scholarly journals Activation of intracellular calcium signaling in osteoblasts colocalizes with the formation of post-yield diffuse microdamage in bone matrix

2016 ◽  
Vol 5 ◽  
Author(s):  
Hyungjin Jung ◽  
Ozan Akkus
Keyword(s):  
Calcium Signaling ◽  
Intracellular Calcium ◽  
Bone Matrix ◽  
Intracellular Calcium Signaling

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.

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