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Integrins are transmembrane receptors that help cell-cell and cell-extracellular matrix (ECM) adhesion. Upon ligand binding, integrins activate signal transduction pathways that mediate cellular signals such as regulation of the cell cycle, organization of the intracellular cytoskeleton, and movement of new receptors to the cell membrane. The presence of integrins allows rapid and flexible responses to events at the cell surface (e.g. signal platelets to initiate an interaction with coagulation factors). Several types of integrins exist, and one cell generally has multiple different types on its surface. Integrins are found in all animals while integrin-like receptors are found in plant cells. Integrins work alongside other proteins such as cadherins, the immunoglobulin superfamily cell adhesion molecules, selectins and syndecans, to mediate cell–cell and cell–matrix interaction. Ligands for integrins include fibronectin, vitronectin, collagen and laminin.

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Fibronectin is a high-molecular weight (~500-~600 kDa) glycoprotein of the extracellular matrix that binds to membrane-spanning receptor proteins called integrins. It is approved for marketing as a t

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Ce cours décrit le fonctionnement du système immunitaire humain et les bases immunologiques de la vaccination, de la transplantation, de l'immunothérapie, et de l'allergie. Il présente aussi le rôle des cellules souches dans la formation des tissus, notamment la lignée hématopoïétique.

Selective integrin targeting with DNA-based nanomaterials

Eva Eugene Kurisinkal

Targeting cells specific to type and state remains a challenge in developing effective therapies, sensitive diagnostics, also robust and versatile tissue engineering. A promising strategy is to focuses on improving the inherent selectivity of the targeting system through precise orchestration of ligand-receptor interactions. Integrin receptors present themselves as a strategic target as their expression has been reported to be regulated across cell types and states. The principle of super-selectivity permits the selective targeting of integrin receptors above a threshold concentration in high valency and relative low affinity systems, leaving sparser counterparts unaffected. Here, we demonstrate that DNA based scaffolds with rigid ligand nanoscale spatial presentation can be designed to discriminate between adhesions by varying RGD ligand spacing targeting integrin âº5Î²1 receptors. We begin by modelling integrin âº5Î²1 receptors nearest neighbour distributions across HUVEC, CHO and HeLa cells. Targeting spacings in the sub-60nm reveal trends in binding efficacies based on cell type and activation state. An ensuing study of HUVEC response to local ligand geometries of varying global inter-geometry spacings presented on higher valency DNA scaffolds randomly immobilised result in two distinct adhesion cluster formations. Our findings open avenues in the design of super-selective targeting elements, besides providing insight on the regulation of integrin receptors on the cell surface across different cell types. Parameters for ligand presentation at the sub-adhesion scale affords selective cell engagement in biomaterial presentation.

EPFL2022

Integrin-Mediated Adhesion in the Unicellular Holozoan Capsaspora owczarzaki

Omaya Pierre Dudin

In animals, cell-matrix adhesions are essential for cell migration, tissue organization, and differentiation, which have central roles in embryonic development [1-6]. Integrins are the major cell surface adhesion receptors mediating cell-matrix adhesion in animals. They are heterodimeric transmembrane proteins that bind extracellular matrix (ECM) molecules on one side and connect to the actin cytoskeleton on the other [7]. Given the importance of integrin-mediated cell-matrix adhesion in development of multicellular animals, it is of interest to discover when and how this machinery arose during evolution. Comparative genomic analyses have shown that core components of the integrin adhesome pre-date the emergence of animals [8-11]; however, whether it mediates cell adhesion in non-metazoan taxa remains unknown. Here, we investigate cell-substrate adhesion in Capsaspora owczarzaki, the closest unicellular relative of animals with the most complete integrin adhesome [11, 12]. Previous work described that the life cycle of C. owczarzaki (hereafter, Capsaspora) includes three distinct life stages: adherent; cystic; and aggregative [13]. Using an adhesion assay, we show that, during the adherent life stage, C. owczarzaki adheres to surfaces using actin-dependent filopodia. We show that integrin b2 and its associated protein vinculin localize as distinct patches in the filopodia. We also demonstrate that substrate adhesion and integrin localization are enhanced by mammalian fibronectin. Finally, using a specific antibody for integrin b2, we inhibited cell adhesion to a fibronectin-coated surface. Our results suggest that adhesion to the substrate in C. owczarzaki is mediated by integrins. Wethus propose that integrin-mediated adhesion pre-dates the emergence of animals.

CELL PRESS2020

Engineering integrin signaling for promoting embryonic stem cell self-renewal in a precisely defined niche

Jeffrey Alan Hubbell, Jong Eun Ihm, Yun Suk Jo, Stephane Kontos, Seung Tae Lee, Mayumi Mochizuki Martino, Jungim Yun

We present development and use of a 3D synthetic extracellular matrix (ECM) analog with integrin- specific adhesion ligands to characterize the microenvironmental influences in embryonic stem cell (ESC) self-renewal. Transcriptional analysis of 24 integrin subunits followed by confirmation at the trans- lational and functional levels suggested that integrins a5b1, avb5, a6b1 and a9b1 play important roles in maintenance of stemness in undifferentiated mouse ESCs. Using the well-defined matrix as a tool to activate integrins a5b1 plus avb5, a6b1 and a9b1, individually and in combination, differential integrin activation was demonstrated to exert exquisite control over ESC fate decisions. Simultaneous ligation of these four integrin heterodimers promoted self-renewal, as evidence by prolonged SSEA-1, Oct4 and Nanog expression, and induced Akt1 kinase signaling along with translational regulation of other stemness-related genes. The biofunctional network we have designed based on this knowledge may be useful as a defined niche for regulating ESC pluripotency through selective cell–matrix interactions, and the method we present may be more generally useful for probing matrix interactions in stem cell self- renewal and differentiation.

Elsevier2010