αV-class integrins exert dual roles on α5β1 integrins to strengthen adhesion to fibronectin

Bharadwaj, Mitasha; Strohmeyer, Nico; Colò, G.; Helenius, Jonne; Beerenwinkel, Niko; Schiller, Herbert B.; Fässler, Reinhard; Müller, Daniel J.

doi:10.1038/ncomms14348

Cited by 99 publications

(100 citation statements)

References 51 publications

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“…The initial step includes the faster adhesion of αV‐class integrins to fibronectin than that shown by α5β1 integrins, which leads to the activation of a group of adhesion‐associated proteins that involved in binding to the Actin cytoskeleton. A consequence of the initial step is the activation of Rac1/Wave/Arp2/3 and RhoA/Rock signaling, which leads to the binding of α5β1 integrins …”

Section: Ecm‐derived Adhesion Moleculesmentioning

confidence: 95%

“…A recent study revealed the impact of αV‐class integrins on the potent adhesion to fibronectin, which characterized by two main steps . The initial step includes the faster adhesion of αV‐class integrins to fibronectin than that shown by α5β1 integrins, which leads to the activation of a group of adhesion‐associated proteins that involved in binding to the Actin cytoskeleton.…”

Section: Ecm‐derived Adhesion Moleculesmentioning

confidence: 99%

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The Impact of Adhesion Molecules on the In Vitro Culture and Differentiation of Stem Cells

Dayem

Lee

Choi

et al. 2017

Biotechnology Journal

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The term "cell adhesion" represents cell-cell interactions and the interaction between the cell and the extracellular matrix (ECM). These interactions are crucial for the development of the stem cells niche to determine stem cell shape. The ECM is considered as a natural niche for cell residence. Cell adhesion molecules (CAMs) enable cell-cell interactions and the interactions between the cell and ECM via various mechanisms, such as trans-interaction and the heterophilic interactions. These interactions promote a broad spectrum of cell signaling that directly or indirectly modulates stem cell proliferation, self-renewal property, adhesion, and multilineage differentiation. Over many years, animal-derived feeder layers and culture components have been used for stem cell culture, which produces stem cells unsuitable for clinical applications in the regenerative medicine. This review briefly describes the stages of the development of stem cell culture toward a defined condition and the drawbacks of using animal-derived culture components. Stem cell niche-derived and ECM-derived adhesion molecules and their detailed impact on stem cell adhesion and functions will be discussed. Efficient and novel adhesion molecules for stem cell culture and differentiation are needed for further large-scale applications in tissue regeneration.

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Section: Ecm‐derived Adhesion Moleculesmentioning

confidence: 95%

Section: Ecm‐derived Adhesion Moleculesmentioning

confidence: 99%

The Impact of Adhesion Molecules on the In Vitro Culture and Differentiation of Stem Cells

Dayem

Lee

Choi

et al. 2017

Biotechnology Journal

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“…The glial scar-inhibitor aggrecan can impair integrin activation (79), which inhibits neurite outgrowth. At the same time, talin binding to integrin tails is a significant step in integrin activation (31), whereas actinin, ICAP-1, filamin, SHARPIN, and DOK1 can compete with talin for binding to integrin (53)(54)(55)(56)(57)(58)(59)61). Therefore, we investigated the connection between the competitive binding proteins of talin and aggrecan stimulation during neuron polarization.…”

Section: Role Of Talin-integrin Signaling In Osmotic Pressurementioning

confidence: 99%

“…Filamin binds to the actin skeleton under tension, resulting in exposure of integrin binding sites, which also induces competitive binding with talin (53)(54)(55). Furthermore, integrin cytoplasmic domain-associated protein-1 (ICAP-1) and docking protein 1 (DOK1) can bind to integrin b through a phosphorylated (p) Y binding domain-Asn-Pro-Xaa-phosphotyrosine (NPxY) interaction (55)(56)(57)(58)(59)(60), and SHANK-associated RH domain interactor (SHARPIN) can bind to the highly conserved WHXGFFKR sequence in the tail of integrin a both of which cause direct competition with talin for integrin b binding (61). Whether this competitive binding affects the chemical and mechanical signals remains unclear.…”

mentioning

confidence: 99%

Talin promotes integrin activation accompanied by generation of tension in talin and an increase in osmotic pressure in neurite outgrowth

