Digital holographic microscopy for the three-dimensional dynamic analysis of in vitro cancer cell migration

2006 ◽  
Vol 11 (5) ◽  
pp. 054032 ◽  
Author(s):  
Frank Dubois ◽  
Catherine Yourassowsky ◽  
Olivier Monnom ◽  
Jean-Claude Legros ◽  
Olivier Debeir ◽  
...  
Keyword(s):  
Cell Migration ◽  
Dynamic Analysis ◽  
Cancer Cell ◽  
Three Dimensional ◽  
Digital Holographic Microscopy ◽  
Cancer Cell Migration ◽  
Holographic Microscopy

scholarly journals Lactobacilli inhibit cervical cancer cell migration in vitro and reduce tumor burden in vivo through upregulation of E-cadherin

2017 ◽  
Vol 38 (3) ◽  
pp. 1561-1568 ◽  
Author(s):  
Xiaoxi Li ◽  
Hong Wang ◽  
Xingxing Du ◽  
Wenna Yu ◽  
Jingwen Jiang ◽  
...  
Keyword(s):  
Cervical Cancer ◽  
Cell Migration ◽  
Cancer Cell ◽  
Tumor Burden ◽  
Cervical Cancer Cell ◽  
Cancer Cell Migration ◽  
Reduce Tumor Burden ◽  
E Cadherin

scholarly journals Characterization of three-dimensional cancer cell migration in mixed collagen-Matrigel scaffolds using microfluidics and image analysis

PLoS ONE ◽  
2017 ◽  
Vol 12 (2) ◽  
pp. e0171417 ◽  
Author(s):  
María Anguiano ◽  
Carlos Castilla ◽  
Martin Maška ◽  
Cristina Ederra ◽  
Rafael Peláez ◽  
...  
Keyword(s):  
Image Analysis ◽  
Cell Migration ◽  
Cancer Cell ◽  
Three Dimensional ◽  
Cancer Cell Migration

scholarly journals CRMP2 as a Candidate Target to Interfere with Lung Cancer Cell Migration

Biomolecules ◽  
2021 ◽  
Vol 11 (10) ◽  
pp. 1533
Author(s):  
Xabier Morales ◽  
Rafael Peláez ◽  
Saray Garasa ◽  
Carlos Ortiz de Solórzano ◽  
Ana Rouzaut
Keyword(s):  
Cell Migration ◽  
Lung Adenocarcinoma ◽  
Cancer Cell ◽  
Adaptor Protein ◽  
Mechanistic Explanation ◽  
In Vitro Assays ◽  
Cancer Cell Migration ◽  
Cortical Actin

Collapsin response mediator protein 2 (CRMP2) is an adaptor protein that adds tubulin dimers to the growing tip of a microtubule. First described in neurons, it is now considered a ubiquitous protein that intervenes in processes such as cytoskeletal remodeling, synaptic connection and trafficking of voltage channels. Mounting evidence supports that CRMP2 plays an essential role in neuropathology and, more recently, in cancer. We have previously described a positive correlation between nuclear phosphorylation of CRMP2 and poor prognosis in lung adenocarcinoma patients. In this work, we studied whether this cytoskeleton molding protein is involved in cancer cell migration. To this aim, we evaluated CRMP2 phosphorylation and localization in the extending lamella of lung adenocarcinoma migrating cells using in vitro assays and in vivo confocal microscopy. We demonstrated that constitutive phosphorylation of CRMP2 impaired lamella formation, cell adhesion and oriented migration. In search of a mechanistic explanation of this phenomenon, we discovered that CRMP2 Ser522 phospho-mimetic mutants display unstable tubulin polymers, unable to bind EB1 plus-Tip protein and the cortical actin adaptor IQGAP1. In addition, integrin recycling is defective and invasive structures are less evident in these mutants. Significantly, mouse xenograft tumors of NSCLC expressing CRMP2 phosphorylation mimetic mutants grew significantly less than wild-type tumors. Given the recent development of small molecule inhibitors of CRMP2 phosphorylation to treat neurodegenerative diseases, our results open the door for their use in cancer treatment.

scholarly journals Wnt5a induces ROR1 to recruit cortactin to promote breast-cancer migration and metastasis

2019 ◽  
Vol 5 (1) ◽  
Author(s):  
Md Kamrul Hasan ◽  
George F. Widhopf ◽  
Suping Zhang ◽  
Sharon M. Lam ◽  
Zhouxin Shen ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cell Migration ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Surface Protein ◽  
Cancer Cell Migration ◽  
Breast Cancer Cell Migration ◽  
Promote Breast Cancer

Abstract ROR1 is a conserved oncoembryonic surface protein expressed in breast cancer. Here we report that ROR1 associates with cortactin in primary breast-cancer cells or in MCF7 transfected to express ROR1. Wnt5a also induced ROR1-dependent tyrosine phosphorylation of cortactin (Y421), which recruited ARHGEF1 to activate RhoA and promote breast-cancer-cell migration; such effects could be inhibited by cirmtuzumab, a humanized mAb specific for ROR1. Furthermore, treatment of mice bearing breast-cancer xenograft with cirmtuzumab inhibited cortactin phosphorylation in vivo and impaired metastatic development. We established that the proline at 841 of ROR1 was required for it to recruit cortactin and ARHGEF1, activate RhoA, and enhance breast-cancer-cell migration in vitro or development of metastases in vivo. Collectively, these studies demonstrate that the interaction of ROR1 with cortactin plays an important role in breast-cancer-cell migration and metastasis.

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