Bibliografías temáticas / Integrin affinity

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Literatura académica sobre el tema "Integrin affinity"

Autor: Grafiati
Publicado: 11 de marzo de 2023

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Artículos de revistas sobre el tema "Integrin affinity"

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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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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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