scholarly journals The c-Jun-induced transformation process involves complex regulation of tenascin-C expression.

1997 ◽  
Vol 17 (6) ◽  
pp. 3202-3209 ◽  
Author(s):  
A Mettouchi ◽  
F Cabon ◽  
N Montreau ◽  
V Dejong ◽  
P Vernier ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Cell Attachment ◽  
Matrix Composition ◽  
Expression Vectors ◽  
Extracellular Matrix Protein ◽  
Cdna Clones ◽  
Tenascin C ◽  
Nf Kappab ◽  
Factor C

In cooperation with an activated ras oncogene, the site-dependent AP-1 transcription factor c-Jun transforms primary rat embryo fibroblasts (REF). Although signal transduction pathways leading to activation of c-Jun proteins have been extensively studied, little is known about c-Jun cellular targets. We identified c-Jun-upregulated cDNA clones homologous to the tenascin-C gene by differential screening of a cDNA library from REF. This tightly regulated gene encodes a rare extracellular matrix protein involved in cell attachment and migration and in the control of cell growth. Transient overexpression of c-Jun induced tenascin-C expression in primary REF and in FR3T3, an established fibroblast cell line. Surprisingly, tenascin-C synthesis was repressed after stable transformation by c-Jun compared to that in the nontransformed parental cells. As assessed by using the tenascin-C (-220 to +79) promoter fragment cloned in a reporter construct, the c-Jun-induced transient activation is mediated by two binding sites: one GCN4/AP-1-like site, at position -146, and one NF-kappaB site, at position -210. Furthermore, as demonstrated by gel shift experiments and cotransfections of the reporter plasmid and expression vectors encoding the p65 subunit of NF-kappaB and c-Jun, the two transcription factors bind and synergistically transactivate the tenascin-C promoter. We previously described two other extracellular matrix proteins, SPARC and thrombospondin-1, as c-Jun targets. Thus, our results strongly suggest that the regulation of the extracellular matrix composition plays a central role in c-Jun-induced transformation.

Restrictin: a chick neural extracellular matrix protein involved in cell attachment co-purifies with the cell recognition molecule F11

Development ◽  
1991 ◽  
Vol 113 (1) ◽  
pp. 151-164 ◽  
Author(s):  
F.G. Rathjen ◽  
J.M. Wolff ◽  
R. Chiquet-Ehrismann
Keyword(s):  
Extracellular Matrix ◽  
Nervous System ◽  
Matrix Protein ◽  
Cell Attachment ◽  
Extracellular Matrix Protein ◽  
Relative Molecular Mass ◽  
Adhesion Assay ◽  
Cell Recognition ◽  
Neural Extracellular Matrix ◽  
Recognition Molecule

We report here the characterization of restrictin, a novel chick neural extracellular matrix glycoprotein associated with the cell recognition molecule F11. Immunoaffinity chromatography using monoclonal antibody 23–13 directed to restrictin yield a major relative molecular mass band at 170 × 10(3) and minor bands at 160, 180, 250 and 320 × 10(3) which are immunologically related to each other. Neural cells attach on immobilized restrictin in a short-term adhesion assay. This adhesion can be blocked specifically by monoclonal or polyclonal antibodies to restrictin but not by antibodies to F11 or by the peptide GRGDSP. Antibodies to restrictin do not interfere with the fasciculation of retinal axons and the isolated restrictin does not stimulate the outgrowth of axons. In the developing nervous system, restrictin is localized in very restricted regions and is found within areas of F11 expression. The timing and pattern of expression of restrictin and its cell attachment activity suggest that it participates in developmental events of the nervous system.

scholarly journals Characterization of multiple adhesive and counteradhesive domains in the extracellular matrix protein cytotactin.

1992 ◽  
Vol 119 (3) ◽  
pp. 663-678 ◽  
Author(s):  
A L Prieto ◽  
C Andersson-Fisone ◽  
K L Crossin
Keyword(s):  
Extracellular Matrix ◽  
Cell Attachment ◽  
Cell Types ◽  
Expression Vectors ◽  
Extracellular Matrix Protein ◽  
Dependent Manner ◽  
Type Iii ◽  
Fibronectin Type Iii ◽  
Fibronectin Type ◽  
Better Than

The extracellular matrix molecule cytotactin is a multidomain protein that plays a role in cell migration, proliferation, and differentiation during development. To analyze the structure-function relationships of the different domains of this glycoprotein, we have prepared a series of fusion constructs in bacterial expression vectors. Results obtained using a number of adhesion assays suggest that at least four independent cell binding regions are distributed among the various cytotactin domains. Two of these are adhesive; two others appear to be counteradhesive in that they inhibit cell attachment to otherwise favorable substrates. The adhesive regions were mapped to the fibronectin type III repeats II-VI and the fibrinogen domain. The morphology of the cells plated onto these adhesive fragments differed; the cells spread on the fibronectin type III repeats as they do on fibronectin, but remained round on the fibrinogen domain. The counteradhesive properties of the molecule were mapped to the EGF-like repeats and the last two fibronectin type III repeats, VII-VIII. The latter region also contained a cell attachment activity that was observed only after proteolysis of the cells. Several cell types were used in these analyses, including fibroblasts, neurons, and glia, all of which are known to bind to cytotactin. The different domains exert their effects in a concentration-dependent manner and can be inhibited by an excess of the soluble molecule, consistent with the hypothesis that the observed properties are mediated by specific receptors. Moreover, it appears that some of these receptors are restricted to particular cell types. For example, glial cells bound better than neurons to the fibrinogen domain and fibroblasts bound better than glia and neurons to the EGF fragment. These results provide a basis for understanding the multiple activities of cytotactin and a framework for isolating different receptors that mediate the various cellular responses to this molecule.

