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Journal articles on the topic 'Integrin affinity'

Author: Grafiati

Published: 11 March 2023

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1

Hughes, Paul E., and Martin Pfaff. "Integrin affinity modulation." Trends in Cell Biology 8, no. 9 (1998): 359–64. http://dx.doi.org/10.1016/s0962-8924(98)01339-7.

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2

Li, Jing, and Timothy A. Springer. "Energy landscape differences among integrins establish the framework for understanding activation." Journal of Cell Biology 217, no. 1 (2017): 397–412. http://dx.doi.org/10.1083/jcb.201701169.

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Why do integrins differ in basal activity, and how does affinity for soluble ligand correlate with cellular adhesiveness? We show that basal conformational equilibrium set points for integrin α4β1 are cell type specific and differ from integrin α5β1 when the two integrins are coexpressed on the same cell. Although α4β1 is easier to activate, its high-affinity state binds vascular cell adhesion molecule and fibronectin 100- to 1,000-fold more weakly than α5β1 binds fibronectin. Furthermore, the difference in affinity between the high- and low-affinity states is more compressed in α4β1 (600- to

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3

Liddington, R. C., and M. H. Ginsberg. "Integrin activation takes shape." Journal of Cell Biology 158, no. 5 (2002): 833–39. http://dx.doi.org/10.1083/jcb.200206011.

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Integrins are cell surface adhesion receptors that are essential for the development and function of multicellular animals. Here we summarize recent findings on the regulation of integrin affinity for ligand (activation), one mechanism by which cells modulate integrin function. The focus is on the structural basis of integrin activation, the role of the cytoplasmic domain in integrin affinity regulation, and potential mechanisms by which activation signals are propagated from integrin cytoplasmic domains to the extracellular ligand-binding domain.

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Dormond, Olivier, Lionel Ponsonnet, Meriem Hasmim, Alessandro Foletti та Curzio Rüegg. "Manganese-induced integrin affinity maturation promotes recruitment of αVβ3 integrin to focal adhesions in endothelial cells: evidence for a role of phosphatidylinositol 3-kinase and Src". Thrombosis and Haemostasis 92, № 07 (2004): 151–61. http://dx.doi.org/10.1160/th03-11-0728.

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SummaryIntegrin activity is controlled by changes in affinity (i.e. ligand binding) and avidity (i.e. receptor clustering). Little is known, however, about the effect of affinity maturation on integrin avidity and on the associated signaling pathways. To study the effect of affinity maturation on integrin avidity, we stimulated human umbilical vein endothelial cells (HUVEC) with MnCl2 to increase integrin affinity and monitored clustering of β1 and β3 integrins. In unstimulated HUVEC, β1 integrins were present in fibrillar adhesions, while αVβ3 was detected in peripheral focal adhesions. Clust

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Yu, Tao, Xing Wu, Kiran B. Gupta та Dennis F. Kucik. "Affinity, lateral mobility, and clustering contribute independently to β2-integrin-mediated adhesion". American Journal of Physiology-Cell Physiology 299, № 2 (2010): C399—C410. http://dx.doi.org/10.1152/ajpcell.00039.2009.

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Affinity changes and avidity modulation both contribute to activation of β2-integrin-mediated adhesion, an essential, early step in inflammation. Avidity modulation, defined as an increase in adhesiveness independent of integrin conformational changes, might be due to integrin clustering, motion, or both. Increased integrin diffusion upon leukocyte activation has been demonstrated, but whether it is proadhesive in itself, or just constitutes a mechanism for integrin clustering, remains unclear. To understand the proadhesive effects of integrin affinity changes, clustering, and motion, an exper

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Helsten, Teresa L., Thomas A. Bunch, Hisashi Kato, et al. "Differences in Regulation ofDrosophilaand Vertebrate Integrin Affinity by Talin." Molecular Biology of the Cell 19, no. 8 (2008): 3589–98. http://dx.doi.org/10.1091/mbc.e08-01-0085.

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Integrin-mediated cell adhesion is essential for development of multicellular organisms. In worms, flies, and vertebrates, talin forms a physical link between integrin cytoplasmic domains and the actin cytoskeleton. Loss of either integrins or talin leads to similar phenotypes. In vertebrates, talin is also a key regulator of integrin affinity. We used a ligand-mimetic Fab fragment, TWOW-1, to assess talin's role in regulating Drosophila αPS2βPS affinity. Depletion of cellular metabolic energy reduced TWOW-1 binding, suggesting αPS2βPS affinity is an active process as it is for vertebrate inte

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Tozer, Eileen Collins, Paul E. Hughes, and Joseph C. Loftus. "Ligand binding and affinity modulation of integrins." Biochemistry and Cell Biology 74, no. 6 (1996): 785–98. http://dx.doi.org/10.1139/o96-085.

