Journal articles: 'Cancer cells – Motility'

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De la Fuente, Ildefonso M., and José I. López. "Cell Motility and Cancer." Cancers 12, no. 8 (August 5, 2020): 2177. http://dx.doi.org/10.3390/cancers12082177.

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Cell migration is an essential systemic behavior, tightly regulated, of all living cells endowed with directional motility that is involved in the major developmental stages of all complex organisms such as morphogenesis, embryogenesis, organogenesis, adult tissue remodeling, wound healing, immunological cell activities, angiogenesis, tissue repair, cell differentiation, tissue regeneration as well as in a myriad of pathological conditions. However, how cells efficiently regulate their locomotion movements is still unclear. Since migration is also a crucial issue in cancer development, the goal of this narrative is to show the connection between basic findings in cell locomotion of unicellular eukaryotic organisms and the regulatory mechanisms of cell migration necessary for tumor invasion and metastases. More specifically, the review focuses on three main issues, (i) the regulation of the locomotion system in unicellular eukaryotic organisms and human cells, (ii) how the nucleus does not significantly affect the migratory trajectories of cells in two-dimension (2D) surfaces and (iii) the conditioned behavior detected in single cells as a primitive form of learning and adaptation to different contexts during cell migration. New findings in the control of cell motility both in unicellular organisms and mammalian cells open up a new framework in the understanding of the complex processes involved in systemic cellular locomotion and adaptation of a wide spectrum of diseases with high impact in the society such as cancer.

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Mandel, Savannah. "Collective motility of cancer cells in hyperthermia." Scilight 2020, no. 5 (January 31, 2020): 051106. http://dx.doi.org/10.1063/10.0000459.

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Jo, Jung, Soo Park, Semi Park, Hee Lee, Chanyang Kim, Dawoon Jung, and Si Song. "Novel Gastric Cancer Stem Cell-Related Marker LINGO2 Is Associated with Cancer Cell Phenotype and Patient Outcome." International Journal of Molecular Sciences 20, no. 3 (January 28, 2019): 555. http://dx.doi.org/10.3390/ijms20030555.

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The expression of leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 2 (LINGO2) has been reported in Parkinson’s disease; however, its role in other diseases is unknown. Gastric cancer is the second leading cause of cancer death. Cancer stem cells (CSC) are a subpopulation of cancer cells that contribute to the initiation and invasion of cancer. We identified LINGO2 as a CSC-associated protein in gastric cancers both in vitro and in patient-derived tissues. We studied the effect of LINGO2 on cell motility, stemness, tumorigenicity, and angiogenic capacity using cells sorted based on LINGO2 expression and LINGO2-silenced cells. Tissue microarray analysis showed that LINGO2 expression was significantly elevated in advanced gastric cancers. The overall survival of patients expressing high LINGO2 was significantly shorter than that of patients with low LINGO2. Cells expressing high LINGO2 showed elevated cell motility, angiogenic capacity, and tumorigenicity, while LINGO2 silencing reversed these properties. Silencing LINGO2 reduced kinase B (AKT)/extracellular signal-regulated kinase (ERK)/ERK kinase (MEK) phosphorylation and decreased epithelial-mesenchymal transition (EMT)-associated markers—N-Cadherin and Vimentin and stemness-associated markers— POU class 5 homeobox 1 (OCT4) and Indian hedgehog (IHH), and markedly decreased the CD44+ population. These indicate the involvement of LINGO2 in gastric cancer initiation and progression by altering cell motility, stemness, and tumorigenicity, suggesting LINGO2 as a putative target for gastric cancer treatment.

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Kariya, Yoshinobu, Midori Oyama, Yukiko Kariya, and Yasuhiro Hashimoto. "Phosphorylated Osteopontin Secreted from Cancer Cells Induces Cancer Cell Motility." Biomolecules 11, no. 9 (September 7, 2021): 1323. http://dx.doi.org/10.3390/biom11091323.

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Osteopontin (OPN) plays a pivotal role in cancer cell invasion and metastasis. Although OPN has a large number of phosphorylation sites, the functional significance of OPN phosphorylation in cancer cell motility remains unclear. In this study, we attempted to investigate whether phosphorylated OPN secreted from cancer cells affect cancer cell migration. Quantitative PCR and Western blot analyses revealed that MDA-MB435S, A549, and H460 cells highly expressed OPN, whereas the OPN expression levels in H358, MIAPaca-2, and Panc-1 cells were quite low or were not detected. Compared with the cancer cell lines with a low OPN expression, the high OPN-expressing cancer cell lines displayed a higher cell migration, and the cell migration was suppressed by the anti-OPN antibody. This was confirmed by the OPN overexpression in H358 cancer cells with a low endogenous OPN. Phos-tag ELISA showed that phosphorylated OPN was abundant in the cell culture media of A549 and H460 cells, but not in those of MDA-MB435S cells. Moreover, the A549 and H460 cell culture media, as well as the MDA-MB435S cell culture media with a kinase treatment increased cancer cell motility, both of which were abrogated by phosphatase treatment or anti-OPN antibodies. These results suggest that phosphorylated OPN secreted from cancer cells regulates cancer cell motility.

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Leo, Angela, Erica Pranzini, Laura Pietrovito, Elisa Pardella, Matteo Parri, Paolo Cirri, Gennaro Bruno, et al. "Claisened Hexafluoro Inhibits Metastatic Spreading of Amoeboid Melanoma Cells." Cancers 13, no. 14 (July 15, 2021): 3551. http://dx.doi.org/10.3390/cancers13143551.

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Metastatic melanoma is characterized by poor prognosis and a low free-survival rate. Thanks to their high plasticity, melanoma cells are able to migrate exploiting different cell motility strategies, such as the rounded/amoeboid-type motility and the elongated/mesenchymal-type motility. In particular, the amoeboid motility strongly contributes to the dissemination of highly invasive melanoma cells and no treatment targeting this process is currently available for clinical application. Here, we tested Claisened Hexafluoro as a novel inhibitor of the amoeboid motility. Reported data demonstrate that Claisened Hexafluoro specifically inhibits melanoma cells moving through amoeboid motility by deregulating mitochondrial activity and activating the AMPK signaling. Moreover, Claisened Hexafluoro is able to interfere with the adhesion abilities and the stemness features of melanoma cells, thus decreasing the in vivo metastatic process. This evidence may contribute to pave the way for future possible therapeutic applications of Claisened Hexafluoro to counteract metastatic melanoma dissemination.

