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Cancer cells have a tremendous ability to sense and respond to extracellular matrix (ECM) stiffness, modulating invasion. The magnitude of the sensed stiffness can either promote or inhibit the migration of cancer cells out of the primary tumor into surrounding tissue. Work has been done on examining the role of stiffness in tuning cancer cell migration by controlling elastic modulus in the bulk. However, a powerful and complementary approach for controlling stiffness is to leverage interactions between stiff-soft (e.g. glass-hydrogel) interfaces. Unfortunately, most work in this area probes cells in 2D environments. Of the reports that probe 3D environments, none have assessed the role of mechanical linkage to the interface as a potential handle in controlling local stiffness and cell behavior. In this paper, we examine the migration of cancer cells embedded in a collagen fiber network between two flat plates. We examine the role of both surface attachment of the collagen network to the stiff interface as well as thickness (50-540 μm) of the collagen gel in driving collagen organization, cell morphology and cell migration. We find that surface attachment and thickness do not operate overlapping mechanisms, because they elicit different cell responses. While thickness and surface chemistry appear to control morphology, only thickness regulates collagen organization and cell migration speed. This suggests that surface attachment and thickness of the collagen gel control cell behavior through both collagen structure and local stiffness in confined fiber-forming networks.
This article was published in the following journal.
Name: Colloids and surfaces. B, Biointerfaces
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Collagen receptors are cell surface receptors that modulate signal transduction between cells and the EXTRACELLULAR MATRIX. They are found in many cell types and are involved in the maintenance and regulation of cell shape and behavior, including PLATELET ACTIVATION and aggregation, through many different signaling pathways and differences in their affinities for collagen isoforms. Collagen receptors include discoidin domain receptors, INTEGRINS, and glycoprotein VI.
Cell surface receptor for LAMININ, epiligrin, FIBRONECTINS, entactin, and COLLAGEN. Integrin alpha3beta1 is the major integrin present in EPITHELIAL CELLS, where it plays a role in the assembly of BASEMENT MEMBRANE as well as in cell migration, and may regulate the functions of other integrins. Two alternatively spliced isoforms of the alpha subunit (INTEGRIN ALPHA3), are differentially expressed in different cell types.
A fibril-associated collagen usually found crosslinked to the surface of COLLAGEN TYPE II fibrils. It is a heterotrimer containing alpha1(IX), alpha2(IX) and alpha3(IX) subunits.
A large superfamily of cell surface membrane proteins characterized by their four transmembrane domains. They play a role in a variety of processes such as cellular adhesion and motility. They may be involved in the organization of cell surface MEMBRANE MICRODOMAINS that regulate the activation of LEUKOCYTES.
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Cancer is not just one disease but many diseases. There are more than 100 different types of cancer. Most cancers are named for the organ or type of cell in which they start - for example, cancer that begins in the colon is called colon cancer; cancer th...
Bladder Cancer Brain Cancer Breast Cancer Cancer Cervical Cancer Colorectal Head & Neck Cancers Hodgkin Lymphoma Leukemia Lung Cancer Melanoma Myeloma Ovarian Cancer Pancreatic Cancer ...