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Integrins are cell adhesion receptors that mediate cell–cell and cell–extracellular matrix interactions. The extracellular domains of these receptors possess binding sites for a diverse range of protein ligands. Ligand binding is divalent cation dependent and involves well-defined motifs in the ligand. Integrins can dynamically regulate their affinity for ligands (inside-out signaling). This ability to rapidly modulate their affinity state is key to their involvement in such processes as cell migration and platelet aggregation. This review will focus on two aspects of integrin function: first,

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Dong, Xianchi, Bo Zhao, Fu-Yang Lin, Chafen Lu, Bruce N. Rogers та Timothy A. Springer. "High integrin αVβ6 affinity reached by hybrid domain deletion slows ligand-binding on-rate". Proceedings of the National Academy of Sciences 115, № 7 (2018): E1429—E1436. http://dx.doi.org/10.1073/pnas.1718662115.

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The role of the hybrid domain in integrin affinity regulation is unknown, as is whether the kinetics of ligand binding is modulated by integrin affinity state. Here, we compare cell surface and soluble integrin αVβ6 truncation mutants for ligand-binding affinity, kinetics, and thermodynamics. Removal of the integrin transmembrane/cytoplasmic domains or lower legs has little effect on αVβ6 affinity, in contrast to β1 integrins. In integrin opening, rearrangement at the interface between the βI and hybrid domains is linked to remodeling at the ligand-binding site at the opposite end of the βI do

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Bialkowska, Katarzyna, Jun Qin, and Edward F. Plow. "Phosphorylation of Kindlins and the Control of Integrin Function." Cells 10, no. 4 (2021): 825. http://dx.doi.org/10.3390/cells10040825.

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Integrins serve as conduits for the transmission of information between cells and their extracellular environment. Signaling across integrins is bidirectional, transducing both inside-out and outside-signaling. Integrin activation, a transition from a low affinity/avidity state to a high affinity/avidity state for cognate ligands, is an outcome of inside-signaling. Such activation is particularly important for the recognition of soluble ligands by blood cells but also influences cell-cell and cell-matrix interactions. Integrin activation depends on a complex series of interactions, which both

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Mahabeleshwar, Ganapati H., Juhua Chen, Weiyi Feng, Payaningal R. Somanath, Olga V. Razorenova, and Tatiana V. Byzova. "Integrin affinity modulation in angiogenesis." Cell Cycle 7, no. 3 (2008): 335–47. http://dx.doi.org/10.4161/cc.7.3.5234.

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11

Sun, Guangyu, Emilie Guillon, and Scott A. Holley. "Integrin intra-heterodimer affinity inversely correlates with integrin activatability." Cell Reports 35, no. 10 (2021): 109230. http://dx.doi.org/10.1016/j.celrep.2021.109230.

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12

Woodside, D. G., S. Liu, and M. H. Ginsberg. "Integrin Activation." Thrombosis and Haemostasis 86, no. 07 (2001): 316–23. http://dx.doi.org/10.1055/s-0037-1616229.

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SummaryIntegrins are cell surface adhesion receptors that participate in a variety of important processes throughout the vasculature. Here we summarize some recent findings on the regulation of integrin mediated cellular adhesion. Particular emphasis is placed on the regulation of integrin affinity for ligand (activation), although this is just one mechanism by which regulation of integrin-dependent cell adhesion can occur. Also discussed are recent observations on the structural basis of integrin activation, the role of the cytoplasmic domain in integrin affinity regulation, and potential mec

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Kinashi, Tatsuo, Tetsuo Asaoka, Ruri Setoguchi, and Kiyoshi Takatsu. "Affinity Modulation of Very Late Antigen-5 Through Phosphatidylinositol 3-Kinase in Mast Cells." Journal of Immunology 162, no. 5 (1999): 2850–57. http://dx.doi.org/10.4049/jimmunol.162.5.2850.

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Abstract Adhesiveness of integrins is up-regulated rapidly by a number of molecules, including growth factors, cytokines, chemokines, and other cell surface receptors, through a mechanism termed inside-out signaling. The inside-out signaling pathways are thought to alter integrin affinity for ligand, or cell surface distribution of integrin by diffusion/clustering. However, it remains to be clarified whether any physiologically relevant agonists induce a rapid change in the affinity of β1 integrins and how ligand-binding affinity is modulated upon stimulation. In this study, we reported that a

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Pinon, Perrine, Jenita Pärssinen, Patricia Vazquez, et al. "Talin-bound NPLY motif recruits integrin-signaling adapters to regulate cell spreading and mechanosensing." Journal of Cell Biology 205, no. 2 (2014): 265–81. http://dx.doi.org/10.1083/jcb.201308136.

