Linked Life Data

9334235

Source:http://linkedlifedata.com/resource/pubmed/id/9334235

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
42
pubmed:dateCreated
1997-11-17
pubmed:abstractText
Treatment of NIH 3T3 cells with cytochalasin D (10 microM, 1 h at 37 degrees C) disrupted the actin cytoskeleton and changed the cells from a planar, extended morphology, to a rounded shape. Calcium mobilization by ATP or by platelet-derived growth factor was abolished, while the ability of thapsigargin (2 microM) to empty calcium stores and activate calcium influx was unaffected. Similar experiments with nocodazole to depolymerize the tubulin network yielded identical results. Platelet-derived growth factor induced an increase in inositol phosphates, and this increase was undiminished in the presence of cytochalasin D. Therefore, the blockade of agonist responses by this drug does not result from decreased phospholipase C. Injection of inositol 1,4,5-trisphosphate (IP3) released calcium to the same extent in control and cytochalasin D-treated cells. Confocal microscopic studies revealed a significant rearrangement of the endoplasmic reticulum after cytochalasin D treatment. Thus, disruption of the cytoskeleton blocks agonist-elicited [Ca2+]i mobilization, but this effect does not result from a lower calcium storage capacity, impaired function of the IP3 receptor, or diminished phospholipase C activity. We suggest that cytoskeletal disruption alters the spatial relationship between phospholipase C and IP3 receptors, impairing phospholipase C-dependent calcium signaling. Capacitative calcium entry was not altered under these conditions, indicating that the coupling between depletion of intracellular calcium stores and calcium entry does not depend on a precise structural relationship between intracellular stores and plasma membrane calcium channels.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
26555-61
pubmed:dateRevised
2007-7-18
pubmed:meshHeading
pubmed-meshheading:9334235-3T3 Cells, pubmed-meshheading:9334235-Adenosine Triphosphate, pubmed-meshheading:9334235-Animals, pubmed-meshheading:9334235-Calcium, pubmed-meshheading:9334235-Calcium Channels, pubmed-meshheading:9334235-Cell Membrane, pubmed-meshheading:9334235-Cytochalasin D, pubmed-meshheading:9334235-Cytoskeleton, pubmed-meshheading:9334235-Inositol 1,4,5-Trisphosphate, pubmed-meshheading:9334235-Inositol 1,4,5-Trisphosphate Receptors, pubmed-meshheading:9334235-Ion Transport, pubmed-meshheading:9334235-Mice, pubmed-meshheading:9334235-Microscopy, Confocal, pubmed-meshheading:9334235-Microscopy, Fluorescence, pubmed-meshheading:9334235-Nocodazole, pubmed-meshheading:9334235-Platelet-Derived Growth Factor, pubmed-meshheading:9334235-Receptors, Cytoplasmic and Nuclear, pubmed-meshheading:9334235-Signal Transduction, pubmed-meshheading:9334235-Thapsigargin
pubmed:year
1997
pubmed:articleTitle
Role of the cytoskeleton in calcium signaling in NIH 3T3 cells. An intact cytoskeleton is required for agonist-induced [Ca2+]i signaling, but not for capacitative calcium entry.
pubmed:affiliation
Laboratory of Signal Transduction, NIEHS, National Institutes of Health, Research Triangle Park, North Carolina 27709, USA.
pubmed:publicationType
Journal Article