Measuring systematic changes in invasive cancer cell shape using Zernike moments

2016 ◽  
Vol 8 (11) ◽  
pp. 1183-1193 ◽  
Author(s):  
Elaheh Alizadeh ◽  
Samanthe Merrick Lyons ◽  
Jordan Marie Castle ◽  
Ashok Prasad
Keyword(s):  
Cancer Cells ◽  
Cancer Cell ◽  
Cell Shape ◽  
Zernike Moments ◽  
Invasive Cancer ◽  
Two Dimensional ◽  
Dimensional Cell ◽  
Invasive Cancer Cell

Cancer cells show similar changes in two dimensional cell shape analyzed using Zernike moments.

scholarly journals Mammalian SIRT6 Represses Invasive Cancer Cell Phenotypes through ATP Citrate Lyase (ACLY)-Dependent Histone Acetylation

Genes ◽  
2021 ◽  
Vol 12 (9) ◽  
pp. 1460
Author(s):  
Wei Zheng ◽  
Luisa Tasselli ◽  
Tie-mei Li ◽  
Katrin F. Chua
Keyword(s):  
Gene Expression ◽  
Histone Acetylation ◽  
Cancer Cells ◽  
Cancer Cell ◽  
Invasive Cancer ◽  
Atp Citrate Lyase ◽  
Acetyl Coa ◽  
Citrate Lyase ◽  
Cell Phenotypes ◽  
Invasive Cancer Cell

The modulation of dynamic histone acetylation states is key for organizing chromatin structure and modulating gene expression and is regulated by histone acetyltransferase (HAT) and histone deacetylase (HDAC) enzymes. The mammalian SIRT6 protein, a member of the Class III HDAC Sirtuin family of NAD+-dependent enzymes, plays pivotal roles in aging, metabolism, and cancer biology. Through its site-specific histone deacetylation activity, SIRT6 promotes chromatin silencing and transcriptional regulation of aging-associated, metabolic, and tumor suppressive gene expression programs. ATP citrate lyase (ACLY) is a nucleo-cytoplasmic enzyme that produces acetyl coenzyme A (acetyl-CoA), which is the required acetyl donor for lysine acetylation by HATs. In addition to playing a central role in generating cytosolic acetyl-CoA for de novo lipogenesis, a growing body of work indicates that ACLY also functions in the nucleus where it contributes to the nutrient-sensitive regulation of nuclear acetyl-CoA availability for histone acetylation in cancer cells. In this study, we have identified a novel function of SIRT6 in controlling nuclear levels of ACLY and ACLY-dependent tumor suppressive gene regulation. The inactivation of SIRT6 in cancer cells leads to the accumulation of nuclear ACLY protein and increases nuclear acetyl-CoA pools, which in turn drive locus-specific histone acetylation and the expression of cancer cell adhesion and migration genes that promote tumor invasiveness. Our findings uncover a novel mechanism of SIRT6 in suppressing invasive cancer cell phenotypes and identify acetyl-CoA responsive cell migration and adhesion genes as downstream targets of SIRT6.

Harmless glucose‐modified ruthenium complexes suppressing cell migration of highly invasive cancer cell lines

2019 ◽  
Vol 34 (1) ◽  
Author(s):  
Martin Lamač ◽  
Michal Horáček ◽  
Lucie Červenková Šťastná ◽  
Jindřich Karban ◽  
Lucia Sommerová ◽  
...  
Keyword(s):  
Cell Migration ◽  
Cell Lines ◽  
Cancer Cell ◽  
Ruthenium Complexes ◽  
Cancer Cell Lines ◽  
Invasive Cancer ◽  
Invasive Cancer Cell

EGF enhances low-invasive cancer cell invasion by promoting IMP-3 expression

Tumor Biology ◽  
2015 ◽  
Vol 37 (2) ◽  
pp. 2555-2563 ◽  
Author(s):  
Xianglan Zhang ◽  
Im-hee Jung ◽  
Young Sun Hwang
Keyword(s):  
Cancer Cell ◽  
Cell Invasion ◽  
Invasive Cancer ◽  
Cancer Cell Invasion ◽  
Invasive Cancer Cell

scholarly journals Dynamic Control of Mitochondrial Ca2+ Levels as a Survival Strategy of Cancer Cells

2021 ◽  
Vol 9 ◽  
Author(s):  
Corina T. Madreiter-Sokolowski ◽  
Benjamin Gottschalk ◽  
Armin A. Sokolowski ◽  
Roland Malli ◽  
Wolfgang F. Graier
Keyword(s):  
Cell Death ◽  
Cancer Cells ◽  
Cancer Cell ◽  
Uncoupling Protein ◽  
Expression Patterns ◽  
Prostate Adenocarcinoma ◽  
Invasive Cancer ◽  
Fine Tuning ◽  
Human Breast ◽  
Interaction Sites