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Integrin-dependent cell adhesion and spreading are critical for morphogenesis, tissue regeneration, and immune defense but also tumor growth. However, the mechanisms that induce integrin-mediated cell spreading and provide mechanosensing on different extracellular matrix conditions are not fully understood. By expressing β3-GFP-integrins with enhanced talin-binding affinity, we experimentally uncoupled integrin activation, clustering, and substrate binding from its function in cell spreading. Mutational analysis revealed Tyr747, located in the first cytoplasmic NPLY747 motif, to induce spreadi

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Sethi, Tariq, Mark H. Ginsberg, Julian Downward, and Paul E. Hughes. "The Small GTP-binding Protein R-Ras Can Influence Integrin Activation by Antagonizing a Ras/Raf-initiated Integrin Suppression Pathway." Molecular Biology of the Cell 10, no. 6 (1999): 1799–809. http://dx.doi.org/10.1091/mbc.10.6.1799.

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The rapid modulation of ligand-binding affinity (“activation”) is a central property of the integrin family of cell adhesion receptors. The small GTP-binding protein Ras and its downstream effector kinase Raf-1 suppress integrin activation. In this study we explored the relationship between Ras and the closely related small GTP-binding protein R-Ras in modulating the integrin affinity state. We found that R-Ras does not seem to be a direct activator of integrins in Chinese hamster ovary cells. However, we observed that GTP-bound R-Ras strongly antagonizes the Ras/Raf-initiated integrin suppres

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Huttenlocher, A., M. H. Ginsberg, and A. F. Horwitz. "Modulation of cell migration by integrin-mediated cytoskeletal linkages and ligand-binding affinity." Journal of Cell Biology 134, no. 6 (1996): 1551–62. http://dx.doi.org/10.1083/jcb.134.6.1551.

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Integrin cell surface adhesion receptors play a central role in mediating cell migration. We have developed a model system consisting of CHO cells ectopically expressing the alpha IIb beta 3 integrin to study integrin affinity and cytoskeletal interactions during cell migration. The alpha IIb beta 3 integrins are suited for study of integrin receptors during cell migration because they are well characterized with respect to ligand binding, cytoskeletal interactions, and signal transduction, and mutants with altered receptor function are available. The alpha IIb beta 3 receptor specifically med

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17

Martin-Bermudo, Maria D., Olga M. Dunin-Borkowski, and Nicholas H. Brown. "Modulation of Integrin Activity is Vital for Morphogenesis." Journal of Cell Biology 141, no. 4 (1998): 1073–81. http://dx.doi.org/10.1083/jcb.141.4.1073.

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Cells can vary their adhesive properties by modulating the affinity of integrin receptors. The activation and inactivation of integrins by inside-out mechanisms acting on the cytoplasmic domains of the integrin subunits has been demonstrated in platelets, lymphocytes, and keratinocytes. We show that in the embryo, normal morphogenesis requires the α subunit cytoplasmic domain to control integrin adhesion at the right times and places. PS2 integrin (αPS2βPS) adhesion is normally restricted to the muscle termini, where it is required for attaching the muscles to the ends of other muscles and to

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18

Kim, Chungho, Tong-Lay Lau, Tobias S. Ulmer та Mark H. Ginsberg. "Interactions of platelet integrin αΙΙb and β3 transmembrane domains in mammalian cell membranes and their role in integrin activation". Blood 113, № 19 (2009): 4747–53. http://dx.doi.org/10.1182/blood-2008-10-186551.

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Abstract Clustering and occupancy of platelet integrin αIIbβ3 (GPIIb-IIIa) generate biologically important signals: conversely, intracellular signals increase the integrins' affinity, leading to integrin activation; both forms of integrin signaling play important roles in hemostasis and thrombosis. Indirect evidence implicates interactions between integrin α and β transmembrane domains (TMDs) and cytoplasmic domains in integrin signaling; however, efforts to directly identify these associations have met with varying and controversial results. In this study, we develop mini-integrin affinity ca

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Palecek, S. P., A. Huttenlocher, A. F. Horwitz, and D. A. Lauffenburger. "Physical and biochemical regulation of integrin release during rear detachment of migrating cells." Journal of Cell Science 111, no. 7 (1998): 929–40. http://dx.doi.org/10.1242/jcs.111.7.929.

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Cell migration can be considered as a repeated cycle of membrane protrusion and attachment, cytoskeletal contraction and rear detachment. At intermediate and high levels of cell-substratum adhesiveness, cell speed appears to be rate-limited by rear detachment, specifically by the disruption of cytoskeleton-adhesion receptor-extracellular matrix (ECM) linkages. Often, cytoskeletal linkages fracture to release integrin adhesion receptors from the cell. Cell-extracellular matrix bonds may also dissociate, allowing the integrins to remain with the cell. To investigate molecular mechanisms involved

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Fan, Zhichao, Sara McArdle, Zbigniew Mikulski та ін. "Neutrophil recruitment limited by high affinity bent β2 integrin binding ligand in cis". Journal of Immunology 196, № 1_Supplement (2016): 119.5. http://dx.doi.org/10.4049/jimmunol.196.supp.119.5.