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Sehgal, Pravinkumar B., and Igor Tamm. "Interleukin-6 Enhances Motility of Breast Cancer Cells." Cancer Investigation 8, no. 6 (January 1990): 661–63. http://dx.doi.org/10.3109/07357909009018940.

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Thiery, JeanPaul. "Adhesion and motility of embryonic and cancer cells." Cell Differentiation and Development 27 (August 1989): 54. http://dx.doi.org/10.1016/0922-3371(89)90193-7.

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Sharma, Pooja, Van K. Lam, Christopher B. Raub, and Byung Min Chung. "Tracking Single Cells Motility on Different Substrates." Methods and Protocols 3, no. 3 (August 4, 2020): 56. http://dx.doi.org/10.3390/mps3030056.

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Motility is a key property of a cell, required for several physiological processes, including embryonic development, axon guidance, tissue regeneration, gastrulation, immune response, and cancer metastasis. Therefore, the ability to examine cell motility, especially at a single cell level, is important for understanding various biological processes. Several different assays are currently available to examine cell motility. However, studying cell motility at a single cell level can be costly and/or challenging. Here, we describe a method of tracking random cell motility on different substrates such as glass, tissue-culture polystyrene, and type I collagen hydrogels, which can be modified to generate different collagen network microstructures. In this study we tracked MDA-MB-231 breast cancer cells using The CytoSMARTTM System (Lonza Group, Basel, Switzerland) for live cell imaging and assessed the average cell migration speed using ImageJ and wrMTrck plugin. Our cost-effective and easy-to-use method allows studying cell motility at a single cell level on different substrates with varying degrees of stiffness and varied compositions. This procedure can be successfully performed in a highly accessible manner with a simple setup.

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Yilmaz, Mahmut, and Gerhard Christofori. "Mechanisms of Motility in Metastasizing Cells." Molecular Cancer Research 8, no. 5 (May 2010): 629–42. http://dx.doi.org/10.1158/1541-7786.mcr-10-0139.

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Jeoung, Nam Ho, Ae Lim Jo, and Hee Sung Park. "The effect of autocrine motility factor alone and in combination with methyl jasmonate on liver cancer cell growth." Bioscience, Biotechnology, and Biochemistry 85, no. 7 (May 14, 2021): 1711–15. http://dx.doi.org/10.1093/bbb/zbab087.

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ABSTRACT Neoplastic cells secrete autocrine motility factor (AMF) to stimulate the motility of cancer cells. In this study, AMF secreted from HT-29 colorectal cancer cells selectively suppressed liver cancer cells by downregulating pAKT and β-catenin. In addition, HT-29 AMF significantly augmented the activity of methyl jasmonate against liver cancer cells and is a promising alternative for liver cancer therapy.

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Nieman, Marvin T., Ryan S. Prudoff, Keith R. Johnson, and Margaret J. Wheelock. "N-Cadherin Promotes Motility in Human Breast Cancer Cells Regardless of Their E-Cadherin Expression." Journal of Cell Biology 147, no. 3 (November 1, 1999): 631–44. http://dx.doi.org/10.1083/jcb.147.3.631.

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E-cadherin is a transmembrane glycoprotein that mediates calcium-dependent, homotypic cell–cell adhesion and plays a role in maintaining the normal phenotype of epithelial cells. Decreased expression of E-cadherin has been correlated with increased invasiveness of breast cancer. In other systems, inappropriate expression of a nonepithelial cadherin, such as N-cadherin, by an epithelial cell has been shown to downregulate E-cadherin expression and to contribute to a scattered phenotype. In this study, we explored the possibility that expression of nonepithelial cadherins may be correlated with increased motility and invasion in breast cancer cells. We show that N-cadherin promotes motility and invasion; that decreased expression of E-cadherin does not necessarily correlate with motility or invasion; that N-cadherin expression correlates both with invasion and motility, and likely plays a direct role in promoting motility; that forced expression of E-cadherin in invasive, N-cadherin–positive cells does not reduce their motility or invasive capacity; that forced expression of N-cadherin in noninvasive, E-cadherin–positive cells produces an invasive cell, even though these cells continue to express high levels of E-cadherin; that N-cadherin–dependent motility may be mediated by FGF receptor signaling; and that cadherin-11 promotes epithelial cell motility in a manner similar to N-cadherin.

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Rieppi, Monica, Veronica Vergani, Carmen Gatto, Gerardo Zanetta, Paola Allavena, Giulia Taraboletti, and Raffaella Giavazzi. "Mesothelial cells induce the motility of human ovarian carcinoma cells." International Journal of Cancer 80, no. 2 (January 18, 1999): 303–7. http://dx.doi.org/10.1002/(sici)1097-0215(19990118)80:2<303::aid-ijc21>3.0.co;2-w.

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Coene, Elisabeth D., Catarina Gadelha, Nicholas White, Ashraf Malhas, Benjamin Thomas, Michael Shaw, and David J. Vaux. "A novel role for BRCA1 in regulating breast cancer cell spreading and motility." Journal of Cell Biology 192, no. 3 (January 31, 2011): 497–512. http://dx.doi.org/10.1083/jcb.201004136.

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BRCA1 C-terminal (BRCT) domains in BRCA1 are essential for tumor suppressor function, though the underlying mechanisms remain unclear. We identified ezrin, radixin, and moesin as BRCA1 BRCT domain–interacting proteins. Ezrin–radixin–moesin (ERM) and F-actin colocalized with BRCA1 at the plasma membrane (PM) of cancer cells, especially at leading edges and focal adhesion sites. In stably expressing cancer cells, high levels of enhanced green fluorescent protein (EGFP)-BRCA11634–1863 acted as a dominant-negative factor, displacing endogenous BRCA1 from the PM. This led to delayed cell spreading, increased spontaneous motility, and irregular monolayer wound healing. MCF-7 cells (intact BRCA1) showed lower motility than HCC1937 cells (truncated BRCA1), but expression of EGFP-BRCA11634–1863 in MCF-7 increased motility. Conversely, full-length BRCA1 expression in HCC1937 decreased motility but only if the protein retained ubiquitin ligase activity. We conclude that full-length BRCA1 is important for complete tumor suppressor activity via interaction of its BRCT domains with ERM at the PM, controlling spreading and motility of cancer cells via ubiquitin ligase activity.

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Al Hassan, Marwa, Isabelle Fakhoury, Zeinab El Masri, Noura Ghazale, Rayane Dennaoui, Oula El Atat, Amjad Kanaan, and Mirvat El-Sibai. "Metformin Treatment Inhibits Motility and Invasion of Glioblastoma Cancer Cells." Analytical Cellular Pathology 2018 (June 26, 2018): 1–9. http://dx.doi.org/10.1155/2018/5917470.

