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Titlebook: Integrin-Ligand Interaction; Johannes A. Eble,Klaus Kühn Book 1997 Springer Science+Business Media Dordrecht 1997 activation.cell.developm

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Integrins—A Versatile and Old Family of Cell Adhesion Moleculesanchoring molecules, but also play a role as receptors for extracellular matrix proteins, which transduce signals from the environment into the cell and trigger various cellular behaviors, such as cell spreading, migration and anchorage-dependent growth.. In the opposite way, called inside-out signa
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Activation States of Integrinshysiological and pathological conditions, resulting in a change in the adhesion properties of the cell. For example, cells in suspension can be induced to aggregate, or to attach to matrix proteins. Conversely, adherent cells may receive signals that induce them to detach and migrate on a matrix sub
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Integrins During Developmentan cultures or developing organisms. Explicit functions have been inferred from inhibition experiments with antibodies and peptides, translational blockade with antisense oligonucleotides, from analyses of naturally occurring mutations, and more recently, from truncations, mutations and deletions in the genes coding for selected proteins.
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Snake Venom Disintegrins and Disintegrin-Like Domains: Soluble Antagonists and Cellular Ligands of Ial cells other than platelets have been shown to bind disintegrins in adhesion-inhibition assays and these interactions may primarily involve integrins α.β. and α.β., known as the classical vitronectin and fibronectin receptors, respectively..
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Conformation-Dependent Recognition Sitesognition sites within laminin-1 for the integrins were mapped to distinct regions and domains using defined proteolytic laminin fragments or more recently, using fragments expressed recombinantly. The most detailed investigations were carried out with laminin-1 from the murine EHS tumor.
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