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Experientia1995; 51(8); 804-808; doi: 10.1007/BF01922434

Sr2+ can become incorporated into an agonist-sensitive, cytoplasmic Ca2+ store in a cell line derived from the equine sweat gland epithelium.

Abstract: We have explored the properties of a Ca(2+)-dependent cell-signalling pathway that becomes active when cultured equine sweat gland cells are stimulated with ATP. The ATP-regulated, Ca(2+)-influx pathway allowed Sr2+ to enter the cytoplasm but permitted only a minimal influx of Ba2+. Experiments in which cells were repeatedly stimulated with ATP suggested that Sr2+, but not Ba2+, could become incorporated into the agonist-sensitive, cytoplasmic Ca2+ store. Further evidence for this was provided by experiments using ionomycin, a Ca2+ ionophore which has no affinity for Sr2+.
Publication Date: 1995-08-16 PubMed ID: 7649240DOI: 10.1007/BF01922434Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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This research explores how Strontium (Sr2+) can be integrated into an ATP-sensitive calcium (Ca2+) store in sweat gland cells from horses. The study involved experiments on cultured cells, evaluating how the influx of Sr2+ and Barium (Ba2+) are controlled, and unveiling that only Sr2+ could be incorporated into the cytoplasmic Ca2+ store, a key element in cell signaling.

Study of Ca(2+)-Dependent Cell-Signalling Pathway

  • The researchers focused on a specific cell-signaling pathway in cultured equine sweat gland cells that can be activated with Adenosine Triphosphate (ATP).
  • ATP is a primary molecule that carries energy within cells and thus plays a crucial role in managing a range of physiological processes in the cells.

Investigating Role of Sr2+ and Ba2+

  • The research discovered that the ATP-controlled Ca(2+) influx pathway allowed Sr2+ to enter the cytoplasm, whereas the influx of Ba2+ was minimal.
  • Influx pathway describes the mechanisms by which certain ions or molecules enter a cell.
  • It’s also suggested Sr2+, unlike Ba2+, could be incorporated into what the researchers term the ‘agonist-sensitive, cytoplasmic Ca2+ store’.
  • The ‘agonist-sensitive, cytoplasmic Ca2+ store’ could refer to a pool or storage of Ca2+ ion regulated by ATP within the cell’s cytoplasm which is ready to be used when needed or upon stimulation.

Ionomycin Experiment

  • Additional evidence to back the theory that Sr2+ could be incorporated into the cytoplasmic Ca2+ store was provided by experiments involving ionomycin.
  • Ionomycin is a type of calcium ionophore – substances which are able to form a structure that can shuttle ions across the cell membrane.
  • In this context, ionomycin provided a way of verifying that Sr2+ was indeed being integrated into the intracellular store since ionomycin has no affinity for Sr2+, indicating that if Sr2+ was present, it must have used another pathway to enter the Ca2+ storage site.

Cite This Article

APA
Ko WH, Pediani JD, Bovell DL, Wilson SM. (1995). Sr2+ can become incorporated into an agonist-sensitive, cytoplasmic Ca2+ store in a cell line derived from the equine sweat gland epithelium. Experientia, 51(8), 804-808. https://doi.org/10.1007/BF01922434

Publication

ISSN: 0014-4754
NlmUniqueID: 0376547
Country: Switzerland
Language: English
Volume: 51
Issue: 8
Pages: 804-808

Researcher Affiliations

Ko, W H
  • Division of Neuroscience and Biomedical Systems, University of Glasgow, Scotland, UK.
Pediani, J D
    Bovell, D L
      Wilson, S M

        MeSH Terms

        • Adenosine Triphosphate / metabolism
        • Animals
        • Barium / metabolism
        • Calcium / metabolism
        • Cell Line
        • Cytoplasm / metabolism
        • Epithelium
        • Fura-2
        • Horses
        • In Vitro Techniques
        • Receptors, Purinergic / physiology
        • Strontium / metabolism
        • Sweat Glands / cytology
        • Sweat Glands / metabolism

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        Citations

        This article has been cited 1 times.
        1. Ko WH, Chan HC, Wong PY. Anion secretion induced by capacitative Ca2+ entry through apical and basolateral membranes of cultured equine sweat gland epithelium. J Physiol 1996 Nov 15;497 ( Pt 1)(Pt 1):19-29.
          doi: 10.1113/jphysiol.1996.sp021746pubmed: 8951708google scholar: lookup