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Abstract Neutrophils are essential in innate immunity and inflammation. Many neutrophil functions are β2 integrin-dependent. Integrins can extend (E+) and acquire a high affinity conformation with an “open” headpiece (H+). The canonical switchblade model of integrin activation proposes that the E+ conformation precedes H+, and the two are believed to be structurally linked. Here, by using high-resolution quantitative dynamic foot printing (qDF) microscopy combined with a homogenous conformation-reporter binding assay in a microfluidic device, we show that a substantial fraction of β2 integrins

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Kolasangiani, Reza, Tamara C. Bidone, and Martin A. Schwartz. "Integrin Conformational Dynamics and Mechanotransduction." Cells 11, no. 22 (2022): 3584. http://dx.doi.org/10.3390/cells11223584.

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The function of the integrin family of receptors as central mediators of cell-extracellular matrix (ECM) and cell–cell adhesion requires a remarkable convergence of interactions and influences. Integrins must be anchored to the cytoskeleton and bound to extracellular ligands in order to provide firm adhesion, with force transmission across this linkage conferring tissue integrity. Integrin affinity to ligands is highly regulated by cell signaling pathways, altering affinity constants by 1000-fold or more, via a series of long-range conformational transitions. In this review, we first summarize

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Wen, Lai, Alex Marki, Zhihao Wang та ін. "A new β2 integrin activation reporter mouse reveals localized intra- and extra-vascular neutrophil integrin activation in vivo". Journal of Immunology 208, № 1_Supplement (2022): 105.07. http://dx.doi.org/10.4049/jimmunol.208.supp.105.07.

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Abstract β2 integrins (LFA-1, Mac-1, CD11c-CD18, and CD11d-CD18) are leukocyte-specific adhesion receptors that play critical roles in leukocyte recruitment, as well as other immunological processes such as phagocytosis and immunological synapse formation. Adhesion of leukocytes to other cells such as endothelial cells are regulated by integrin affinity changes for their ligands (“activation”). Human β2 integrin activation can be detected by reporter antibodies including mAb24 and KIM127. No such activation epitopes are known in mouse β2 integrins. Because of the lack of mouse β2 integrin acti

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Hyduk, Sharon J., Jiwon Oh, Haiyan Xiao, Mian Chen та Myron I. Cybulsky. "Paxillin selectively associates with constitutive and chemoattractant-induced high-affinity α4β1 integrins: implications for integrin signaling". Blood 104, № 9 (2004): 2818–24. http://dx.doi.org/10.1182/blood-2003-12-4402.

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Abstract Leukocyte α4β1 integrins regulate hematopoietic and lymphoid development, as well as the emigration of circulating cells to sites of inflammation. Because vascular cell adhesion molecule-1 (VCAM-1) binding to high-affinity α4β1 is stable, these integrins can be detected and selectively precipitated from cell lysates using VCAM-1/Fc. With this approach, high-affinity α4β1 integrin expression was demonstrated on lymphocytes in the bone marrow, thymus, spleen, and the peritoneal cavity of normal mice, but not in peripheral lymph nodes. Immature lymphocytes preferentially expressed high-a

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Yue, Jiao, YouDong Pan, LiFang Sun та ін. "The Unique Disulfide Bond-stabilized W1 β4-β1 Loop in the α4 β-Propeller Domain Regulates Integrin α4β7 Affinity and Signaling". Journal of Biological Chemistry 288, № 20 (2013): 14228–37. http://dx.doi.org/10.1074/jbc.m113.462630.

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Integrin α4β7 mediates rolling and firm adhesion of lymphocytes pre- and post-activation, which is distinct from most integrins only mediating firm cell adhesion upon activation. This two-phase cell adhesion suggests a unique molecular basis for the dynamic interaction of α4β7 with its ligand, mucosal addressin cell adhesion molecule 1 (MAdCAM-1). Here we report that a disulfide bond-stabilized W1 β4-β1 loop in α4 β-propeller domain plays critical roles in regulating integrin α4β7 affinity and signaling. Either breaking the disulfide bond or deleting the disulfide bond-occluded segment in the

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Jovanović, Jelena, Sarah Iqbal, Sacha Jensen, Helen Mardon, and Penny Handford. "Fibrillin–integrin interactions in health and disease." Biochemical Society Transactions 36, no. 2 (2008): 257–62. http://dx.doi.org/10.1042/bst0360257.

