Capacitative calcium entry is inhibited in vascular endothelial cells by disruption of cytoskeletal microfilaments

Holda, Jaclyn R.; Blatter, Lothar A.

doi:10.1016/s0014-5793(97)00051-3

Cited by 127 publications

(108 citation statements)

References 38 publications

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“…Our results demonstrate clearly that cytochalasin D decreases Ca# + entry after store depletion in human platelets. This is in agreement with recent reports describing the effect of actin cytoskeleton disruption in vascular endothelial cells [60]. However, Pedrosa-Ribeiro et al [61] have reported essentially the opposite results in NIH 3T3 cells.…”

Section: Discussionsupporting

confidence: 93%

“…These observations are in agreement with previous results [47] and confirm that if ' treadmilling ' (the net polymerization at one end of the filament and depolymerization at the other) occurs in resting platelets it must occur very slowly. Inhibition of actin polymerization by cytochalasin D was observed to be dependent on the duration of incubation of the cells with the agent, in agreement with previous studies [48,60]. A similar effect was observed for the inhibition in Ca# + entry, which is in agreement with Holda and Blatter [60].…”

Section: Discussionsupporting

confidence: 91%

“…Inhibition of actin polymerization by cytochalasin D was observed to be dependent on the duration of incubation of the cells with the agent, in agreement with previous studies [48,60]. A similar effect was observed for the inhibition in Ca# + entry, which is in agreement with Holda and Blatter [60]. However, complete inhibition of actin polymerization by cytochalasin D after 40 min of preincubation decreased Ca# + entry by only 50%.…”

Section: Discussionsupporting

confidence: 91%

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Farnesylcysteine analogues inhibit store-regulated Ca2+ entry in human platelets: evidence for involvement of small GTP-binding proteins and actin cytoskeleton

Rosado

Sage

2000

Biochemical Journal

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We have investigated the mechanism of Ca# + entry into fura-2-loaded human platelets by preventing the prenylation of proteins such as small GTP-binding proteins. The farnesylcysteine analogues farnesylthioacetic acid (FTA) and N-acetyl-S-geranylgeranyl--cysteine (AGGC), which are inhibitors of the methylation of prenylated and geranylgeranylated proteins respectively, significantly decreased thrombin-evoked increases in intracellular free Ca# + concentration ([Ca# + ] i ) in the presence, but not in the absence, of external Ca# + , suggesting a relatively selective inhibition of Ca# + entry over internal release. Both these compounds and N-acetyl-S-farnesyl--cysteine, which had similar effects to those of FTA, also decreased Ca# + entry evoked by the depletion of intracellular Ca# + stores with thapsigargin. The inactive control N-acetyl-S-geranyl--cysteine was without effect. Patulin, an inhibitor of prenylation that is inert with respect to

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Section: Discussionsupporting

confidence: 93%

Section: Discussionsupporting

confidence: 91%

Section: Discussionsupporting

confidence: 91%

See 1 more Smart Citation

Farnesylcysteine analogues inhibit store-regulated Ca2+ entry in human platelets: evidence for involvement of small GTP-binding proteins and actin cytoskeleton

Rosado

Sage

2000

Biochemical Journal

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“…Disorganization of the cell shape induced by disrupting cytoskeleton organization was previously found to differentially affect calcium transients and CCE in different cell types (17,18). In this study, we provide evidence that active and rapid rearrangement of astrocyte morphology induced by activation of the protein kinase A (PKA), is responsible for enhancement of InsP 3 -induced cytosolic calcium concentration ([Ca 2ϩ ] i ) elevation via an enhanced CCE.…”

mentioning

confidence: 61%

cAMP-induced Cytoskeleton Rearrangement Increases Calcium Transients through the Enhancement of Capacitative Calcium Entry