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Glioblastoma multiforme (GBM) is one of the most common and deadliest cancers of the central nervous system (CNS). GBMs high ability to infiltrate healthy brain tissues makes it difficult to remove surgically and account for its fatal outcomes. To improve the chances of survival, it is critical to screen for GBM-targeted anticancer agents with anti-invasive and antimigratory potential. Metformin, a commonly used drug for the treatment of diabetes, has recently emerged as a promising anticancer molecule. This prompted us, to investigate the anticancer potential of metformin against GBMs, specifically its effects on cell motility and invasion. The results show a significant decrease in the survival of SF268 cancer cells in response to treatment with metformin. Furthermore, metformin’s efficiency in inhibiting 2D cell motility and cell invasion in addition to increasing cellular adhesion was also demonstrated in SF268 and U87 cells. Finally, AKT inactivation by downregulation of the phosphorylation level upon metformin treatment was also evidenced. In conclusion, this study provides insights into the anti-invasive antimetastatic potential of metformin as well as its underlying mechanism of action.

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Sedwick, Caitlin. "Carole Parent: Migrating cells relay the message." Journal of Cell Biology 205, no. 3 (May 12, 2014): 286–87. http://dx.doi.org/10.1083/jcb.2053pi.

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Hiramoto-Yamaki, Nao, Shingo Takeuchi, Shuhei Ueda, Kohei Harada, Satoshi Fujimoto, Manabu Negishi, and Hironori Katoh. "Ephexin4 and EphA2 mediate cell migration through a RhoG-dependent mechanism." Journal of Cell Biology 190, no. 3 (August 2, 2010): 461–77. http://dx.doi.org/10.1083/jcb.201005141.

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EphA2, a member of the Eph receptor family, is frequently overexpressed in a variety of human cancers, including breast cancers, and promotes cancer cell motility and invasion independently of its ligand ephrin stimulation. In this study, we identify Ephexin4 as a guanine nucleotide exchange factor (GEF) for RhoG that interacts with EphA2 in breast cancer cells, and knockdown and rescue experiments show that Ephexin4 acts downstream of EphA2 to promote ligand-independent breast cancer cell migration and invasion toward epidermal growth factor through activation of RhoG. The activation of RhoG recruits its effector ELMO2 and a Rac GEF Dock4 to form a complex with EphA2 at the tips of cortactin-rich protrusions in migrating breast cancer cells. In addition, the Dock4-mediated Rac activation is required for breast cancer cell migration. Our findings reveal a novel link between EphA2 and Rac activation that contributes to the cell motility and invasiveness of breast cancer cells.

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TOMIZAWA, MINORU, FUMINOBU SHINOZAKI, YASUFUMI MOTOYOSHI, TAKAO SUGIYAMA, SHIGENORI YAMAMOTO, and NAOKI ISHIGE. "SU11274 suppresses proliferation and motility of pancreatic cancer cells." Oncology Letters 10, no. 3 (July 2, 2015): 1468–72. http://dx.doi.org/10.3892/ol.2015.3452.

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Iwasaki, Masahiro, Sachiko Homma, Akinori Hishiya, Samuel J. Dolezal, John C. Reed, and Shinichi Takayama. "BAG3 Regulates Motility and Adhesion of Epithelial Cancer Cells." Cancer Research 67, no. 21 (November 1, 2007): 10252–59. http://dx.doi.org/10.1158/0008-5472.can-07-0618.

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Chow, Jimmy Y. C., Makiko Ban, Helen L. Wu, Flang Nguyen, Mei Huang, Heekyung Chung, Hui Dong, and John M. Carethers. "TGF-β downregulates PTEN via activation of NF-κB in pancreatic cancer cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 298, no. 2 (February 2010): G275—G282. http://dx.doi.org/10.1152/ajpgi.00344.2009.

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TGF-β utilizes receptor-activated SMAD signaling to mediate growth suppression; however, non-SMAD signaling that modulates the TGF-β response in epithelial cells become apparent when the SMAD signaling is abrogated, a common occurrence in pancreatic cancers. Here, we examined whether TGF-β utilized NF-κB to downregulate PTEN, a gene that is rarely mutated in pancreatic cancers. SMAD4-null BxPc3 and CAPAN-1 pancreatic cancer cells were treated with TGF-β (10 ng/ml) and lysed, and cellular proteins were analyzed by Western blots using p-IκB, p65, and PTEN antibodies. PTEN promoter and NF-κB activities were assessed by PTEN-luc and p-NF-luc constructs, respectively. Dominant negative p-IκB-α-M (NF-κB superrepressor) was used to block activation of NF-κB. Cell motility was assessed by Boyden chamber migration assay. TGF-β induced IκB-α phosphorylation followed by NF-κB p65 subunit nuclear translocation and increased NF-κB activity. IκB-α-M blocked TGF-β-induced NF-κB activity, reversed downregulated PTEN promoter activity and PTEN expression, and prevented augmentation of cell motility induced by TGF-β. SMAD4 restoration, but not knockdown of SMAD2 and/or 3, reversed TGF-β-induced NF-κB activity. Thus TGF-β suppresses PTEN in pancreatic cancer cells through NF-κB activation and enhances cell motility and invasiveness in a SMAD4-independent manner that can be counteracted when TGF-β-SMAD signaling is restored. The TGF-β/NF-κB/PTEN cascade may be a critical pathway for pancreatic cancer cells to proliferate and metastasize.

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Rudolf, Emil, Lada Klvačová, Stanislav John, and Miroslav Červinka. "Zinc Alters Cytoskeletal Integrity and Migration in Colon Cancer Cells." Acta Medica (Hradec Kralove, Czech Republic) 51, no. 1 (2008): 51–57. http://dx.doi.org/10.14712/18059694.2017.8.

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Zinc has been shown to have inhibitory effects on proliferation and metabolism of malignant colonocytes. Still, there is no information available concerning putative effects of zinc against motility and migration of colon cancer cells. Using fluorescence microscopy, immunoblotting and microflorimetry we show that treatment with zinc sulfate affected motility, invasiveness, cytoskeletal integrity and expression of selected markers (E-cadherin, catenin, vimentin, tubulin and actin) of invasive SW480 colon tumor cells. These results emphasize the possible multitudinous role of zinc in the process of colon cancer development and hint at the potential of this element in chemoprevention of advanced colorectal carcinoma.

