scholarly journals Fluoxetine suppresses calcium signaling in human T lymphocytes through depletion of intracellular calcium stores

Cell Calcium ◽  
2015 ◽  
Vol 58 (3) ◽  
pp. 254-263 ◽  
Author(s):  
V. Gobin ◽  
M. De Bock ◽  
B.J.G. Broeckx ◽  
M. Kiselinova ◽  
W. De Spiegelaere ◽  
...  
Keyword(s):  
T Lymphocytes ◽  
Calcium Signaling ◽  
Intracellular Calcium ◽  
Calcium Stores ◽  
Intracellular Calcium Stores ◽  
Human T Lymphocytes

scholarly journals Capacitative Calcium Entry Deficits and Elevated Luminal Calcium Content in Mutant Presenilin-1 Knockin Mice

2000 ◽  
Vol 149 (4) ◽  
pp. 793-798 ◽  
Author(s):  
Malcolm A. Leissring ◽  
Yama Akbari ◽  
Christopher M. Fanger ◽  
Michael D. Cahalan ◽  
Mark P. Mattson ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Calcium Signaling ◽  
Intracellular Calcium ◽  
Brain Aging ◽  
Calcium Entry ◽  
Calcium Stores ◽  
Capacitative Calcium Entry ◽  
Intracellular Calcium Stores ◽  
Agonist Stimulation

Dysregulation of calcium signaling has been causally implicated in brain aging and Alzheimer's disease. Mutations in the presenilin genes (PS1, PS2), the leading cause of autosomal dominant familial Alzheimer's disease (FAD), cause highly specific alterations in intracellular calcium signaling pathways that may contribute to the neurodegenerative and pathological lesions of the disease. To elucidate the cellular mechanisms underlying these disturbances, we studied calcium signaling in fibroblasts isolated from mutant PS1 knockin mice. Mutant PS1 knockin cells exhibited a marked potentiation in the amplitude of calcium transients evoked by agonist stimulation. These cells also showed significant impairments in capacitative calcium entry (CCE, also known as store-operated calcium entry), an important cellular signaling pathway wherein depletion of intracellular calcium stores triggers influx of extracellular calcium into the cytosol. Notably, deficits in CCE were evident after agonist stimulation, but not if intracellular calcium stores were completely depleted with thapsigargin. Treatment with ionomycin and thapsigargin revealed that calcium levels within the ER were significantly increased in mutant PS1 knockin cells. Collectively, our findings suggest that the overfilling of calcium stores represents the fundamental cellular defect underlying the alterations in calcium signaling conferred by presenilin mutations.

Presenilin-1 and intracellular calcium stores regulate neuronal glutamate uptake

2004 ◽  
Vol 88 (6) ◽  
pp. 1361-1372 ◽  
Author(s):  
Yaxiong Yang ◽  
Gregory A. Kinney ◽  
William J. Spain ◽  
John C. S. Breitner ◽  
David G. Cook
Keyword(s):  
Intracellular Calcium ◽  
Glutamate Uptake ◽  
Presenilin 1 ◽  
Calcium Stores ◽  
Intracellular Calcium Stores

scholarly journals Multiple Receptor Interactions Trigger Release of Membrane and Intracellular Calcium Stores Critical for Herpes Simplex Virus Entry

2007 ◽  
Vol 18 (8) ◽  
pp. 3119-3130 ◽  
Author(s):  
Natalia Cheshenko ◽  
Wen Liu ◽  
Lisa M. Satlin ◽  
Betsy C. Herold
Keyword(s):  
Herpes Simplex ◽  
Intracellular Calcium ◽  
Viral Entry ◽  
Calcium Stores ◽  
Calcium Response ◽  
Herpes Simplex Viruses ◽  
Intracellular Calcium Stores ◽  
Viral Binding ◽  
Glycoprotein H ◽  
Simplex Virus

Herpes simplex viruses (HSV) harness cellular calcium signaling pathways to facilitate viral entry. Confocal microscopy and small interfering RNA (siRNA) were used to identify the source of the calcium and to dissect the requisite viral–cell interactions. Binding of HSV to human epithelial cells induced no calcium response, but shifting the cells to temperatures permissive for penetration triggered increases in plasma membrane calcium followed by a global release of intracellular calcium. Transfection with siRNA targeting the proteoglycan syndecan-2 blocked viral binding and abrogated any calcium response. Transfection with siRNA targeting nectin-1, a glycoprotein D receptor, also prevented both membrane and intracellular calcium responses. In contrast, the membrane response was preserved after transfection with siRNA targeting integrinαv, a novel glycoprotein H receptor. The membrane response, however, was not sufficient for viral entry, which required interactions with integrinαv and release of inositol-triphosphate receptor-dependent intracellular calcium stores. Thus, calcium plays a critical, complex role in HSV entry.

scholarly journals Agonist-induced Ca2+ influx in human neutrophils is secondary to the emptying of intracellular calcium stores

1991 ◽  
Vol 277 (1) ◽  
pp. 73-79 ◽  
Author(s):  
M Montero ◽  
J Alvarez ◽  
J Garcia-Sancho
Keyword(s):  
Plasma Membrane ◽  
Intracellular Calcium ◽  
Time Course ◽  
Human Neutrophils ◽  
Calcium Stores ◽  
Free Medium ◽  
Prolonged Incubation ◽  
Intracellular Calcium Stores ◽  
Cytochrome P 450 ◽  
In Cells

Emptying of the intracellular calcium stores of human neutrophils, by prolonged incubation in Ca(2+)-free medium, by treatment with low concentrations of the Ca2+ inophore ionomycin, or by activation with cell agonists, increased the plasma-membrane permeability to Ca2+ and Mn2+. The chemotactic peptide formylmethionyl-leucyl-phenylalanine and the natural agonists platelet-activating factor and leukotriene B4 released different amounts of calcium from the stores and induced Ca2+ (Mn2+) uptake, the rate of which correlated inversely with the amount of calcium left in the stores. The increased Mn2+ uptake induced by these agonists was persistent in cells incubated in Ca(2+)-free medium, but returned to basal levels in cells incubated in Ca(2+)-containing medium, with the same time course as the refilling of the calcium stores. The calcium-stores-regulated Mn2+ influx, including that induced by agonists, was prevented by cytochrome P-450 inhibitors. We propose that agonist-induced Ca2+ (Mn2+) influx in human neutrophils is secondary to the emptying of the intracellular stores which, in turn, activates plasma-membrane Ca2+ channels by a mechanism involving microsomal cytochrome P-450, similar to that described previously in thymocytes [Alvarez, Montero & Garcia-Sancho (1991) Biochem. J. 274, 193-197].

Sign in / Sign up

Export Citation Format

Share Document