Grimaldi

Favit²,

Alkon

1999

Journal of Biological Chemistry

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In this report we investigated the correlation between cell morphology and regulation of cytosolic calcium homeostasis. Type I astrocytes were differentiated to stellate process-bearing cells by a 100-min exposure to cAMP. Differentiation of cortical astrocytes increased the magnitude and duration of calcium transients elicited by phospholipase C-activating agents as measured by single cell Fura-2-based imaging. Calcium imaging showed differences in the spatial pattern of the response. In both differentiated and the control cells, the response originated in the periphery and gradually extended into the center of the cell. However, the elevation of cytosolic calcium concentration ([Ca 2؉ ] i ) was particularly evident within the processes and adjacent to the inner cell membrane of the differentiated astrocytes. In addition, differentiation significantly prolonged the duration of the [Ca 2؉ ] i elevation. Potentiation of the calcium transients was mimicked by forskolin-induced differentiation and abolished by a specific protein kinase-A blocker. Conversely, the enhancement of the calcium transients was not mimicked by brief exposure to cAMP not causing morphological differentiation, and in PC12 cells that did not undergo morphological changes after 100 min of cAMP treatment. Impairing cAMP-induced cytoskeleton re-organization, by means of cytochalasin D and nocodazole, prevented the potentiation of the calcium transients in cAMPtreated astrocytes. Phospholipase C activity and sensitivity to inositol (1,4,5)-trisphosphate were not involved in the enhancement of the calcium responses. Also, potentiation of the calcium transients was dependent on extracellular calcium. Calcium storage and thapsigargin-depletable intracellular calcium reservoirs were analogously not increased in differentiated astrocytes. Rearrangement of the cell shape also caused a condensation of the endoplasmic reticulum and altered the spatial relationship between the endoplasmic reticulum and the cell membrane. In conclusion, morphological rearrangements of type I astrocytes increase the magnitude and the duration of agonist-induced calcium transients via enhancement of capacitative calcium entry and is associated with a spatial reorganization of the relationship between cell membrane and the endoplasmic reticulum structures.

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“…Before, SOCE had been identified in T-lymphocytes (Zweifach and Lewis 1995) and endothelial tissue (Holder and Blatter 1997). In their original study, Kurebayashi and Ogawa used intact thin mouse EDL fiber bundles that they subjected to short (30 s) high K + pulses in Ca 2+ -free solution and recorded force transients and fura-2 Mn 2+ influx.…”

Section: Store-operated Ca 2+ Entry (Soce) In Skeletal Musclementioning

confidence: 99%

New factors contributing to dynamic calcium regulation in the skeletal muscle triad—a crowded place

2009

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Skeletal muscle is a highly organized tissue that has to be optimized for fast signalling events conveying electrical excitation to contractile response. The site of electro-chemico-mechanical coupling is the skeletal muscle triad where two membrane systems, the extracellular ttubules and the intracellular sarcoplasmic reticulum, come into very close contact. Structure fits function here and the signalling proteins DHPR and RyR1 were the first to be discovered to bridge this gap in a conformational coupling arrangement. Since then, however, new proteins and more signalling cascades have been identified just in the last decade, adding more diversity and fine tuning to the regulation of excitation-contraction coupling (ECC) and control over Ca 2+ store content. The concept of Ca 2+ entry into working skeletal muscle has become attractive again with the experimental evidence summarized in this review. Store-operated Ca 2+ entry (SOCE), excitation-coupled Ca 2+ entry (ECCE), action-potential-activated Ca 2+ current (APACC), and retrograde EC-coupling (ECC) are new concepts additional to the conventional orthograde ECC; they have provided fascinating new insights into muscle physiology. In this review, we discuss the discovery of these pathways, their potential roles, and the signalling proteins involved that show that the triad may become a crowded place in time.

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Capacitative calcium entry is inhibited in vascular endothelial cells by disruption of cytoskeletal microfilaments

Cited by 127 publications

References 38 publications

Farnesylcysteine analogues inhibit store-regulated Ca2+ entry in human platelets: evidence for involvement of small GTP-binding proteins and actin cytoskeleton

Farnesylcysteine analogues inhibit store-regulated Ca2+ entry in human platelets: evidence for involvement of small GTP-binding proteins and actin cytoskeleton

cAMP-induced Cytoskeleton Rearrangement Increases Calcium Transients through the Enhancement of Capacitative Calcium Entry

New factors contributing to dynamic calcium regulation in the skeletal muscle triad—a crowded place

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