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Human fibrillin-1 is the major structural protein of extracellular matrix 10–12 nm microfibrils. It has a disulfide-rich modular organization which consists primarily of cbEGF (Ca2+-binding epidermal growth factor-like) domains and TB (transforming growth factor β-binding protein-like) domains. TB4 contains an RGD (Arg-Gly-Asp) integrin-binding motif. The atomic structure of this region has been solved by X-ray crystallography and shows the TB4 and flanking cbEGF domains to be arranged as a tetragonal pyramid with N- and C-termini exposed at opposite ends of the fragment. The RGD integrin-bind

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Fan, Zhichao, Lai Wen, Yi-Ting Yeh та ін. "Kindlin-3 organizes a ring of clustered high affinity β2 integrins during human neutrophil spreading under flow". Journal of Immunology 204, № 1_Supplement (2020): 220.1. http://dx.doi.org/10.4049/jimmunol.204.supp.220.1.

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Abstract Neutrophils are vital for inflammation and immune defense. Dependent on β2 integrins, spherical neutrophils spread on vascular endothelium after arrest, which is critical for their recruitment from circulation to resist high shear flow and to initiate intravascular crawling. Here, we use high-resolution quantitative dynamic footprinting microscopy to monitor neutrophil spreading on a substrate of recombinant ICAM-1 and P-selectin under flow. A homogenous binding assay using the conformation-reporter antibodies mAb24 (reporting high-affinity β2, H+) and KIM127 (reporting extended β2, E

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D’Souza-Schorey, Crislyn, Benjamin Boettner, and Linda Van Aelst. "Rac Regulates Integrin-Mediated Spreading and Increased Adhesion of T Lymphocytes." Molecular and Cellular Biology 18, no. 7 (1998): 3936–46. http://dx.doi.org/10.1128/mcb.18.7.3936.

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ABSTRACT Leukocyte adhesion to the extracellular matrix (ECM) is tightly controlled and is vital for the immune response. Circulating lymphocytes leave the bloodstream and adhere to ECM components at sites of inflammation and lymphoid tissues. Mechanisms for regulating T-lymphocyte–ECM adhesion include (i) an alteration in the affinity of cell surface integrin receptors for their extracellular ligands and (ii) an alteration of events following postreceptor occupancy (e.g., cell spreading). Whereas H-Ras and R-Ras were previously shown to affect T-cell adhesion by altering the affinity state of

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O'Toole, TE, Y. Katagiri, RJ Faull, et al. "Integrin cytoplasmic domains mediate inside-out signal transduction." Journal of Cell Biology 124, no. 6 (1994): 1047–59. http://dx.doi.org/10.1083/jcb.124.6.1047.

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We analyzed the binding of fibronectin to integrin alpha 5 beta 1 in various cells; in some cells fibronectin bound with low affinity (e.g., K562 cells) whereas in others (e.g., CHO), it bound with high affinity (Kd approximately 100 nM) in an energy-dependent manner. We constructed chimeras of the extracellular and transmembrane domains of alpha IIb beta 3 joined to the cytoplasmic domains of alpha 5 beta 1. The affinity state of these chimeras was assessed by binding of fibrinogen or the monoclonal antibody, PAC1. The cytoplasmic domains of alpha 5 beta 1 conferred an energy-dependent high a

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29

Schürpf, Thomas, and Timothy A. Springer. "Regulation of integrin affinity on cell surfaces." EMBO Journal 30, no. 23 (2011): 4712–27. http://dx.doi.org/10.1038/emboj.2011.333.

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30

Karsan, A. "Notch and Integrin Affinity: A Sticky Situation." Science Signaling 1, no. 2 (2008): pe2. http://dx.doi.org/10.1126/stke.12pe2.

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Rose, David M., Valentin Grabovsky, Ronen Alon та Mark H. Ginsberg. "The Affinity of Integrin α4β1Governs Lymphocyte Migration". Journal of Immunology 167, № 5 (2001): 2824–30. http://dx.doi.org/10.4049/jimmunol.167.5.2824.

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Brown, Simon B., and Ian Dransfield. "Electric Fields and Inflammation: May the Force be with You." Scientific World JOURNAL 8 (2008): 1280–94. http://dx.doi.org/10.1100/tsw.2008.158.

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Integrins are a family of ubiquitous cell surface receptors comprising heterodimers of β and α chains that are required for cell adhesion and motility. Integrin-dependent adhesion and signaling is associated with major conformational changes in the ectodomain as it shifts from a low-affinity “bent” to a high-affinity “extended” structure. The ability of a cell to regulate dynamically the affinity or activation state of an integrin, and hence its binding to extracellular matrix or cell adhesion molecules, is assumed to be driven by intracellular signaling events transmitted by protein binding t

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Hyduk, Sharon J., Haiyan Xiao та Myron I. Cybulsky. "PAXILLIN SELECTIVELY ASSOCIATES WITH HIGH AFFINITY α4β1 INTEGRINS: IMPLICATIONS FOR INTEGRIN SIGNALING". Cardiovascular Pathology 13, № 3 (2004): 6. http://dx.doi.org/10.1016/j.carpath.2004.03.012.

