Modulation of cell-extracellular matrix interactions. 1998

J L Sechler, and S A Corbett, and M B Wenk, and J E Schwarzbauer
Department of Molecular Biology, Princeton University, New Jersey 08544-1014, USA.

Changes in extracellular matrix (ECM) structure and composition, such as occur during morphogenesis, can have important regulatory effects on cell behavior. Two fibronectin (FN)-based systems have been developed to dissect how cells respond to different types of ECM. One system mimics the provisional matrix of the wound and is composed of FN cross-linked into a fibrin clot matrix. Unlike cells on FN alone, cells on an FN-fibrin matrix are smaller with cortical distribution of actin filaments and membrane ruffles. Addition of the ECM protein tenascin to the FN-fibrin matrix induces a different cell morphology. Thus, matrix composition can have profound effects on cell phenotype. Cells also interact with FN while assembling it into a fibrillar matrix. Using recombinant FNs, a domain that is required for normal progression of FN fibril formation has been identified. During assembly of this recombinant matrix, formation of actin stress fibers and focal adhesions is delayed, demonstrating that changes in FN matrix structure can affect intracellular organization and activation of signaling pathways.

UI MeSH Term Description Entries
D009024 Morphogenesis The development of anatomical structures to create the form of a single- or multi-cell organism. Morphogenesis provides form changes of a part, parts, or the whole organism.
D002468 Cell Physiological Phenomena Cellular processes, properties, and characteristics. Cell Physiological Processes,Cell Physiology,Cell Physiological Phenomenon,Cell Physiological Process,Physiology, Cell,Phenomena, Cell Physiological,Phenomenon, Cell Physiological,Physiological Process, Cell,Physiological Processes, Cell,Process, Cell Physiological,Processes, Cell Physiological
D005109 Extracellular Matrix A meshwork-like substance found within the extracellular space and in association with the basement membrane of the cell surface. It promotes cellular proliferation and provides a supporting structure to which cells or cell lysates in culture dishes adhere. Matrix, Extracellular,Extracellular Matrices,Matrices, Extracellular
D005337 Fibrin A protein derived from FIBRINOGEN in the presence of THROMBIN, which forms part of the blood clot. Antithrombin I
D005353 Fibronectins Glycoproteins found on the surfaces of cells, particularly in fibrillar structures. The proteins are lost or reduced when these cells undergo viral or chemical transformation. They are highly susceptible to proteolysis and are substrates for activated blood coagulation factor VIII. The forms present in plasma are called cold-insoluble globulins. Cold-Insoluble Globulins,LETS Proteins,Fibronectin,Opsonic Glycoprotein,Opsonic alpha(2)SB Glycoprotein,alpha 2-Surface Binding Glycoprotein,Cold Insoluble Globulins,Globulins, Cold-Insoluble,Glycoprotein, Opsonic,Proteins, LETS,alpha 2 Surface Binding Glycoprotein
D000199 Actins Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle. F-Actin,G-Actin,Actin,Isoactin,N-Actin,alpha-Actin,alpha-Isoactin,beta-Actin,gamma-Actin,F Actin,G Actin,N Actin,alpha Actin,alpha Isoactin,beta Actin,gamma Actin
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D015398 Signal Transduction The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway. Cell Signaling,Receptor-Mediated Signal Transduction,Signal Pathways,Receptor Mediated Signal Transduction,Signal Transduction Pathways,Signal Transduction Systems,Pathway, Signal,Pathway, Signal Transduction,Pathways, Signal,Pathways, Signal Transduction,Receptor-Mediated Signal Transductions,Signal Pathway,Signal Transduction Pathway,Signal Transduction System,Signal Transduction, Receptor-Mediated,Signal Transductions,Signal Transductions, Receptor-Mediated,System, Signal Transduction,Systems, Signal Transduction,Transduction, Signal,Transductions, Signal
D019063 Tenascin Hexameric extracellular matrix glycoprotein transiently expressed in many developing organs and often re-expressed in tumors. It is present in the central and peripheral nervous systems as well as in smooth muscle and tendons. (From Kreis & Vale, Guidebook to the Extracellular Matrix and Adhesion Proteins, 1993, p93) Cytotactin,Hexabrachion,Tenascin-C,J1-200-220,Tenascin C

Related Publications

J L Sechler, and S A Corbett, and M B Wenk, and J E Schwarzbauer
January 1995, Experimental nephrology,
J L Sechler, and S A Corbett, and M B Wenk, and J E Schwarzbauer
January 2002, International journal of developmental neuroscience : the official journal of the International Society for Developmental Neuroscience,
J L Sechler, and S A Corbett, and M B Wenk, and J E Schwarzbauer
December 1990, Cell differentiation and development : the official journal of the International Society of Developmental Biologists,
J L Sechler, and S A Corbett, and M B Wenk, and J E Schwarzbauer
January 1985, Annals of the New York Academy of Sciences,
J L Sechler, and S A Corbett, and M B Wenk, and J E Schwarzbauer
January 2001, Methods in cell biology,
J L Sechler, and S A Corbett, and M B Wenk, and J E Schwarzbauer
March 1993, Journal of periodontal research,
J L Sechler, and S A Corbett, and M B Wenk, and J E Schwarzbauer
September 1997, Transplant immunology,
J L Sechler, and S A Corbett, and M B Wenk, and J E Schwarzbauer
January 1977, Clinical orthopaedics and related research,
J L Sechler, and S A Corbett, and M B Wenk, and J E Schwarzbauer
January 2020, Advances in experimental medicine and biology,
J L Sechler, and S A Corbett, and M B Wenk, and J E Schwarzbauer
January 2010, Cell and tissue research,
Copied contents to your clipboard!