Integrin ligands at a glance

Humphries, Jonathan D.; Byron, Adam

doi:10.1242/jcs.03098

Cited by 1,408 publications

(1,332 citation statements)

References 16 publications

(14 reference statements)

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“…For specifi c control of cell adhesion, azobenzenes can be biofunctionalized with bio active molecules such as RGD (arginine-glycine-aspartate) peptides that bind members of the integrin cell adhesion receptor family. [ 13 ] Several studies have employed RGD-functionalized azobenzenes for controlling adhesion with promising results, but more than one hour of illumination with UV light was required for switching. [14][15][16] Extended UV exposure is not suitable for bioapplications due to severe phototoxic damage to living cells, [ 17 ] whereas short UV exposure has proven successful in irreversible photoswitching approaches.…”

Section: Doi: 101002/adma201504394mentioning

confidence: 99%

Rapid Reversible Photoswitching of Integrin‐Mediated Adhesion at the Single‐Cell Level

et al. 2015

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Section: Doi: 101002/adma201504394mentioning

confidence: 99%

Rapid Reversible Photoswitching of Integrin‐Mediated Adhesion at the Single‐Cell Level

et al. 2015

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“…Integrin-2 (ITGA2) can form a heterodimer with ITGB1, which is a known collagen receptor [15]. Furthermore, we reported that ITGA2 and ITGB1 regulate lung cancer cell invasion in a 3D collagen matrix [12].…”

Section: Itga2 and Itgb1 Expression Is Controlled By Atf5 To Promotementioning

confidence: 99%

Role of ATF5 in the invasive potential of diverse human cancer cell lines

Nukuda

Endoh

Yasuda

et al. 2016

Biochemical and Biophysical Research Communications

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Activating transcription factor 5 (ATF5) is a member of the ATF/cAMP response element-binding protein family. Our research group recently revealed that ATF5 expression increases the invasiveness of human lung carcinoma cells. However, the effects of ATF5 on the invasive potential of other cancer cells lines remain unclear.Therefore, in this study, we investigated the role of ATF5 in the invasive activity of diverse human cancer cell lines. Invasiveness was assessed using Matrigel invasion assays. ATF5 knockdown resulted in decreased invasiveness in seven of eight cancer cell lines tested. These results suggest that ATF5 promotes invasiveness in several cancer cell lines. Furthermore, the roles of ATF5 in the invasiveness were evaluated in three-dimensional (3D) culture conditions. In 3D collagen gel, HT-1080 and MDA-MB-231 cells exhibited high invasiveness, with spindle morphology and high invasion speed. In both cell lines, knockdown of ATF5 resulted in rounded morphology and decreased invasion speed. Next, we showed that ATF5 induced integrin-2 and integrin-1 expression and that the depletion of integrin-2 or integrin-1 resulted in round morphology and decreased invasion speed. Our results suggest that ATF5 promotes invasion by inducing the expression of integrin-2 and integrin-1 in several 3 human cancer cell lines. ATF5 regulates cell morphology in a 3D collagen gel via integrin-21 activity. Keywords

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“…chondroitin sulfate and keratan sulfate) and are secreted by cells to create their extracellular niche (Humphries et al 2006). Non-ECM ligands include counter-receptors (ICAMs and VCAMs), plasma proteins (fibrinogen and von Willebrand factor), complement factors, cytokines and pathogens (viruses, bacteria and toxins) (Laurie et al 1982;Humphries et al 2006).…”

Section: Integrin Ligandsmentioning

confidence: 99%

“…The third group is the A-domain β1 integrins, which comprises α-subunits containing the inserted αI domain that pair with β1 integrins to form a specific subfamily of laminin/ collagen-binding receptors. The fourth group is the non-αA-domain-containing laminin-binding integrins, which is composed of α-subunits that lack the inserted αI domain and pair with β1 integrins to form specific laminin receptors (Humphries et al 2006). Integrins can also bind to a number of other ligands (for review, see van der Flier and Sonnenberg 2001; Humphries et al 2006).…”

Section: Integrin Ligandsmentioning

confidence: 99%

Structural and mechanical functions of integrins

2013

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Integrins are ubiquitously expressed cell surface receptors that play a critical role in regulating the interaction between a cell and its microenvironment to control cell fate. These molecules are regulated either via their expression on the cell surface or through a unique bidirectional signalling mechanism. However, integrins are just the tip of the adhesome iceberg, initiating the assembly of a large range of adaptor and signalling proteins that mediate the structural and signalling functions of integrin. In this review, we summarise the structure of integrins and mechanisms by which integrin activation is controlled. The different adhesion structures formed by integrins are discussed, as well as the mechanical and structural roles integrins play during cell migration. As the function of integrin signalling can be quite varied based on cell type and context, an in depth understanding of these processes will aid our understanding of aberrant adhesion and migration, which is often associated with human pathologies such as cancer.

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Integrin ligands at a glance

Cited by 1,408 publications

References 16 publications

Rapid Reversible Photoswitching of Integrin‐Mediated Adhesion at the Single‐Cell Level

Rapid Reversible Photoswitching of Integrin‐Mediated Adhesion at the Single‐Cell Level

Role of ATF5 in the invasive potential of diverse human cancer cell lines

Structural and mechanical functions of integrins

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