Tenascin interferes with fibronectin action

Chiquet‐Ehrismann, Ruth; Kalla, Peter; Pearson, Carolyn A.; Beck, Konrad; Chiquet, Matthias

doi:10.1016/0092-8674(88)90158-4

Cited by 564 publications

(350 citation statements)

References 40 publications

Supporting

Mentioning

331

Contrasting

Unclassified

Order By: Relevance

“…(Ghert et al 2001) It has both adhesive and anti-adhesive effects and is involved in cell migration, ECM remodeling, development, tumorogenesis and wound healing. (Chiquet-Ehrismann et al 1988;Vainio et al 1989;Ghert et al 2001;Bornstein and Sage 2002;Chiquet-Ehrismann and Chiquet 2003;ChiquetEhrismann 2004) Some of these processes occur via tenascin C's association with fibronectin fibrils and effects on fibronectin-cell interactions. (Chung et al 1995;Ghert et al 2001) In addition to exhibiting changes in levels with various treatments that modify outflow facility (see later), tenascin C also undergoes a number of changes in mRNA splicing (Keller et al, manuscript in preparation).…”

Section: Matricellular Proteinsmentioning

confidence: 99%

Extracellular matrix in the trabecular meshwork

Acott

Kelley

2008

Experimental Eye Research

424

443

View full text Add to dashboard Cite

The extracellular matrix (ECM) of the trabecular meshwork (TM) is thought to be important in regulating intraocular pressure (IOP) in both normal and glaucomatous eyes. IOP is regulated primarily by a fluid resistance to aqueous humor outflow. However, neither the exact site nor the identity of the normal resistance to aqueous humor outflow has been established. Whether the site and nature of the increased outflow resistance, which is associated with open-angle glaucoma, is the same or different from the normal resistance is also unclear.The ECMs of the TM beams, juxtacanalicular region (JCT) and Schlemm's canal (SC) inner wall are comprised of fibrillar and non-fibrillar collagens, elastin-containing microfibrils, matricellular and structural organizing proteins, glycosaminoglycans (GAGs) and proteoglycans. Both basement membranes and stromal ECM are present in the TM beams and JCT region. Cell adhesion proteins, cell surface ECM receptors and associated binding proteins are also present in the beams, JCT and SC inner wall region.The outflow pathway ECM is relatively dynamic, undergoing constant turnover and remodeling. Regulated changes in enzymes responsible for ECM degradation and biosynthetic replacement are observed. IOP homeostasis, triggered by pressure changes or mechanical stretching of the TM, appears to involve ECM turnover. Several cytokines, growth factors and drugs, which affect the outflow resistance, change ECM component expression, mRNA alternative splicing, cellular cytoskeletal organization or all of these. Changes in ECM associated with open-angle glaucoma have been identified.

show abstract

Section: Matricellular Proteinsmentioning

confidence: 99%

Extracellular matrix in the trabecular meshwork

Acott

Kelley

2008

Experimental Eye Research

424

443

View full text Add to dashboard Cite

show abstract

“…Lightner and Erickson (1990) did not find significant interaction of tenascin neither with several collagen types tested nor with fibronectin. Faissner et al (1990) reported on the binding of tenascin to various collagens but not to fibronectin, and finally Chiquet-Ehrismann et al (1988) and Hoffman et al (1988) presented evidence for the interaction of tenascin with fibronectin.…”

Section: Introductionmentioning

confidence: 99%

Tenascin variants: differential binding to fibronectin and distinct distribution in cell cultures and tissues.

et al. 1991

View full text Add to dashboard Cite

In the chicken, three tenascin variants have been characterized that are generated by alternative splicing of 3 of its 11 fibronectin type III repeats. Using monoclonal antibodies that react with common regions versus extra repeats of tenascin, we could distinguish and separate tenascin variants and investigate their interaction with fibronectin using multiple experimental procedures. Interestingly, in all assays used the smallest tenascin variant bound more strongly to fibronectin than the larger ones. These biochemical data were paralleled by the observation that in chick embryo fibroblast cultures only the smallest form of tenascin could be detected in the fibronectin-rich extracellular matrix network laid down by the cells. Furthermore, each tissue present in adult chicken gizzard contained a distinct set of tenascin variants. Those tissues particularly rich in extracellular matrix, such as the tendon, contained the smallest tenascin only. Intermediate-sized tenascin was present in smooth muscle, whereas the largest form was exclusively detectable underneath the epithelial lining of the villi. Thus it appears that cell type-specific forms of tenascin exist that are appropriate for the functional requirements of the respective extracellular matrices.

