Integrin-mediated adhesion and mechanosensing in the mammary gland

Paavolainen, Oona; Peuhu, Emilia

doi:10.1016/j.semcdb.2020.10.010

Cited by 14 publications

(8 citation statements)

References 150 publications

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“…α2β1 and α5β1 integrin heterodimers exhibit the highest affinity towards collagens and RGD motif-containing matrix proteins (e.g. Fibronectin), respectively, and are involved in the process of branching morphogenesis during mammary gland development [ 13 , 35 ]. On the other hand, integrin β1 subunit forms heterodimers with α1–11 subunits, covering a wide range of interacting ECM proteins.…”

Section: Resultsmentioning

confidence: 99%

FGFR2 Controls Growth, Adhesion and Migration of Nontumorigenic Human Mammary Epithelial Cells by Regulation of Integrin β1 Degradation

Mieczkowski

Popęda

Lesniak

et al. 2023

J Mammary Gland Biol Neoplasia

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The role of fibroblast growth factor receptor 2 (FGFR2), an important mediator of stromal paracrine and autocrine signals, in mammary gland morphogenesis and breast cancer has been extensively studied over the last years. However, the function of FGFR2 signalling in the initiation of mammary epithelial oncogenic transformation remains elusive. Here, FGFR2-dependent behaviour of nontumorigenic model of mammary epithelial cells was studied. In vitro analyses demonstrated that FGFR2 regulates epithelial cell communication with extracellular matrix (ECM) proteins. Silencing of FGFR2 significantly changed the phenotype of cell colonies in three-dimensional cultures, decreased integrins α2, α5 and β1 protein levels and affected integrin-driven processes, such as cell adhesion and migration. More detailed analysis revealed the FGFR2 knock-down-induced proteasomal degradation of integrin β1. Analysis of RNA-seq databases showed significantly decreased FGFR2 and ITGB1 mRNA levels in breast tumour samples, when compared to non-transformed tissues. Additionally, high risk healthy individuals were found to have disrupted correlation profiles of genes associated with FGFR2 and integrin signalling, cell adhesion/migration and ECM remodelling. Taken together, our results strongly suggest that FGFR2 loss with concomitant integrin β1 degradation is responsible for deregulation of epithelial cell-ECM interactions and this process may play an important role in the initiation of mammary gland epithelial tumorigenesis.

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Section: Resultsmentioning

confidence: 99%

FGFR2 Controls Growth, Adhesion and Migration of Nontumorigenic Human Mammary Epithelial Cells by Regulation of Integrin β1 Degradation

Mieczkowski

Popęda

Lesniak

et al. 2023

J Mammary Gland Biol Neoplasia

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“…They can be combined with specific domains on ECM proteins such as RGD domain. 74 , 100 After integrins bind with the targeted ECM proteins, intracellular signaling pathways induce integrins to assemble at the plasma membrane and change their conformation to influence the cytoskeletal organization. 101 The integrin assembling accelerates hundreds of cytoplasmic proteins and signaling molecules to move to the attachment site, enhancing the adhesion strength and forming focal adhesions.…”

Section: The Impact Of Tio 2 Ntas On Titanium Impl...mentioning

confidence: 99%

Nanostructured Titanium Implant Surface Facilitating Osseointegration from Protein Adsorption to Osteogenesis: The Example of TiO2 NTAs

Wu¹,

Tang²,

Wang³

et al. 2022

IJN

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“…ECM stiffness plays a critical role in tumor progression by modulating intrinsic properties of tumor cells. The presence of a rigid ECM can determine intracellular contractions further sustaining cell migration [93]. ECM stiffness induces the activation of TGFβ signalling that mediates EMT in cancer cells.…”

Section: Detailed Role In Cancer Referencementioning

confidence: 99%

The extracellular matrix alteration, implication in modulation of drug resistance mechanism: friends or foes?

Jurj

Ionescu

Berindan‐Neagoe

et al. 2022

J Exp Clin Cancer Res

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The extracellular matrix (ECM) is an important component of the tumor microenvironment (TME), having several important roles related to the hallmarks of cancer. In cancer, multiple components of the ECM have been shown to be altered. Although most of these alterations are represented by the increased or decreased quantity of the ECM components, changes regarding the functional alteration of a particular ECM component or of the ECM as a whole have been described. These alterations can be induced by the cancer cells directly or by the TME cells, with cancer-associated fibroblasts being of particular interest in this regard. Because the ECM has this wide array of functions in the tumor, preclinical and clinical studies have assessed the possibility of targeting the ECM, with some of them showing encouraging results. In the present review, we will highlight the most relevant ECM components presenting a comprehensive description of their physical, cellular and molecular properties which can alter the therapy response of the tumor cells. Lastly, some evidences regarding important biological processes were discussed, offering a more detailed understanding of how to modulate altered signalling pathways and to counteract drug resistance mechanisms in tumor cells.

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Integrin-mediated adhesion and mechanosensing in the mammary gland

Cited by 14 publications

References 150 publications

FGFR2 Controls Growth, Adhesion and Migration of Nontumorigenic Human Mammary Epithelial Cells by Regulation of Integrin β1 Degradation

FGFR2 Controls Growth, Adhesion and Migration of Nontumorigenic Human Mammary Epithelial Cells by Regulation of Integrin β1 Degradation

Nanostructured Titanium Implant Surface Facilitating Osseointegration from Protein Adsorption to Osteogenesis: The Example of TiO2 NTAs

The extracellular matrix alteration, implication in modulation of drug resistance mechanism: friends or foes?

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