Integrin Regulation in Immunological and Cancerous Cells and Exosomes.
TLDR
In this article, integrins represent the biologically and medically significant family of cell adhesion molecules that govern a wide range of normal physiology and are dynamically controlled via activation-dependent conformational changes regulated by the balance of intracellular activators and inactivators, such as Shank-associated RH domain interactor (SHARPIN) and integrin cytoplasmic domain-associated protein 1 (ICAP-1).Abstract:
Integrins represent the biologically and medically significant family of cell adhesion molecules that govern a wide range of normal physiology. The activities of integrins in cells are dynamically controlled via activation-dependent conformational changes regulated by the balance of intracellular activators, such as talin and kindlin, and inactivators, such as Shank-associated RH domain interactor (SHARPIN) and integrin cytoplasmic domain-associated protein 1 (ICAP-1). The activities of integrins are alternatively controlled by homotypic lateral association with themselves to induce integrin clustering and/or by heterotypic lateral engagement with tetraspanin and syndecan in the same cells to modulate integrin adhesiveness. It has recently emerged that integrins are expressed not only in cells but also in exosomes, important entities of extracellular vesicles secreted from cells. Exosomal integrins have received considerable attention in recent years, and they are clearly involved in determining the tissue distribution of exosomes, forming premetastatic niches, supporting internalization of exosomes by target cells and mediating exosome-mediated transfer of the membrane proteins and associated kinases to target cells. A growing body of evidence shows that tumor and immune cell exosomes have the ability to alter endothelial characteristics (proliferation, migration) and gene expression, some of these effects being facilitated by vesicle-bound integrins. As endothelial metabolism is now thought to play a key role in tumor angiogenesis, we also discuss how tumor cells and their exosomes pleiotropically modulate endothelial functions in the tumor microenvironment.read more
Citations
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Possible Role of Extracellular Vesicles in Hepatotoxicity of Acetaminophen
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Role and correlation of exosomes and integrins in bone metastasis of prostate cancer
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Full-length αIIbβ3 CryoEM structure reveals intact integrin initiate-activation intrinsic architecture
TL;DR: In this article , the structure of integrin αIIbβ3 was resolved at 3Å resolution, revealing the overall topology of the heterodimer with the transmembrane (TM) helices and the head region ligand-binding domain tucked in a specific angle proximity to the TM region.
Posted ContentDOI
Full-length αIIbβ3 CryoEM structure reveals intact integrin initiate-activation intrinsic architecture
TL;DR: In this paper , the structure of the αIIbβ3 lower leg was resolved at 3Å resolution, revealing the overall topology of the heterodimer with the transmembrane (TM) helices and the head region ligand-binding domain tucked in a specific angle proximity to the TM region.
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Integrins and Epithelial-Mesenchymal Cooperation in the Tumor Microenvironment of Muscle-Invasive Lethal Cancers
TL;DR: It is hypothesized that a functional epithelial-mesenchymal cooperation (EMC) exists within the tumor invasive network to facilitate tumor escape from the primary organ, invasion and traversing of muscle, and navigation to metastatic sites.
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B lymphocytes secrete antigen-presenting vesicles.
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