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Varani, James, Suzanne E. G. Fligeil, and Patricia Perone. "Directional motility in strongly malignant murine tumor cells." International Journal of Cancer 35, no. 4 (April 15, 1985): 559–64. http://dx.doi.org/10.1002/ijc.2910350422.

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Patel, Megha, Marek Feith, Birgit Janicke, Kersti Alm, and Zahra El-Schich. "Evaluation of the Impact of Imprinted Polymer Particles on Morphology and Motility of Breast Cancer Cells by Using Digital Holographic Cytometry." Applied Sciences 10, no. 3 (January 21, 2020): 750. http://dx.doi.org/10.3390/app10030750.

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Breast cancer is the second most common cancer type worldwide and breast cancer metastasis accounts for the majority of breast cancer-related deaths. Tumour cells produce increased levels of sialic acid (SA) that terminates the monosaccharide on glycan chains of the glycosylated proteins. SA can contribute to cellular recognition, cancer invasiveness and increase the metastatic potential of cancer cells. SA-templated molecularly imprinted polymers (MIPs) have been proposed as promising reporters for specific targeting of cancer cells when deployed in nanoparticle format. The sialic acid-molecularly imprinted polymers (SA-MIPs), which use SA for the generation of binding sites through which the nanoparticles can target and stain breast cancer cells, opens new strategies for efficient diagnostic tools. This study aims at monitoring the effects of SA-MIPs on morphology and motility of the epithelial type MCF-7 and the highly metastatic MDAMB231 breast cancer cell lines, using digital holographic cytometry (DHC). DHC is a label-free technique that is used in cell morphology studies of e.g., cell volume, area and thickness as well as in motility studies. Here, we show that MCF-7 cells move slower than MDAMB231 cells. We also show that SA-MIPs have an effect on cell morphology, motility and viability of both cell lines. In conclusion, by using DH microscopy, we could detect SA-MIPs impact on different breast cancer cells regarding morphology and motility.

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Hsu, Stephen, Fei Huang, Liliana Ossowski, and Eileen Friedman. "Colon carcinoma cells with inactive nm23 show increased motility and response to motility factors." Carcinogenesis 16, no. 9 (1995): 2259–62. http://dx.doi.org/10.1093/carcin/16.9.2259.

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Grubisha, Melanie J., M. E. Cifuentes, Stephen R. Hammes, and Donald B. DeFranco. "A Local Paracrine and Endocrine Network Involving TGFβ, Cox-2, ROS, and Estrogen Receptor β Influences Reactive Stromal Cell Regulation of Prostate Cancer Cell Motility." Molecular Endocrinology 26, no. 6 (June 1, 2012): 940–54. http://dx.doi.org/10.1210/me.2011-1371.

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Abstract The tumor microenvironment plays a critical role in supporting cancer cells particularly as they disengage from limitations on their growth and motility imposed by surrounding nonreactive stromal cells. We show here that stromal-derived androgenic precursors are metabolized by DU145 human prostate cancer (PCa) cells to generate ligands for estrogen receptor-β, which act to limit their motility through transcriptional regulation of E-cadherin. Although primary human PCa-associated fibroblasts and the human WPMY-1-reactive prostate stromal cell line maintain this inherent estrogen receptor (ER)β-dependent motility inhibitor activity, they are subverted by TGF-β1 pro-oxidant signals derived from cocultured DU145 PCa cells. Specifically, stromal-produced H2O2, which requires Cox-2, acts as a second paracrine factor to inhibit ERβ activity in adjacent DU145 cells. Chromatin immunoprecipitation analysis reveals that ERβ recruitment to the E-cadherin promoter is inhibited when H2O2 is present. Both neutralization of H2O2 with catalase and prevention of its production by silencing Cox-2 expression in stromal cells restore the motility-suppression activity of stromal-derived ERβ ligand precursors. These data suggest that reactive stromal cells may still have a capacity to limit cancer cell motility through a local endocrine network but must be protected from pro-oxidant signals triggered by cancer cell-derived TGF-β1 to exhibit this cancer-suppressive function.

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Wang, Jin, Jie-min Dai, Ya-ling Che, Yi-meng Gao, Hui-juan Peng, Bin Liu, Hui Wang, and Hua Linghu. "Elmo1 Helps Dock180 to Regulate Rac1 Activity and Cell Migration of Ovarian Cancer." International Journal of Gynecologic Cancer 24, no. 5 (June 2014): 844–50. http://dx.doi.org/10.1097/igc.0000000000000137.

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ObjectiveEngulfment and cell motility 1 (Elmo1) has been reported to cooperate with dedicator of cytokinesis 1 (Dock180) and to be linked to the invasive phenotype of cancer cells through activating small G-protein Rac. We aimed to study the role of Elmo1 in the malignant migration of ovarian cancer.MethodsEngulfment and cell motility 1 expression was evaluated in specimens from 93 patients with serous ovarian cancer (SOC) by immunohistochemical staining. Next, Elmo1-RNAi cells were established by validated small interference RNAs. Cell proliferation and cell motility were observed and compared with Dock180-RNAi cells. To confirm their synergetic contribution to forming focal adhesion and activating Rac1, Rac1-GTP level was measured by GST pull-down assay and immunofluorescence was used to observe focal adhesion formation both in Elmo1-RNAi and Dock180-RNAi cells.ResultsEngulfment and cell motility 1 was mainly overexpressed in high-grade SOC tissues. Western blot analysis demonstrated that both Elmo1 and Dock180 expressions were hampered in Elmo1-RNAi cells. Compared with the negative control, decreased colony formation and cell invasion were observed in Elmo1-RNAi cells and Dock180-RNAi cells. Consistently, both exhibited reduced Rac1-GTP level and inhibited focal adhesion formation.ConclusionsEngulfment and cell motility 1 presents with synergetic action in helping Dock180 to activate Rac1 and promote cell motility, and thus promote untoward expansion and aggressiveness of SOC.

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Suzuki, Y., A. Mobaraki, W. Al-Jahdari, Y. Yoshida, H. Sakurai, and T. Nakano. "In Vitro, Fractionation Enhances Cells Motility." International Journal of Radiation Oncology*Biology*Physics 72, no. 1 (September 2008): S719. http://dx.doi.org/10.1016/j.ijrobp.2008.06.1588.

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Stohnii, Y. M., M. V. Ryzhykova, A. V. Rebriev, M. D. Kuchma, R. Y. Marunych, V. O. Chernyshenko, V. A. Shablii, et al. "Aggregation of platelets, proliferation of endothelial cells and motility of cancer cells are mediated by the B?1(15)-42 residue of fibrin(ogen)." Ukrainian Biochemical Journal 92, no. 2 (April 17, 2020): 72–84. http://dx.doi.org/10.15407/ubj92.02.072.

