Sr2+ can become incorporated into an agonist-sensitive, cytoplasmic Ca2+ store in a cell line derived from the equine sweat gland epithelium.
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+.
Ko
W H
WH
Division of Neuroscience and Biomedical Systems, University of Glasgow, Scotland, UK.
Pediani
J D
JD
Bovell
D L
DL
Wilson
S M
SM
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001464:Barium / Q000378:metabolism; D002118:Calcium / Q000378:metabolism*; D002460:Cell Line; D003593:Cytoplasm / Q000378:metabolism; D004848:Epithelium; D016257:Fura-2; D006736:Horses; D066298:In Vitro Techniques; D011983:Receptors, Purinergic / Q000502:physiology; D013324:Strontium / Q000378:metabolism*; D013545:Sweat Glands / Q000166:cytology / Q000378:metabolism*
D011983:Receptors, Purinergic; D001464:Barium; D000255:Adenosine Triphosphate; D002118:Calcium; D016257:Fura-2; D013324:Strontium