scholarly journals Extracellular Matrix Protein Tenascin C Increases Phagocytosis Mediated by CD47 Loss of Function in Glioblastoma

2019 ◽  
Vol 79 (10) ◽  
pp. 2697-2708 ◽  
Author(s):  
Ding Ma ◽  
Senquan Liu ◽  
Bachchu Lal ◽  
Shuang Wei ◽  
Shuyan Wang ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Extracellular Matrix Protein ◽  
Loss Of Function ◽  
Tenascin C

Extracellular Matrix Protein Coatings for Facilitation of Urothelial Cell Attachment

2007 ◽  
Vol 13 (9) ◽  
pp. 2219-2225 ◽  
Author(s):  
Amber E. Hudson ◽  
Nicole Carmean ◽  
James A. Bassuk
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Cell Attachment ◽  
Urothelial Cell ◽  
Extracellular Matrix Protein ◽  
Protein Coatings

Immunomodulatory role of the extracellular matrix protein tenascin-C in neuroinflammation

2019 ◽  
Vol 47 (6) ◽  
pp. 1651-1660 ◽  
Author(s):  
Susanne Wiemann ◽  
Jacqueline Reinhard ◽  
Andreas Faissner
Keyword(s):  
Extracellular Matrix ◽  
Intracellular Signaling ◽  
Matrix Protein ◽  
Dynamic Network ◽  
Adaptor Proteins ◽  
Extracellular Matrix Protein ◽  
Tenascin C ◽  
Pathological Conditions ◽  
Main Components

The extracellular matrix (ECM) consists of a dynamic network of various macromolecules that are synthesized and released by surrounding cells into the intercellular space. Glycoproteins, proteoglycans and fibrillar proteins are main components of the ECM. In addition to general functions such as structure and stability, the ECM controls several cellular signaling pathways. In this context, ECM molecules have a profound influence on intracellular signaling as receptor-, adhesion- and adaptor-proteins. Due to its various functions, the ECM is essential in the healthy organism, but also under pathological conditions. ECM constituents are part of the glial scar, which is formed in several neurodegenerative diseases that are accompanied by the activation and infiltration of glia as well as immune cells. Remodeling of the ECM modulates the release of pro- and anti-inflammatory cytokines affecting the fate of immune, glial and neuronal cells. Tenascin-C is an ECM glycoprotein that is expressed during embryonic central nervous system (CNS) development. In adults it is present at lower levels but reappears under pathological conditions such as in brain tumors, following injury and in neurodegenerative disorders and is highly associated with glial reactivity as well as scar formation. As a key modulator of the immune response during neurodegeneration in the CNS, tenascin-C is highlighted in this mini-review.

Expression of the Extracellular Matrix Protein Tenascin-C Varies During Lactation

2016 ◽  
Vol 11 (2) ◽  
pp. 86-90
Author(s):  
Wenyi Qin ◽  
Santanu Dasgupta ◽  
Nitai Mukhopadhyay ◽  
Edward R. Sauter
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Extracellular Matrix Protein ◽  
Tenascin C

scholarly journals Hexabrachion proteins in embryonic chicken tissues and human tumors.

1987 ◽  
Vol 105 (3) ◽  
pp. 1387-1394 ◽  
Author(s):  
H P Erickson ◽  
H C Taylor
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Cell Attachment ◽  
Human Fibroblasts ◽  
Human Tumors ◽  
Extracellular Matrix Protein ◽  
Functional Roles ◽  
Chicken Tissues ◽  
Extracellular Matrix Molecule ◽  
Separate Factor

Cell cultures of chicken embryo and human fibroblasts produce a large extracellular matrix molecule with a six-armed structure that we called a hexabrachion (Erickson, H. P., and J. L. Iglesias, 1984, Nature (Lond.), 311:267-269. In the present work we have determined that the myotendinous (M1) antigen described by M. Chiquet and D. M. Fambrough in chicken tissues (1984, J. Cell Biol., 98:1926-1936), and the glioma mesenchymal extracellular matrix protein described by Bourdon et al. in human tumors (Bourdon, M. A., C. J. Wikstrand, H. Furthmayr, T. J. Matthews, and D. D. Bigner, 1983, Cancer Res. 43:2796-2805) have the structure of hexabrachions. We also demonstrate that the M1 antigen is present in embryonic brain, where it was previously reported absent, and have purified hexabrachions from brain homogenates. The recently described cytotactin (Grumet, M., S. Hoffman, K. L. Crossin, and G. M. Edelman, 1985, Proc. Natl. Acad. Sci. USA, 82:8075-8079) now appears to be identical to the chicken hexabrachion protein. In a search for functional roles, we looked for a possible cell attachment activity. A strong, fibronectin-like attachment activity was present in (NH4)2SO4 precipitates of cell supernatant and sedimented with hexabrachions in glycerol gradients. Hexabrachions purified by antibody adsorption, however, had lost this activity, suggesting that it was due to a separate factor associated with hexabrachions in the gradient fractions. The combined information in the several, previously unrelated studies suggests that hexabrachions may play a role in organizing localized regions of extracellular matrix. The protein is prominently expressed at specific times and locations during embryonic development, is retained in certain adult tissues, and is reexpressed in a variety of tumors.

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