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Baker, Martin J., Martín C. Abba, Rafael Garcia-Mata, and Marcelo G. Kazanietz. "P-REX1-Independent, Calcium-Dependent RAC1 Hyperactivation in Prostate Cancer." Cancers 12, no. 2 (February 19, 2020): 480. http://dx.doi.org/10.3390/cancers12020480.

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The GTPase Rac1 is a well-established master regulator of cell motility and invasiveness contributing to cancer metastasis. Dysregulation of the Rac1 signaling pathway, resulting in elevated motile and invasive potential, has been reported in multiple cancers. However, there are limited studies on the regulation of Rac1 in prostate cancer. Here, we demonstrate that aggressive androgen-independent prostate cancer cells display marked hyperactivation of Rac1. This hyperactivation is independent of P-Rex1 activity or its direct activators, the PI3K product PIP3 and Gβγ subunits. Furthermore, we demonstrate that the motility and invasiveness of PC3 prostate cancer cells is independent of P-Rex1, supporting the analysis of publicly available datasets indicating no correlation between high P-Rex1 expression and cancer progression in patients. Rac1 hyperactivation was not related to the presence of activating Rac1 mutations and was insensitive to overexpression of a Rac-GAP or the silencing of specific Rac-GEFs expressed in prostate cancer cells. Interestingly, active Rac1 levels in these cells were markedly reduced by elevations in intracellular calcium or by serum stimulation, suggesting the presence of an alternative means of Rac1 regulation in prostate cancer that does not involve previously established paradigms.

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McCarty, Samantha K., Motoyasu Saji, Xiaoli Zhang, Christina M. Knippler, Lawrence S. Kirschner, Soledad Fernandez, and Matthew D. Ringel. "BRAF activates and physically interacts with PAK to regulate cell motility." Endocrine-Related Cancer 21, no. 6 (September 16, 2014): 865–77. http://dx.doi.org/10.1530/erc-14-0424.

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Increased p21-activated kinase (PAK) signaling and expression have been identified in the invasive fronts of aggressive papillary thyroid cancers (PTCs), including those withRET/PTC, BRAFV600E, and mutantRASexpression. Functionally, thyroid cancer cell motilityin vitrois dependent on group 1 PAKs, particularly PAK1. In this study, we hypothesize that BRAF, a central kinase in PTC tumorigenesis and invasion, regulates thyroid cancer cell motility in part through PAK activation. Using three well-characterized human thyroid cancer cell lines, we demonstrated in all cell lines thatBRAFknockdown reduced PAK phosphorylation of direct downstream targets. In contrast, inhibition of MEK activity either pharmacologically or with siRNA did not reduce PAK activity, indicating MEK is dispensable for PAK activity. Inhibition of cell migration through BRAF loss is rescued by overexpression of either constitutive active MEK1 or PAK1, demonstrating that both signaling pathways are involved in BRAF-regulated cell motility. To further characterize BRAF–PAK signaling, immunofluorescence and immunoprecipitation demonstrated that both exogenously overexpressed and endogenous PAK1 and BRAF co-localize and physically interact, and that this interaction was enhanced in mitosis. Finally, we demonstrated that acute induction of BRAFV600E expressionin vivoin murine thyroid glands results in increased PAK expression and activity confirming a positive signaling relationshipin vivo. In conclusion, we have identified a signaling pathway in thyroid cancer cells which BRAF activates and physically interacts with PAK and regulates cell motility.

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KURAMITSU, SHOTARO, TAKAAKI MASUDA, QINGJIANG HU, TARO TOBO, MASAKAZU YASHIRO, ATSUSHI FUJII, AKIHIRO KITAGAWA, et al. "Cancer-associated Fibroblast-derived Spondin-2 Promotes Motility of Gastric Cancer Cells." Cancer Genomics - Proteomics 18, no. 4 (2021): 521–29. http://dx.doi.org/10.21873/cgp.20277.

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Ramonaite, Rima, Robertas Petrolis, Simge Unay, Gediminas Kiudelis, Jurgita Skieceviciene, Limas Kupcinskas, Mehmet Dincer Bilgin, and Algimantas Krisciukaitis. "Mathematical morphology-based imaging of gastrointestinal cancer cell motility and 5-aminolevulinic acid-induced fluorescence." Biomedical Engineering / Biomedizinische Technik 64, no. 6 (December 18, 2019): 711–20. http://dx.doi.org/10.1515/bmt-2018-0197.

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Abstract The aim of this study was the quantitative evaluation of gastrointestinal cancer cell motility and 5-aminolevulinic acid (5-ALA)-induced fluorescence in vitro using mathematical morphology and structural analysis methods. The results of our study showed that MKN28 cells derived from the lymph node have the highest motility compared with AGS or HCT116 cells derived from primary tumors. Regions of single cells were characterized as most moving, and “tightly packed” cell colonies as nearly immobile. We determined the reduction of cell motility in late passage compared to early passage. Application of 5-ALA caused fluorescence in all investigated cells, and the fluorescence was different with regard to the cell type and application time. We observed higher fluorescence in MKN28 cells. Comprehensive image analysis did not reveal any statistically significant difference in fluorescence intensity between “tightly packed” cell regions, where nearly no motility was registered and loosely distributed cells, where the highest cell motility was registered. In conclusions, our study revealed that MKN28 cells derived from the lymph node have higher motility and 5-ALA-induced fluorescence than AGS or HCT116 derived from primary tumors. Moreover, image analysis based on a large amount of processed data is an important tool to study these tumor cell properties.

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Butler, George, Shirley J. Keeton, Louise J. Johnson, and Philip R. Dash. "A phenotypic switch in the dispersal strategy of breast cancer cells selected for metastatic colonization." Proceedings of the Royal Society B: Biological Sciences 287, no. 1940 (December 2, 2020): 20202523. http://dx.doi.org/10.1098/rspb.2020.2523.

