100 proteins could play a crucial role in the regulation of Ca2+ homeostasis in cancer cells. More... »

PAGES

453-459

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s004180050381

DOI

http://dx.doi.org/10.1007/s004180050381

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1031839092

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/10429967


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