Showing papers by "Jean E. Schwarzbauer published in 2010"
TL;DR: The major steps, molecular interactions, and cellular mechanisms involved in assembling FN dimers into fibrillar matrix are described while highlighting important issues and major questions that require further investigation.
Abstract: In the process of matrix assembly, multivalent extracellular matrix (ECM) proteins are induced to self-associate and to interact with other ECM proteins to form fibrillar networks. Matrix assembly is usually initiated by ECM glycoproteins binding to cell surface receptors, such as fibronectin (FN) dimers binding to α5β1 integrin. Receptor binding stimulates FN self-association mediated by the N-terminal assembly domain and organizes the actin cytoskeleton to promote cell contractility. FN conformational changes expose additional binding sites that participate in fibril formation and in conversion of fibrils into a stabilized, insoluble form. Once assembled, the FN matrix impacts tissue organization by contributing to the assembly of other ECM proteins. Here, we describe the major steps, molecular interactions, and cellular mechanisms involved in assembling FN dimers into fibrillar matrix while highlighting important issues and major questions that require further investigation.
796 citations
01 Jan 2010
TL;DR: The major steps, molecular interactions, and cellular mechanisms involved in assembling FN dimers into fibrillar matrix are described while highlighting important issues and major questions that require further investigation.
Abstract: In the process of matrix assembly, multivalent extracellular matrix (ECM) proteins are induced to self-associate and to interact with other ECM proteins to form fibrillar networks. Matrix assembly is usually initiated by ECM glycoproteins binding to cell surface receptors, such as fibronectin (FN) dimers binding to α5β1 integrin. Receptor binding stimulates FN self-association mediated by the N-terminal assembly domain and organizes the actin cytoskeleton to promote cell contractility. FN conformational changes expose additional binding sites that participate in fibril formation and in conversion of fibrils into a stabilized, insoluble form. Once assembled, the FN matrix impacts tissue organization by contributing to the assembly of other ECM proteins. Here, we describe the major steps, molecular interactions, and cellular mechanisms involved in assembling FN dimers into fibrillar matrix while highlighting important issues and major questions that require further investigation.
13 citations
TL;DR: The authors hypothesize that the underlying mechanism is oxygen plasma treatment-induced selective enhancement of ligand exposure from the deposited functionalized nanoparticles, which facilitates ligand receptor clustering at the cell membrane.
Abstract: The authors demonstrate a novel, efficient, and widely applicable approach to direct the patterning of ligand-functionalized organic nanoparticles derived from albumin on nonconductive, biodegradable polymeric substrates. In contrast to traditional deposition methods for inorganic nanoparticles, the approach involves oxygen plasma treatment of spatially restricted regions on a nonbiopermissive polymer. Albumin nanoparticles conjugated with a truncated fragment of fibronectin containing the Arg-Gly-Asp domain were successfully patterned and used as templates to elicit adhesion and spreading of human mesenchymal stem cells and fibroblasts. Attachment and spreading of both cell types into the plasma-exposed polymer areas was considerably more pronounced than with the ligand alone. The authors hypothesize that the underlying mechanism is oxygen plasma treatment-induced selective enhancement of ligand exposure from the deposited functionalized nanoparticles, which facilitates ligand receptor clustering at the cell membrane. The results highlight a promising nanoscale approach to modulate ligand presentation and spatially direct cell attachment and phenotypic behaviors.
5 citations