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An important question in cancer evolution concerns which traits make a cell likely to successfully metastasize. Cell motility phenotypes, mediated by cell shape change, are strong candidates. We experimentally evolved breast cancer cells in vitro for metastatic capability, using selective regimes designed to simulate stages of metastasis, then quantified their motility behaviours using computer vision. All evolved lines showed changes to motility phenotypes, and we have identified a previously unknown density-dependent motility phenotype only seen in cells selected for colonization of decellularized lung tissue. These cells increase their rate of morphological change with an increase in migration speed when local cell density is high. However, when the local cell density is low, we find the opposite relationship: the rate of morphological change decreases with an increase in migration speed. Neither the ancestral population, nor cells selected for their ability to escape or invade extracellular matrix-like environments, displays this dynamic behavioural switch. Our results suggest that cells capable of distant-site colonization may be characterized by dynamic morphological phenotypes and the capacity to respond to the local social environment.

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He, Huimin, Li Xiao, Sinan Cheng, Qian Yang, Jinmei Li, Yifan Hou, Fengying Song, et al. "Annexin A2 Enhances the Progression of Colorectal Cancer and Hepatocarcinoma via Cytoskeleton Structural Rearrangements." Microscopy and Microanalysis 25, no. 4 (June 7, 2019): 950–60. http://dx.doi.org/10.1017/s1431927619000679.

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AbstractAnnexin A2 (ANXA2) is reported to be associated with cancer development. To investigate the roles ANXA2 plays during the development of cancer, the RNAi method was used to inhibit the ANXA2 expression in caco2 (human colorectal cancer cell line) and SMMC7721 (human hepatocarcinoma cell line) cells. The results showed that when the expression of ANXA2 was efficiently inhibited, the growth and motility of both cell lines were significantly decreased, and the development of the motility relevant microstructures, such as pseudopodia, filopodia, and the polymerization of microfilaments and microtubules were obviously inhibited. The cancer cell apoptosis was enhanced without obvious significance. The possible regulating pathway in the process was also predicted and discussed. Our results suggested that ANXA2 plays important roles in maintaining the malignancy of colorectal and hepatic cancer by enhancing the cell proliferation, motility, and development of the motility associated microstructures of cancer cells based on a possible complicated signal pathway.

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Dong, Xiaoyun, Waixing Tang, Stephen Stopenski, Marcia S. Brose, Christopher Korch, and Judy L. Meinkoth. "RAP1GAP inhibits cytoskeletal remodeling and motility in thyroid cancer cells." Endocrine-Related Cancer 19, no. 4 (June 13, 2012): 575–88. http://dx.doi.org/10.1530/erc-12-0086.

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The functional significance of decreased RAP1GAP protein expression in human tumors is unclear. To identify targets of RAP1GAP downregulation in the thyroid gland, RAP1 and RAP2 protein expression in human thyroid cells and in primary thyroid tumors were analyzed. RAP1GAP and RAP2 were co-expressed in normal thyroid follicular cells. Intriguingly, RAP1 was not detected in normal thyroid cells, although it was detected in papillary thyroid carcinomas, which also expressed RAP2. Both RAP proteins were detected at the membrane in papillary thyroid tumors, suggesting that they are activated when RAP1GAP is downregulated. To explore the functional significance of RAP1GAP depletion, RAP1GAP was transiently expressed at the lowest level that is sufficient to block endogenous RAP2 activity in papillary and anaplastic thyroid carcinoma cell lines. RAP1GAP impaired the ability of cells to spread and migrate on collagen. Although RAP1GAP had no effect on protein tyrosine phosphorylation in growing cells, RAP1GAP impaired phosphorylation of focal adhesion kinase and paxillin at sites phosphorylated by SRC in cells acutely plated on collagen. SRC activity was increased in suspended cells, where it was inhibited by RAP1GAP. Inhibition of SRC kinase activity impaired cell spreading and motility. These findings identify SRC as a target of RAP1GAP depletion and suggest that the downregulation of RAP1GAP in thyroid tumors enhances SRC-dependent signals that regulate cellular architecture and motility.

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Kondratyeva, Liya, Igor Chernov, Eugene Kopantzev, Dmitry Didych, Alexey Kuzmich, Irina Alekseenko, Sergey Kostrov, and Eugene Sverdlov. "Pancreatic Lineage Specifier PDX1 Increases Adhesion and Decreases Motility of Cancer Cells." Cancers 13, no. 17 (August 30, 2021): 4390. http://dx.doi.org/10.3390/cancers13174390.

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Intercellular interactions involving adhesion factors are key operators in cancer progression. In particular, these factors are responsible for facilitating cell migration and metastasis. Strengthening of adhesion between tumor cells and surrounding cells or extracellular matrix (ECM), may provide a way to inhibit tumor cell migration. Recently, we demonstrated that PDX1 ectopic expression results in the reduction of pancreatic cancer line PANC-1 cell motility in vitro and in vivo, and we now provide experimental data confirming the hypothesis that suppression of migration may be related to the effect of PDX1 on cell adhesion. Cell migration analyses demonstrated decreased motility of pancreatic Colo357 and PANC-1 cell lines expressing PDX1. We observed decreased expression levels of genes associated with promoting cell migration and increased expression of genes negatively affecting cell motility. Expression of the EMT regulator genes was only mildly induced in cells expressing PDX1 during the simulation of the epithelial-mesenchymal transition (EMT) by the addition of TGFβ1 to the medium. PDX1-expressing cancer cell lines showed increased cell adhesion to collagen type I, fibronectin, and poly-lysine. We conclude that ectopic expression of PDX1 reduces the migration potential of cancer cells, by increasing the adhesive properties of cells and reducing the sensitivity to TGFβ1-induced EMT.

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Gelsomino, Luca, Cinzia Giordano, Giusi La Camera, Diego Sisci, Stefania Marsico, Antonella Campana, Roberta Tarallo, et al. "Leptin Signaling Contributes to Aromatase Inhibitor Resistant Breast Cancer Cell Growth and Activation of Macrophages." Biomolecules 10, no. 4 (April 3, 2020): 543. http://dx.doi.org/10.3390/biom10040543.

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Obesity represents a risk factor for breast cancer development and therapy resistance, but the molecular players underling these links are unclear. Here, we identify a role for the obesity-cytokine leptin in sustaining aromatase inhibitor (AI) resistant growth and progression in breast cancer. Using as experimental models MCF-7 breast cancer cells surviving long-term treatment with the AI anastrozole (AnaR) and Ana-sensitive counterparts, we found that AnaR cells expressed higher levels of leptin and its receptors (ObR) along with a constitutive activation of downstream effectors. Accordingly, leptin signaling inhibition reduced only AnaR cell growth and motility, highlighting the existence of an autocrine loop in mechanisms governing drug-resistant phenotypes. In agreement with ObR overexpression, increasing doses of leptin were able to stimulate to a greater extent growth and migration in AnaR than sensitive cells. Moreover, leptin contributed to enhanced crosstalk between AnaR cells and macrophages within the tumor microenvironment. Indeed, AnaR, through leptin secretion, modulated macrophage profiles and increased macrophage motility through CXCR4 signaling, as evidenced by RNA-sequencing, real-time PCR, and immunoblotting. Reciprocally, activated macrophages increased AnaR cell growth and motility in coculture systems. In conclusion, acquired AI resistance is accompanied by the development of a leptin-driven phenotype, highlighting the potential clinical benefit of targeting this cytokine network in hormone-resistant breast cancers, especially in obese women.

