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      Remodeling of calcium signaling in tumor progression

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          Abstract

          Intracellular Ca 2+ is one of the crucial signalings that modulate various cellular functions. The dysregulation of Ca 2+ homeostasis has been suggested as an important event in driving the expression of the malignant phenotypes, such as proliferation, migration, invasion, and metastasis. Cell migration is an early prerequisite for tumor metastasis that has a significant impact on patient prognosis. During cell migration, the exquisite spatial and temporal organization of intracellular Ca 2+ provides a rapid and robust way for the selective activation of signaling components that play a central role in cytoskeletal reorganization, traction force generation, and focal adhesion dynamics. A number of known molecular components involved in Ca 2+ influx pathways, including stromal interaction molecule (STIM)/Orai-mediated store-operated Ca 2+ entry (SOCE) and the Ca 2+-permeable transient receptor potential (TRP) channels, have been implicated in cancer cell migration and tumor metastasis. The clinical significance of these molecules, such as STIM proteins and the TRPM7 channel, in tumor progression and their diagnostic and prognostic potentials have also been demonstrated in specific cancer types. In this review, we summarize the recent advances in understanding the important roles and regulatory mechanisms of these Ca 2+ influx pathways on malignant behaviors of tumor cells. The clinical implications in facilitating current diagnostic and therapeutic procedures are also discussed.

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          Most cited references69

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          Non-muscle myosin II takes centre stage in cell adhesion and migration.

          Non-muscle myosin II (NM II) is an actin-binding protein that has actin cross-linking and contractile properties and is regulated by the phosphorylation of its light and heavy chains. The three mammalian NM II isoforms have both overlapping and unique properties. Owing to its position downstream of convergent signalling pathways, NM II is central in the control of cell adhesion, cell migration and tissue architecture. Recent insight into the role of NM II in these processes has been gained from loss-of-function and mutant approaches, methods that quantitatively measure actin and adhesion dynamics and the discovery of NM II mutations that cause monogenic diseases.
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            Mitochondria as sensors and regulators of calcium signalling.

            During the past two decades calcium (Ca(2+)) accumulation in energized mitochondria has emerged as a biological process of utmost physiological relevance. Mitochondrial Ca(2+) uptake was shown to control intracellular Ca(2+) signalling, cell metabolism, cell survival and other cell-type specific functions by buffering cytosolic Ca(2+) levels and regulating mitochondrial effectors. Recently, the identity of mitochondrial Ca(2+) transporters has been revealed, opening new perspectives for investigation and molecular intervention.
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              A mutation in Orai1 causes immune deficiency by abrogating CRAC channel function.

              Antigen stimulation of immune cells triggers Ca2+ entry through Ca2+ release-activated Ca2+ (CRAC) channels, promoting the immune response to pathogens by activating the transcription factor NFAT. We have previously shown that cells from patients with one form of hereditary severe combined immune deficiency (SCID) syndrome are defective in store-operated Ca2+ entry and CRAC channel function. Here we identify the genetic defect in these patients, using a combination of two unbiased genome-wide approaches: a modified linkage analysis with single-nucleotide polymorphism arrays, and a Drosophila RNA interference screen designed to identify regulators of store-operated Ca2+ entry and NFAT nuclear import. Both approaches converged on a novel protein that we call Orai1, which contains four putative transmembrane segments. The SCID patients are homozygous for a single missense mutation in ORAI1, and expression of wild-type Orai1 in SCID T cells restores store-operated Ca2+ influx and the CRAC current (I(CRAC)). We propose that Orai1 is an essential component or regulator of the CRAC channel complex.
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                Author and article information

                Journal
                J Biomed Sci
                J. Biomed. Sci
                Journal of Biomedical Science
                BioMed Central
                1021-7770
                1423-0127
                2013
                17 April 2013
                : 20
                : 1
                : 23
                Affiliations
                [1 ]Department of Pharmacology, National Cheng Kung University, Tainan, Taiwan
                [2 ]Department of Biomedical Engineering, National Cheng Kung University, Tainan, Taiwan
                [3 ]Institute of Basic Medical Sciences, National Cheng Kung University, Tainan, Taiwan
                [4 ]Advanced Optoelectronic Technology Center, National Cheng Kung University, Tainan, Taiwan
                [5 ]Infectious Diseases and Signaling Research Center, National Cheng Kung University, Tainan, Taiwan
                [6 ]Department of Obstetrics & Gynecology, National Cheng Kung University Hospital, Tainan, 704, Taiwan
                Article
                1423-0127-20-23
                10.1186/1423-0127-20-23
                3639169
                23594099
                998a15d9-6303-462b-b5ec-2b756b6e3497
                Copyright ©2013 Chen et al.; licensee BioMed Central Ltd.

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 18 February 2013
                : 8 April 2013
                Categories
                Review

                Molecular medicine
                migration,ca2+ homeostasis,stromal interaction molecule (stim),orai,transient receptor potential (trp) channels

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