Cancer cells have increased energy requirements due to their enhanced proliferation activity. This energy demand is, among others, met by mitochondrial ATP production. Since the second messenger Ca2+ maintains the activity of Krebs cycle dehydrogenases that fuel mitochondrial respiration, proper mitochondrial Ca2+ uptake is crucial for a cancer cell survival. However, a mitochondrial Ca2+ overload induces mitochondrial dysfunction and, ultimately, apoptotic cell death. Because of the vital importance of balancing mitochondrial Ca2+ levels, a highly sophisticated machinery of multiple proteins manages mitochondrial Ca2+ homeostasis. Notably, mitochondria sequester Ca2+ preferentially at the interaction sites between mitochondria and the endoplasmic reticulum (ER), the largest internal Ca2+ store, thus, pointing to mitochondrial-associated membranes (MAMs) as crucial hubs between cancer prosperity and cell death. To investigate potential regulatory mechanisms of the mitochondrial Ca2+ uptake routes in cancer cells, we modulated mitochondria–ER tethering and the expression of UCP2 and analyzed mitochondrial Ca2+ homeostasis under the various conditions. Hence, the expression of contributors to mitochondrial Ca2+ regulation machinery was quantified by qRT-PCR. We further used data from The Cancer Genome Atlas (TCGA) to correlate these in vitro findings with expression patterns in human breast invasive cancer and human prostate adenocarcinoma. ER-mitochondrial linkage was found to support a mitochondrial Ca2+ uptake route dependent on uncoupling protein 2 (UCP2) in cancer cells. Notably, combined overexpression of Rab32, a protein kinase A-anchoring protein fostering the ER-mitochondrial tethering, and UCP2 caused a significant drop in cancer cells' viability. Artificially enhanced ER-mitochondrial tethering further initiated a sudden decline in the expression of UCP2, probably as an adaptive response to avoid mitochondrial Ca2+ overload. Besides, TCGA analysis revealed an inverse expression correlation between proteins stabilizing mitochondrial-ER linkage and UCP2 in tissues of human breast invasive cancer and prostate adenocarcinoma. Based on these results, we assume that cancer cells successfully manage mitochondrial Ca2+ uptake to stimulate Ca2+-dependent mitochondrial metabolism while avoiding Ca2+-triggered cell death by fine-tuning ER-mitochondrial tethering and the expression of UCP2 in an inversed manner. Disruption of this equilibrium yields cancer cell death and may serve as a treatment strategy to specifically kill cancer cells.

scholarly journals ECM cross-linking regulates invadopodia dynamics

2017 ◽  
Author(s):  
Kamyar Esmaeili ◽  
Aviv Bergman ◽  
Bojana Gligorijevic
Keyword(s):  
Cancer Cells ◽  
Cancer Cell ◽  
Time Lapse ◽  
Invasive Cancer ◽  
Cross Linking ◽  
Β1 Integrin ◽  
Cell Behaviors ◽  
Lysine Residues ◽  
Ecm Degradation ◽  
And Function

AbstractInvadopodiInvadopodia are membrane protrusions dynamically assembled by invasive cancer cells in contact with extracellular matrix (ECM). Invadopodia are enriched for the structural proteins actin and cortactin, as well as metalloproteases such as MT1-MMP, whose function is to degrade the surrounding ECM. During metastasis, invadopodia are necessary for cancer cell intravasation and extravasation. While signaling pathways involved in the assembly and function of invadopodia are well studied, few studies address invadopodia dynamics and how the cell-ECM interactions contribute to cell invasion. Using iterative analysis based on time-lapse microscopy and mathematical modeling of invasive cancer cells, we found that cells oscillate between invadopodia presence and cell stasis, termed Invadopodia state and invadopodia absence during cell translocation, termed Migration state. Our data suggests that β1-integrin-ECM binding and ECM cross-linking control the duration of each of the two states. By changing the concentration of cross-linkers in 2D and 3D cultures, we generate ECM where 0-0.92 of total lysine residues are cross-linked. Using ECM with a range of cross-linking degrees we demonstrate that the dynamics of invadopodia-related functions have a biphasic relationship to ECM cross-linking. At intermediate levels of ECM cross-linking (0.39), cells exhibit rapid invadopodia protrusion-retraction cycles and rapid calcium spikes, which lead to more frequent MT1-MMP delivery, causing maximal invadopodia-mediated ECM degradation. In contrast, both extremely high or low levels of cross-linking lead to slower invadopodia-related dynamics and lower ECM degradation. Additionally, β1-integrin inhibition modifies dynamics of invadopodia-related functions, as well as the length of time cells spend in either of the states. Collectively, these data suggest that β1-integrin-ECM binding non-linearly translates small physical differences in extracellular environment to differences in the dynamics of cancer cell behaviors. Understanding conditions under which invadopodia can be reduced by subtle environment-targeting treatments may lead to combination therapies for preventing metastatic spread.

N-hexane Extract and Fraction of Green Tea as Antiproliferation of MCM-B2 Breast Cancer Cells In Vitro

2020 ◽  
Vol 6 (2) ◽  
Author(s):  
Lisni Noraida Waruwu ◽  
Maria Bintang ◽  
Bambang Pontjo Priosoeryanto
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Green Tea ◽  
Cancer Cell ◽  
Breast Cancer Cells ◽  
Green Tea Extract ◽  
Hexane Fraction ◽  
Phytochemical Screening ◽  
Tea Extract

Green tea (Camellia sinensis) is one of traditional plants that have the potential as an anticancer. The sample used in this research commercial green tea extract. The purpose of this study was to test the antiproliferation activity of green tea extract on breast cancer cell MCM-B2 in vitro. Green tea extract fractionated using three solvents, ie water, ethanol 70%, and n-hexane. Extract and fraction of green tea water have value Lethality Concentration 50 (LC50) more than 1000 ppm. The fraction of ethanol 70% and n-hexane had an LC50 value of 883.48 ppm and 600.56 ppm, respectively. The results of the phytochemical screening of green tea extract are flavonoids, tannins, and saponins, while the phytochemical screening results of n-hexane fraction are flavonoids and tannins. Antiproliferation activity was tested on breast cancer cells MCM-B2 and normal cells Vero by trypan blue staining method. The highest MCM-B2 cell inhibitory activity was achieved at a concentration of 13000 ppm green tea extract and 1000 ppm of n-hexane fraction, 59% and 59%, respectively. The extract and n-hexane fraction of green tea are not toxic to normal Vero cells characterized by not inhibiting normal cell proliferation. Keywords: antiproliferative, cancer cell MCM-B2, commercial green tea, cytotoxicity

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