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Xu, Yan-Feng. "Fascin promotes the motility and invasiveness of pancreatic cancer cells." World Journal of Gastroenterology 17, no. 40 (2011): 4470. http://dx.doi.org/10.3748/wjg.v17.i40.4470.

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Chen, Xiaochao, Xiangdong Yang, Jiefei Mu, and Chaochi Yue. "Ligustrazine inhibits the viability and motility of colon cancer cells." Translational Cancer Research 9, no. 5 (May 2020): 3203–13. http://dx.doi.org/10.21037/tcr-20-940.

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Wong, Karrie, Umayal Rubenthiran, and Serge Jothy. "Motility of colon cancer cells: modulation by CD44 isoform expression." Experimental and Molecular Pathology 75, no. 2 (October 2003): 124–30. http://dx.doi.org/10.1016/s0014-4800(03)00053-4.

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Goicoechea, S. M., B. Bednarski, R. García-Mata, H. Prentice-Dunn, H. J. Kim, and C. A. Otey. "Palladin contributes to invasive motility in human breast cancer cells." Oncogene 28, no. 4 (November 3, 2008): 587–98. http://dx.doi.org/10.1038/onc.2008.408.

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Wei, Yan, Guangfu Yin, Chuying Ma, Xiaoming Liao, Xianchun Chen, Zhongbing Huang, and Yadong Yao. "Inhibiting the motility and invasion of cancer cells by biomineralization." Medical Hypotheses 81, no. 2 (August 2013): 169–71. http://dx.doi.org/10.1016/j.mehy.2013.05.014.

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Lee, Yong Joo, Myoung-Eun Han, Su-Jin Baek, Seon-Young Kim, and Sae-Ock Oh. "MED30 Regulates the Proliferation and Motility of Gastric Cancer Cells." PLOS ONE 10, no. 6 (June 25, 2015): e0130826. http://dx.doi.org/10.1371/journal.pone.0130826.

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Naishiro, Yasuyoshi, Masaaki Adachi, Hiroyuki Okuda, Atsushi Yawata, Toshihiro Mitaka, Shinichi Takayama, John C. Reed, Yuji Hinoda, and Kohzoh Imai. "BAG-1 accelerates cell motility of human gastric cancer cells." Oncogene 18, no. 21 (May 1999): 3244–51. http://dx.doi.org/10.1038/sj.onc.1202661.

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Nasir, S. N., N. Abu, N. S. Ab Mutalib, M. Ishak, I. Sagap, L. Mazlan, I. M. Rose, and R. Jamal. "LOC285629 regulates cell proliferation and motility in colorectal cancer cells." Clinical and Translational Oncology 20, no. 6 (November 2, 2017): 775–84. http://dx.doi.org/10.1007/s12094-017-1788-x.

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Liu, Jinyi, Dongyun Zhang, Wenjing Luo, Yonghui Yu, Jianxiu Yu, Jingxia Li, Xinhai Zhang, et al. "X-linked Inhibitor of Apoptosis Protein (XIAP) Mediates Cancer Cell Motility via Rho GDP Dissociation Inhibitor (RhoGDI)-dependent Regulation of the Cytoskeleton." Journal of Biological Chemistry 286, no. 18 (March 14, 2011): 15630–40. http://dx.doi.org/10.1074/jbc.m110.176982.

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X-linked inhibitor of apoptosis protein (XIAP) overexpression has been found to be associated with malignant cancer progression and aggression in individuals with many types of cancers. However, the molecular basis of XIAP in the regulation of cancer cell biological behavior remains largely unknown. In this study, we found that a deficiency of XIAP expression in human cancer cells by either knock-out or knockdown leads to a marked reduction in β-actin polymerization and cytoskeleton formation. Consistently, cell migration and invasion were also decreased in XIAP-deficient cells compared with parental wild-type cells. Subsequent studies demonstrated that the regulation of cell motility by XIAP depends on its interaction with the Rho GDP dissociation inhibitor (RhoGDI) via the XIAP RING domain. Furthermore, XIAP was found to negatively regulate RhoGDI SUMOylation, which might affect its activity in controlling cell motility. Collectively, our studies provide novel insights into the molecular mechanisms by which XIAP regulates cancer invasion and offer a further theoretical basis for setting XIAP as a potential prognostic marker and specific target for treatment of cancers with metastatic properties.

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Pietrovito, Laura, Giuseppina Comito, Matteo Parri, Elisa Giannoni, Paola Chiarugi, and Maria Letizia Taddei. "Zoledronic Acid Inhibits the RhoA-mediated Amoeboid Motility of Prostate Cancer Cells." Current Cancer Drug Targets 19, no. 10 (December 23, 2019): 807–16. http://dx.doi.org/10.2174/1568009619666190115142858.

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Background:The bisphosphonate Zoledronic acid (ZA) is a potent osteoclast inhibitor currently used in the clinic to reduce osteoporosis and cancer-induced osteolysis. Moreover, ZA exerts an anti-tumor effect in several tumors. Despite this evidence, the relevance of ZA in prostate cancer (PCa) is not completely understood.Objective:To investigate the effect of ZA administration on the invasive properties of PC3 cells, which are characterised by RhoA-dependent amoeboid motility.Methods:The effect of ZA administration on the in vitro invasive properties of PC3 cells was evaluated by cell migration in 3D collagen matrices, immunofluorescence and Boyden assays or transendothelial migration. Lung retention and colonization assays were performed to assess the efficacy of ZA administration in vivo.Results:PC3 cells are characterised by RhoA-dependent amoeboid motility. We now report a clear inhibition of in vitro PC3 cell invasion and RhoA activity upon ZA treatment. Moreover, to confirm a specific role of ZA in the inhibition of amoeboid motility of PC3 cells, we demonstrate that ZA interferes only partially with PC3 cells showing a mesenchymal phenotype due to both treatment with conditioned medium of cancer associated fibroblasts or to the acquisition of chemoresistance. Furthermore, we demonstrate that ZA impairs adhesion to endothelial cells and the trans-endothelial cell migration, two essential properties characterising amoeboid motility and PC3 metastatic dissemination. In vivo experiments prove the ability of ZA to inhibit the metastatic process of PC3 cells as shown by the decrease in lung colonization.Conclusion:This study demonstrates that ZA inhibits Rho-dependent amoeboid motility of PC3 cells, thus suggesting ZA as a potential therapy to impede the metastatic dissemination of PC3 cells.