et al. 2019

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Neuronal polarization depends on the interaction of intracellular chemical and mechanical activities in which the cytoplasmic protein, talin, plays a pivotal role during neurite growth. To better understand the mechanism underlying talin function in neuronal polarization, we overexpressed several truncated forms of talin and found that the presence of the rod domain within the overexpressed talin is required for its positive effect on neurite elongation because the neurite number only increased when the talin head region was overexpressed. The tension in the talin rod was recognized using a Förster resonance energy transfer‐based tension probe. Nerve growth factor treatment resulted in inward tension of talin elicited by microfilament force and outward osmotic pressure. By contrast, the glial scar‐inhibitor aggrecan weakened these forces, suggesting that interactions between inward pull forces in the talin rod and outward osmotic pressure participate in neuronal polarization. Integrin activation is also involved in up‐regulation of talin tension and osmotic pressure. Aggrecan stimuli resulted in up‐regulation of docking protein 1 (DOK1), leading to the down‐regulation of integrin activity and attenuation of the intracellular mechanical force. Our study suggests interactions between the intracellular inward tension in talin and the outward osmotic pressure as the effective channel for promoting neurite outgrowth, which can be up‐regulated by integrin activation and down‐regulated by DOK1.—Wang, Y., Zhang, X., Tian, J., Shan, J., Hu, Y., Zhai, Y., Guo, J. Talin promotes integrin activation accompanied by generation of tension in talin and an increase in osmotic pressure in neurite outgrowth. FASEB J. 33, 6311–6326 (2019). http://www.fasebj.org

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“…An interaction between uPAR and different integrin subunits, mostly β1, β3 and β6, has been described by biochemical and computational technics [32][33][34][35] . Because the β1 integrin subunit is the receptor for fibronectin [36][37][38] , and since fibronectin is required in our system for uPA/uPAR to promote axonal regeneration, then we postulated that β1 integrin was the co-receptor that mediates the effect of uPA/uPAR on neurorepair. Our hypothesis was further supported by reports from other groups indicating that neuronal β1 integrin expression increases after ischemic stroke [39] and that β1 integrin promotes the regeneration of sensorial axons at long distances in the spinal cord [40] .…”

Section: Membrane Recruitment Of ß1-integrin Mediates Upa/upar-inducementioning

confidence: 99%

Urokinase-type Plasminogen Activator (uPA) and its Receptor (uPAR) Promote Neurorepair in the Ischemic Brain

Merino

Diaz

Yepes

2017

Receptor Clin Invest

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Despite the fact that ischemic stroke has been considered a leading cause of mortality in the world, recent advances in our understanding of the pathophysiological mechanisms underlying the ischemic injury and the treatment of acute ischemic stroke patients have led to a sharp decrease in the number of stroke deaths. However, this decrease in stroke mortality has also led to an increase in the number of patients that survive the acute ischemic injury with different degrees of disability. Unfortunately, to this date we do not have an effective therapeutic strategy to promote neurological recovery in these growing population of stroke survivors. Cerebral ischemia not only causes the destruction of a large number of axons and synapses but also activates endogenous mechanisms that promote the recovery of those neurons that survive its harmful effects. Here we review experimental evidence indicating that one of these mechanisms of repair is the binding of the serine proteinase urokinase-type plasminogen activator (uPA) to its receptor (uPAR) in the growth cones of injured axons. Indeed, the binding of uPA to uPAR in the periphery of growth cones of injured axons induces the recruitment of β1-integrin to the plasma membrane, β1-integrin-mediated activation of the small Rho GTPase Rac1, and Rac1-induced axonal regeneration. Furthermore, we found that this process is modulated by the low density lipoprotein receptor-related protein (LRP1). The data reviewed here indicate that the uPA-uPAR-LRP1 system is a potential target for the development of therapeutic strategies to promote neurological recovery in acute ischemic stroke patients.Keywords: Urokinase-type plasminogen activator (uPA); urokinase-type plasminogen activator receptor (uPAR); plasmin; cerebral ischemia; neurorepair; low density lipoprotein receptor-related protein 1 (LRP1)To cite this article: Paola Merino, et al. Urokinase-type plasminogen activator (uPA) and its receptor (uPAR) promote neurorepair in the ischemic brain.

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αV-class integrins exert dual roles on α5β1 integrins to strengthen adhesion to fibronectin

Cited by 99 publications

References 51 publications

The Impact of Adhesion Molecules on the In Vitro Culture and Differentiation of Stem Cells

The Impact of Adhesion Molecules on the In Vitro Culture and Differentiation of Stem Cells

Talin promotes integrin activation accompanied by generation of tension in talin and an increase in osmotic pressure in neurite outgrowth

Urokinase-type Plasminogen Activator (uPA) and its Receptor (uPAR) Promote Neurorepair in the Ischemic Brain

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