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Craig, David H., Christopher P. Gayer, Keri L. Schaubert та ін. "Increased extracellular pressure enhances cancer cell integrin-binding affinity through phosphorylation of β1-integrin at threonine 788/789". American Journal of Physiology-Cell Physiology 296, № 1 (2009): C193—C204. http://dx.doi.org/10.1152/ajpcell.00355.2008.

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Increased extracellular pressure stimulates β1-integrin-dependent cancer cell adhesion. We asked whether pressure-induced adhesion is mediated by changes in β1-integrin binding affinity or avidity and whether these changes are phosphorylation dependent. We evaluated integrin affinity and clustering in human SW620 colon cancer cells by measuring differences in binding between soluble Arg-Gly-Asp (RGD)-Fc ligands and RGD-Fc-F(ab′)2 multimeric complexes under ambient and 15-mmHg increased pressures. Phosphorylation of β1-integrin S785 and T788/9 residues in SW620 and primary malignant colonocytes

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Legler, D. F., G. Wiedle, F. P. Ross та B. A. Imhof. "Superactivation of integrin (α)v(β)3 by low antagonist concentrations". Journal of Cell Science 114, № 8 (2001): 1545–53. http://dx.doi.org/10.1242/jcs.114.8.1545.

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Integrins are implicated in cell adhesion, migration and homeostasis. An important feature is their ability to adopt different affinity states that can be regulated by a variety of intra- and extracellular factors. To study affinity modulation of the integrin ectodomain by extracellular factors, we produced a soluble recombinant form of mouse integrin (α)v(β)3 in a mammalian expression system and isolated it to purity. We show that the two transmembrane truncated integrin subunits stably associate to form a functional receptor, soluble recombinant (α)v(β)3. The affinity of this receptor for it

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Fagerholm, Susanna C., Tiina J. Hilden, Susanna M. Nurmi та Carl G. Gahmberg. "Specific integrin α and β chain phosphorylations regulate LFA-1 activation through affinity-dependent and -independent mechanisms". Journal of Cell Biology 171, № 4 (2005): 705–15. http://dx.doi.org/10.1083/jcb.200504016.

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Integrins are adhesion receptors that are crucial to the functions of multicellular organisms. Integrin-mediated adhesion is a complex process that involves both affinity regulation and cytoskeletal coupling, but the molecular mechanisms behind this process have remained incompletely understood. In this study, we report that the phosphorylation of each cytoplasmic domain of the leukocyte function-associated antigen-1 integrin mediates different modes of integrin activation. α Chain phosphorylation on Ser1140 is needed for conformational changes in the integrin after chemokine- or integrin liga

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PICCARDONI, Paola, Stefano MANARINI, Lorenzo FEDERICO, et al. "SRC-dependent outside-in signalling is a key step in the process of autoregulation of beta2 integrins in polymorphonuclear cells." Biochemical Journal 380, no. 1 (2004): 57–65. http://dx.doi.org/10.1042/bj20040151.

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In human PMN (polymorphonuclear cells), challenged by P-selectin, the β2-integrin Mac-1 (macrophage antigen-1) promoted the activation of the SRC (cellular homologue of Rous sarcoma virus oncogenic protein) family members HCK (haematopoietic cell kinase) and LYN (an SRC family protein tyrosine kinase) and phosphorylation of a P-110 (110 kDa protein). SRC kinase activity in turn was necessary for macrophage antigen-1-mediated adhesion [Piccardoni, Sideri, Manarini, Piccoli, Martelli, de Gaetano, Cerletti and Evangelista (2001) Blood 98, 108–116]. This suggested that an SRC-dependent outside-in

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Nieswandt, Bernhard, Markus Moser, Irina Pleines, et al. "Loss of talin1 in platelets abrogates integrin activation, platelet aggregation, and thrombus formation in vitro and in vivo." Journal of Experimental Medicine 204, no. 13 (2007): 3113–18. http://dx.doi.org/10.1084/jem.20071827.

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Platelet adhesion and aggregation at sites of vascular injury are essential for normal hemostasis but may also lead to pathological thrombus formation, causing diseases such as myocardial infarction or stroke. Heterodimeric receptors of the integrin family play a central role in the adhesion and aggregation of platelets. In resting platelets, integrins exhibit a low affinity state for their ligands, and they shift to a high affinity state at sites of vascular injury. It has been proposed that direct binding of the cytoskeletal protein talin1 to the cytoplasmic domain of the integrin β subunits

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Hadari, Y. R., R. Arbel-Goren, Y. Levy, et al. "Galectin-8 binding to integrins inhibits cell adhesion and induces apoptosis." Journal of Cell Science 113, no. 13 (2000): 2385–97. http://dx.doi.org/10.1242/jcs.113.13.2385.