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Hui, T. H., W. C. Cho, H. W. Fong, M. Yu, K. W. Kwan, K. C. Ngan, K. H. Wong, et al. "An electro-osmotic microfluidic system to characterize cancer cell migration under confinement." Journal of The Royal Society Interface 16, no. 155 (June 2019): 20190062. http://dx.doi.org/10.1098/rsif.2019.0062.

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We have developed a novel electro-osmotic microfluidic system to apply precisely controlled osmolarity gradients to cancer cells in micro-channels. We observed that albeit adhesion is not required for cells to migrate in such a confined microenvironment, the migrating velocity of cells is strongly influenced by the interactions between the cells and the channel wall, with a stronger adhesion leading to diminished cell motility. Furthermore, through examining more than 20 different types of cancer cells, we found a linear positive correlation between the protein concentration of the aquaporin-4 (AQP4) and the cell migrating speed. Knockdown of AQP4 in invasive re-populated cancer stem cells reduced their migration capability down to the level that is comparable to their parental cancer cells. Interestingly, these observations can all be quantitatively explained by the osmotic engine model where the cell movement is assumed to be driven by cross-membrane ion/water transport, while adhesion acts as a frictional resistance against the cell motility. By providing versatile and controllable features in regulating and characterizing the migration capability of cells, our system may serve as a useful tool in quantifying how cell motility is influenced by different physical and biochemical factors, as well as elucidating the mechanisms behind, in the future.

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Lang, Sven A., Franziska Brandes, and Edward K. Geissler. "Inhibition of cMET in an experimental model of pancreatic cancer." Journal of Clinical Oncology 31, no. 4_suppl (February 1, 2013): 185. http://dx.doi.org/10.1200/jco.2013.31.4_suppl.185.

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185 Background: In human pancreatic cancer, expression of cMET is associated with poor survival. So far, activation/expression of cMET by hepatocyte growth factor (HGF) has been shown to induce proliferation and motility in cancer cells. Therefore, we hypothesized that inhibition of cMET in human pancreatic cancer cell lines impairs oncogenic signaling and tumor growth. Methods: Pancreatic cancer cell lines (HPAF-II, MiaPaCa2, L3.6pl, BxPC3, Panc02) and the cMET inhibitor INC280 (Novartis Oncology, Basel) were used. MiaPaCa2 and L3.6pl pancreatic cancer cells were grown with gemcitabine up to 500 and 250 nM, respectively (then called MiaPaCa2(G500) and L3.6pl(G250)). MTT and Boyden Chamber assays were used to determine effects of INC280 on growth and motility of cells in vitro. Expression of growth factor receptors, activation of signaling intermediates and expression of transcription factors were assessed by Western blotting. Finally, in vitro results were validated in an orthotopic tumor model using L3.6pl pancreatic cancer cell line. Results: All pancreatic cancer cell lines showed expression of cMET. In vitro treatment of cancer cells with INC280 led to a minor, dose-dependent inhibition of growth even when cells were supplemented with HGF. In contrast, migration assays showed a significant reduction of cancer cell motility upon INC280 when cells were stimulated with HGF (P<0.05). Regarding oncogenic signaling, INC280 led to inhibition of HGF-induced phosphorylation of AKT, ERK and FAK. In addition, c-Myc expression was diminished in cancer cells. Interestingly, gemcitabine resistant cell line MiaPaCa2(G500) showed higher cMET expression levels compared to the normal MiaPaCa2. Stimulation of MiaPaCa2(G500) with HGF led to strong induction of oncogenic signaling and tumor cell motility, an effect that was significantly diminished by INC280. Moreover, results from in vivo experiments show that therapy with INC280 (10 mg/kg/d) significantly reduces tumor growth as determined by final tumor weight (P<0.05). Conclusions: In pancreatic cancer cell lines, targeting cMET with INC280 abrogates oncogenic signaling in vitro and impairs tumor growth in vivo. Therefore, the concept of cMET inhibition warrants further preclinical evaluation.

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Niizeki, H., M. Kobayashi, I. Horiuchi, N. Akakura, J. Chen, J. Wang, J.-i. Hamada, et al. "Hypoxia enhances the expression of autocrine motility factor and the motility of human pancreatic cancer cells." British Journal of Cancer 86, no. 12 (June 2002): 1914–19. http://dx.doi.org/10.1038/sj.bjc.6600331.

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Lee, Hana, Won-Jin Kim, Hyeon-Gu Kang, Jun-Ho Jang, Il Ju Choi, Kyung-Hee Chun, and Seok-Jun Kim. "Upregulation of LAMB1 via ERK/c-Jun Axis Promotes Gastric Cancer Growth and Motility." International Journal of Molecular Sciences 22, no. 2 (January 10, 2021): 626. http://dx.doi.org/10.3390/ijms22020626.

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Gastric cancer is the fifth most common cancer worldwide with a poor survival rate. Therefore, it is important to identify predictive and prognostic biomarkers of gastric cancer. Laminin subunit beta 1 (LAMB1) is involved in attachment, migration, and organization during development, and its elevated expression has been associated with several cancers. However, the role and mechanism of LAMB1 in gastric cancer remains unknown. Here, we determined that LAMB1 is upregulated in gastric cancer tissues and contributes to cell growth and motility. Using a public database, we showed that LAMB1 expression was significantly upregulated in gastric cancer compared to normal tissues. LAMB1 was also found to be associated with poor prognosis in patients with gastric cancer. Overexpression of LAMB1 elevated cell proliferation, invasion, and migration; however, knockdown of LAMB1 decreased these effects in gastric cancer cells. U0126, an extracellular signal-regulated kinase (ERK) inhibitor, regulated the expression of LAMB1 in gastric cancer cells. Additionally, we showed that c-Jun directly binds to the LAMB1 promoter as a transcription factor and regulates its gene expression via the ERK pathway in gastric cancer cells. Therefore, our study indicates that LAMB1 promotes cell growth and motility via the ERK/c-Jun axis and is a potential biomarker and therapeutic target of gastric cancer.

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Journal articles on the topic 'Cancer cells – Motility'

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