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

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,...

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Bibliographic Details
Published in:Histochemistry and cell biology 1999-06, Vol.111 (6), p.453-459
Main Authors: Mueller, A, Bächi, T, Höchli, M, Schäfer, B W, Heizmann, C W
Format: Article
Language:English
Subjects:
Adenocarcinoma
Adenosine Diphosphate Ribose - analogs & derivatives
Adenosine Diphosphate Ribose - pharmacology
Breast
Calcimycin
Calcium (intracellular)
Calcium - metabolism
Calcium homeostasis
Calcium-binding protein
Calcium-Binding Proteins - analysis
Cell Cycle Proteins
Cervical cancer
Cervical carcinoma
Cervix
Chemotactic Factors - analysis
Confocal microscopy
Cyclic ADP-Ribose
EF-hand
Enzyme Inhibitors - pharmacology
HeLa Cells
Homeostasis
Humans
Localization
Metastases
Proteins
S100 Calcium Binding Protein A6
S100 Calcium-Binding Protein A4
S100 Proteins - analysis
S100A4 protein
Subcellular Fractions
Thapsigargin
Thapsigargin - pharmacology
Tumor cell lines
Tumor cells
Tumor Cells, Cultured
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Summary: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.
ISSN:0948-6143
1432-119X
DOI:10.1007/s004180050381