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The interaction of cells with the extracellular matrix regulates cell adhesion, motility, growth, survival and differentiation through integrin-mediated signal transduction. Here we demonstrate that galectin-8, a secreted mammalian (beta)-galactoside binding protein, inhibits adhesion of human carcinoma (1299) cells to plates coated with integrin ligands, and induces cell apoptosis. Pretreatment of the cells with Mn(2+), which increases the affinity of integrins for their ligands, abolished the inhibitory effects of galectin-8. The inhibitory effects of galectin-8 were specific and were not mi

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Vasconcelos, Disraeli, Beatriz Chaves, Aline Albuquerque та ін. "Development of New Potential Inhibitors of β1 Integrins through In Silico Methods—Screening and Computational Validation". Life 12, № 7 (2022): 932. http://dx.doi.org/10.3390/life12070932.

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Integrins are transmembrane receptors that play a critical role in many biological processes which can be therapeutically modulated using integrin blockers, such as peptidomimetic ligands. This work aimed to develop new potential β1 integrin antagonists using modeled receptors based on the aligned crystallographic structures and docked with three lead compounds (BIO1211, BIO5192, and TCS2314), widely known as α4β1 antagonists. Lead-compound complex optimization was performed by keeping intact the carboxylate moiety of the ligand, adding substituents in two other regions of the molecule to incr

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Laudanna, Carlo, and Ronen Alon. "Right on the spot." Thrombosis and Haemostasis 95, no. 01 (2006): 5–11. http://dx.doi.org/10.1160/th05-07-0482.

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SummaryThe arrest of rolling leukocytes on various target vascular beds is crucial for their recruitment at inflammatory sites and secondary lymphoid tissues. Leukocyte arrest is predominantly mediated by integrins interacting with either constitutive or inducible endothelial ligands. Integrins are cytoskeletally regulated heterodimers maintained in largely low affinity conformational states on circulating leukocytes. For arrest to occur, the affinity of integrin heterodimers must be enhanced in situ upon leukocyte encounter with proper endothelial-displayed chemokines or chemoattractants whic

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Asokan, Aravind, Julie B. Hamra, Lakshmanan Govindasamy, Mavis Agbandje-McKenna та Richard J. Samulski. "Adeno-Associated Virus Type 2 Contains an Integrin α5β1 Binding Domain Essential for Viral Cell Entry". Journal of Virology 80, № 18 (2006): 8961–69. http://dx.doi.org/10.1128/jvi.00843-06.

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ABSTRACT Integrins have been implicated as coreceptors in the infectious pathways of several nonenveloped viruses. For example, adenoviruses are known to interact with αV integrins by virtue of a high-affinity arginine-glycine-aspartate (RGD) domain present in the penton bases of the capsids. In the case of adeno-associated virus type 2 (AAV2), which lacks this RGD motif, integrin αVβ5 has been identified as a coreceptor for cellular entry. However, the molecular determinants of AAV2 capsid-integrin interactions and the potential exploitation of alternative integrins as coreceptors by AAV2 hav

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Ye, Feng, Guiqing Hu, Dianne Taylor, et al. "Recreation of the terminal events in physiological integrin activation." Journal of Cell Biology 188, no. 1 (2010): 157–73. http://dx.doi.org/10.1083/jcb.200908045.

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Increased affinity of integrins for the extracellular matrix (activation) regulates cell adhesion and migration, extracellular matrix assembly, and mechanotransduction. Major uncertainties concern the sufficiency of talin for activation, whether conformational change without clustering leads to activation, and whether mechanical force is required for molecular extension. Here, we reconstructed physiological integrin activation in vitro and used cellular, biochemical, biophysical, and ultrastructural analyses to show that talin binding is sufficient to activate integrin αIIbβ3. Furthermore, we

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Otey, C. A., F. M. Pavalko, and K. Burridge. "An interaction between alpha-actinin and the beta 1 integrin subunit in vitro." Journal of Cell Biology 111, no. 2 (1990): 721–29. http://dx.doi.org/10.1083/jcb.111.2.721.

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A number of cytoskeletal-associated proteins that are concentrated in focal contacts, namely alpha-actinin, vinculin, talin, and integrin, have been shown to interact in vitro such that they suggest a potential link between actin filaments and the membrane. Because some of these interactions are of low affinity, we suspect the additional linkages also exist. Therefore, we have used a synthetic peptide corresponding to the cytoplasmic domain of beta 1 integrin and affinity chromatography to identify additional integrin-binding proteins. Here we report our finding of an interaction between the c

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Isberg, R. R., and P. Barnes. "Subversion of integrins by enteropathogenic Yersinia." Journal of Cell Science 114, no. 1 (2001): 21–28. http://dx.doi.org/10.1242/jcs.114.1.21.

