Search results for "β1 integrin"
showing 8 items of 8 documents
Galectin-3 Released by Pancreatic Ductal Adenocarcinoma Suppresses γδ T Cell Proliferation but Not Their Cytotoxicity
2020
Pancreatic ductal adenocarcinoma (PDAC) is characterized by an immunosuppressive tumor microenvironment with a dense desmoplastic stroma. The expression of β-galactoside-binding protein galectin-3 is regarded as an intrinsic tumor escape mechanism for inhibition of tumor-infiltrating T cell function. In this study, we demonstrated that galectin-3 is expressed by PDAC and by γδ or αβ T cells but is only released in small amounts by either cell population. Interestingly, large amounts of galectin-3 were released during the co-culture of allogeneic in vitro expanded or allogeneic or autologous resting T cells with PDAC cells. By focusing on the co-culture of tumor cells and γδ T cells, we obse…
β1 integrin signaling promotes neuronal migration along vascular scaffolds in the post-stroke brain
2017
Cerebral ischemic stroke is a main cause of chronic disability. However, there is currently no effective treatment to promote recovery from stroke-induced neurological symptoms. Recent studies suggest that after stroke, immature neurons, referred to as neuroblasts, generated in a neurogenic niche, the ventricular-subventricular zone, migrate toward the injured area, where they differentiate into mature neurons. Interventions that increase the number of neuroblasts distributed at and around the lesion facilitate neuronal repair in rodent models for ischemic stroke, suggesting that promoting neuroblast migration in the post-stroke brain could improve efficient neuronal regeneration. To move t…
Fluorescent Small Molecule Probe to Modulate and Explore α2β1 Integrin Function
2011
Collagen binding integrins are an important family of cell surface receptors that mediate bidirectionally signals between the interior of the cell and the extracellular matrix. The protein-protein interactions between cells and collagen are necessary for many physiological functions, but also promote diseases. For example, the interaction of α2β1 integrin and collagen has been shown to have an important role in thrombus formation and cancer spread. The fact that the discovery of small molecules that can block such protein-protein interactions is highly challenging has significantly hindered the discovery of pharmaceutical agents to treat these diseases. Here, we present a rationally designe…
Blockage of collagen binding to integrin α2β1: structure–activity relationship of protein–protein interaction inhibitors
2011
The interaction between the α2β1 integrin and collagen plays a crucial role in the development of pathological conditions, such as thrombus formation and cancer cell metastasis. Accordingly, the α2β1 integrin is a promising target for the development of new drug molecules to treat these diseases. Here, we have designed, synthesized, and measured in vitro a set of novel drug-like compounds that block the protein–protein interactions between α2β1 integrin and collagen. The obtained structure–activity relationship reveals the key features that are required for successful inhibition of this integrin–collagen interaction.
The role of the fibronectin synergy site in skin wound healing
2022
Upon skin barrier disruption, complex cellular and molecular events are activated to repair the damage and restore skin integrity. In adulthood, the outcome of this process can result in scarring and fibrosis, whereas complete tissue regeneration is observed in fetal wounds and wounds in lower vertebrates and invertebrates .Although there is abundant literature about the factors and mechanisms that determine the endpoint of either scarring/fibrosis or regeneration after tissue injury, the process is still poorly understood. After cutaneous injury, fibronectin (FN) is instantly released and deposited by cells, and represents a major ECM component in all stages of the wound healing process. F…
Echovirus 1 infectious entry via novel multivesicular bodies
2011
An arthritogenic alphavirus uses the α1β1 integrin collagen receptor
2005
Ross River (RR) virus is an alphavirus endemic to Australia and New Guinea and is the aetiological agent of epidemic polyarthritis or RR virus disease. Here we provide evidence that RR virus uses the collagen-binding alpha1beta1 integrin as a cellular receptor. Infection could be inhibited by collagen IV and antibodies specific for the beta1 and alpha1 integrin proteins, and fibroblasts from alpha1-integrin-/- mice were less efficiently infected than wild-type fibroblasts. Soluble alpha1beta1 integrin bound immobilized RR virus, and peptides representing the alpha1beta1 integrin binding-site on collagen IV inhibited virus binding to cells. We speculate that two highly conserved regions with…