System-Size Biresonance for Intracellular Calcium Signaling

ChemPhysChem ◽  
2004 ◽  
Vol 5 (7) ◽  
pp. 1041-1045 ◽  
Author(s):  
Jiqian Zhang ◽  
Zhonghuai Hou ◽  
Houwen Xin
Keyword(s):  
Calcium Signaling ◽  
Intracellular Calcium ◽  
System Size ◽  
Intracellular Calcium Signaling

THE ROLE OF INTERNAL NOISE FOR OPTIMAL INTRACELLULAR CALCIUM SIGNALING IN COUPLED BIOLOGICAL CELL SYSTEM

2011 ◽  
Vol 10 (01) ◽  
pp. 31-39 ◽  
Author(s):  
HONGYING LI ◽  
JIANHONG BI
Keyword(s):  
Calcium Signaling ◽  
Intracellular Calcium ◽  
Cell Size ◽  
Internal Noise ◽  
System Size ◽  
Cell System ◽  
Calcium Oscillations ◽  
Biological Cell ◽  
Intracellular Calcium Signaling

We have studied the role of internal noise for intracellular calcium signaling in coupled biological cell system. It is found that internal noise can induce calcium oscillations and the performance of such oscillations shows two peaks with the variation of the cell size-Ω for any cell chain length-N, indicating the occurrence of system size bi-resonance or internal noise stochastic bi-resonance, which may be very relevant to the canard explosion. We also find that there exists an optimal cell chain length-N for the first peak at which the collective calcium oscillations show the best performance, it is also a phenomenon of "system size resonance". It is interesting to note that one of the optimal cell sizes is present at Ω ~ 103μm3, which is close to a real living cell size in vivo.

Alterations in intracellular calcium signaling of lymphocytes after exhaustive exercise

2001 ◽  
pp. 242-248 ◽  
Author(s):  
FRANK CH. MOOREN ◽  
ANJA LECHTERMANN ◽  
ALBERT FROMME ◽  
LOTHAR THORWESTEN ◽  
KLAUS V??LKER
Keyword(s):  
Calcium Signaling ◽  
Intracellular Calcium ◽  
Exhaustive Exercise ◽  
Intracellular Calcium Signaling

scholarly journals Presenilins: A novel link between intracellular calcium signaling and lysosomal function?

2012 ◽  
Vol 198 (1) ◽  
pp. 7-10 ◽  
Author(s):  
Ilya Bezprozvanny
Keyword(s):  
Calcium Signaling ◽  
Intracellular Calcium ◽  
Transmembrane Proteins ◽  
Catalytic Subunit ◽  
Familial Alzheimer’S Disease ◽  
Lysosomal Function ◽  
Cell Biol ◽  
Intracellular Calcium Signaling ◽  
Lysosomal Acidification ◽  
In Cells

Mutations in presenilins (PS), transmembrane proteins encoding the catalytic subunit of γ-secretase, result in familial Alzheimer’s disease (FAD). Several studies have identified lysosomal defects in cells lacking PS or expressing FAD-associated PS mutations, which have been previously attributed to a function for PS in lysosomal acidification. Now, in this issue, Coen et al. (2012. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201201076) provide a series of results that challenge this idea and propose instead that presenilins play a role in calcium-mediated lysosomal fusion.

Bimatoprost and prostaglandin F2α selectively stimulate intracellular calcium signaling in different cat iris sphincter cells

2005 ◽  
Vol 80 (1) ◽  
pp. 135-145 ◽  
Author(s):  
Clayton S. Spada ◽  
Achim H.-P. Krauss ◽  
David F. Woodward ◽  
June Chen ◽  
Charles E. Protzman ◽  
...  
Keyword(s):  
Calcium Signaling ◽  
Intracellular Calcium ◽  
Prostaglandin F2α ◽  
Intracellular Calcium Signaling ◽  
Iris Sphincter

scholarly journals The roles of distinct Ca2+ signaling mediated by Piezo and inositol triphosphate receptor (IP3R) in the remodeling of E-cadherin during cell dissemination

2021 ◽  
Author(s):  
Alejandra J.H. Cabrera ◽  
Barry M Gumbiner ◽  
Young V Kwon
Keyword(s):  
Calcium Signaling ◽  
Intracellular Calcium ◽  
Cell Invasion ◽  
Adherens Junctions ◽  
Transformed Cells ◽  
Inositol Triphosphate ◽  
Intracellular Calcium Signaling ◽  
Cell Dissemination

Given the role of E-cadherin (E-cad) in holding epithelial cells together, the inverse relationship between E-cad levels and cell invasion has been perceived as a principle underlying the invasiveness of tumor cells. In contrast, our study employing the Drosophila model of cell dissemination demonstrates that E-cad is necessary for the invasiveness of RasV12-transformed cells in vivo. Drosophila E-cad/β-catenin disassembles at adherens junctions and assembles at invasive protrusions—the actin- and cortactin-rich invadopodia-like protrusions associated with breach of the extracellular matrix (ECM)—during cell dissemination. Loss of E-cad attenuates dissemination of RasV12-transformed cells by impairing their ability to compromise the ECM. Strikingly, the remodeling of E-cad/β-catenin subcellular distribution is controlled by two discrete intracellular calcium signaling pathways: Ca2+ release from endoplasmic reticulum via the inositol triphosphate receptor (IP3R) disassembles E-cad at adherens junctions while Ca2+ entry via the mechanosensitive channel Piezo assembles E-cad at invasive protrusions. Thus, our study provides molecular insights into the unconventional role of E-cad in cell invasion during cell dissemination in vivo and describes the discrete roles of intracellular calcium signaling in the remodeling of E-cad/β-catenin subcellular localization.

Sign in / Sign up

Export Citation Format

Share Document