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Enteropathogenic Yersinia are gram-negative bacterial species that translocate from the lumen of the intestine and are able to grow within deep tissue sites. During the earliest stages of disease, the organism is able to bind integrin receptors that are presented on the apical surface of M cells in the intestine, which allows its internalization and subsequent translocation into regional lymph nodes. The primary integrin substrate is the outer-membrane protein invasin, which binds with extraordinarily high affinity to at least five different integrins that have the (beta)(1) chain. Bacterial u

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De Mets, Richard, Irene Wang, Martial Balland та ін. "Cellular tension encodes local Src-dependent differential β1 and β3 integrin mobility". Molecular Biology of the Cell 30, № 2 (2019): 181–90. http://dx.doi.org/10.1091/mbc.e18-04-0253.

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Integrins are transmembrane receptors that have a pivotal role in mechanotransduction processes by connecting the extracellular matrix to the cytoskeleton. Although it is well established that integrin activation/inhibition cycles are due to highly dynamic interactions, whether integrin mobility depends on local tension and cytoskeletal organization remains surprisingly unclear. Using an original approach combining micropatterning on glass substrates to induce standardized local mechanical constraints within a single cell with temporal image correlation spectroscopy, we measured the mechanosen

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Peter, K., and T. E. O'Toole. "Modulation of cell adhesion by changes in alpha L beta 2 (LFA-1, CD11a/CD18) cytoplasmic domain/cytoskeleton interaction." Journal of Experimental Medicine 181, no. 1 (1995): 315–26. http://dx.doi.org/10.1084/jem.181.1.315.

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The integrin alpha L beta 2 (leukocyte function-associated molecule 1, CD11a/CD18) mediates activation-dependent adhesion of leukocytes. The cytoplasmic domains of alpha L beta 2 have been demonstrated to modulate adhesiveness of alpha L beta 2. Affinity changes of alpha L beta 2 for its ligand or postreceptor events can be responsible for this modulation of adhesiveness. To investigate the possible role of the alpha L beta 2 cytoplasmic domains in postreceptor events we constructed cDNA encoding chimeric proteins with intracellular alpha L beta 2 domains, which are responsible for alpha L bet

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Pasvolsky, Ronit, Sara W. Feigelson, Sara Sebnem Kilic, et al. "A LAD-III syndrome is associated with defective expression of the Rap-1 activator CalDAG-GEFI in lymphocytes, neutrophils, and platelets." Journal of Experimental Medicine 204, no. 7 (2007): 1571–82. http://dx.doi.org/10.1084/jem.20070058.

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Leukocyte and platelet integrins rapidly alter their affinity and adhesiveness in response to various activation (inside-out) signals. A rare leukocyte adhesion deficiency (LAD), LAD-III, is associated with severe defects in leukocyte and platelet integrin activation. We report two new LAD cases in which lymphocytes, neutrophils, and platelets share severe defects in β1, β2, and β3 integrin activation. Patients were both homozygous for a splice junction mutation in their CalDAG-GEFI gene, which is a key Rap-1/2 guanine exchange factor (GEF). Both mRNA and protein levels of the GEF were diminis

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Dogic, D., P. Rousselle, and M. Aumailley. "Cell adhesion to laminin 1 or 5 induces isoform-specific clustering of integrins and other focal adhesion components." Journal of Cell Science 111, no. 6 (1998): 793–802. http://dx.doi.org/10.1242/jcs.111.6.793.

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Laminin 1 (alpha1beta1gamma1) and laminin 5 (alpha3beta3gamma2) induce cell adhesion with different involvement of integrins: both are ligands for the alpha6beta1 integrin, while alpha3beta1 integrin has affinity for laminin 5 only. These two laminin isoforms therefore provide good models to investigate whether alpha3beta1 and alpha6beta1 integrins play different roles in signal transduction and in focal adhesion formation. Laminin 1 or 5 induced adhesion of normal human skin fibroblasts to a similar extent but promoted different overall cell shapes. On laminin 1 the fibroblasts formed mainly

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Haling, Jacob R., Susan J. Monkley, David R. Critchley, and Brian G. Petrich. "Talin-dependent integrin activation is required for fibrin clot retraction by platelets." Blood 117, no. 5 (2011): 1719–22. http://dx.doi.org/10.1182/blood-2010-09-305433.

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Abstract Talin functions both as a regulator of integrin affinity and as an important mechanical link between integrins and the cytoskeleton. Using genetic deletion of talin, we show for the first time that the capacity of talin to activate integrins is required for fibrin clot retraction by platelets. To further dissect which talin functions are required for this process, we tested clot retraction in platelets expressing a talin1(L325R) mutant that binds to integrins, but exhibits impaired integrin activation ascribable to disruption of the interaction between talin and the membrane-proximal

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