show abstract

“…Tenascin has also been found to be associated with mesodermal cell migration during amphibian gastrulation in vivo (Riou et al 1990) and promotes neural crest cell migration in avian embryos (Akitaya and Bronner-Fraser 1992). Because both tenascin and thrombospondin inhibit cell adhesion to fibronectin substrates in vitro, these two large ECM glycoproteins might have counter-adhesive potential in vivo (Bornstein 1995;Chiquet-Ehrismann et al 1988).…”

mentioning

confidence: 99%

Ectopic Expression of SPARC inXenopusEmbryos Interferes with Tissue Morphogenesis: Identification of a Bioactive Sequence in the C-terminal EF Hand

Damjanovski

Karp

Funk

et al. 1997

J Histochem Cytochem.

View full text Add to dashboard Cite

SUMMARY SPARC is a matricellular Ca 2 ϩ -binding glycoprotein that exhibits both counteradhesive and antiproliferative effects on cultured cells. It is secreted by cells of various tissues as a consequence of morphogenesis, response to injury, and cyclic renewal and/or repair. In an earlier study with Xenopus embryos we had shown a highly specific and regulated pattern of SPARC expression. We now show that ectopic expression of SPARC before its normal embryonic activation produces severe anomalies, some of which are consistent with the functions of SPARC proposed from studies in vitro. Microinjection of SPARC RNA, protein, and peptides into Xenopus embryos before endogenous embryonic expression generated different but overlapping phenotypes. (a) Injection of SPARC RNA into one cell of a two-cell embryo resulted in a range of unilateral defects. (b) Precocious exposure of embryos to SPARC by microinjection of protein into the blastocoel cavity was associated with certain axial defects comparable to those obtained with SPARC RNA. (c) SPARC peptides containing follistatin-like and copper-binding sequences were without obvious effect, whereas SPARC peptide 4.2, corresponding to a disulfide-bonded, Ca 2 ϩ -binding domain, was associated with a reduction in axial structures that led eventually to complete ventralization of the embryos. Histological analysis of ventralized embryos indicated that the morphogenetic events associated with gastrulation might have been inhibited. Microinjection of other Ca 2 ϩ -binding glycoproteins, such as osteopontin and bone sialoprotein, resulted in phenotypes that were unique. We probed further the structural correlates of this region of SPARC in the context of tissue development. Co-injection of peptide 4.2 with Ca 2 ϩ or EGTA, and injection of peptide 4.2K (containing a mutated consensus Ca 2 ϩ -binding sequence), demonstrated that the developmental defects associated with peptide 4.2 were independent of Ca 2 ϩ . However, the disulfide bridge in this region of SPARC was found to be critical, as injection of peptide 4.2AA, a mutant lacking the cystine, generated no axial defects. We have therefore shown for the first time in vivo that the temporally inappropriate presence of SPARC is associated with perturbations in tissue morphogenesis. Moreover, we have identified at least one bioactive region of SPARC as the C-terminal disulfide-bonded, Ca 2 ϩ -binding loop that was previously shown to be both counteradhesive and growth-inhibitory. (J Histochem Cytochem 45:643-655, 1997) E xtracellular matrix glycoproteins make major morphoregulatory contributions to early embryonic development. Their complex, transient expression patterns, structural heterogeneity, and functional diversity indicate important roles in the modulation of a broad spectrum of cellular activities, such as adhesion, migration, communication, and/or proliferation. For example, the blastocoel roof of amphibian embryos is coated with an elaborate network of fibronectin fibers before the involution of mesodermal cells durin...

show abstract

Tenascin interferes with fibronectin action

Cited by 564 publications

References 40 publications

Extracellular matrix in the trabecular meshwork

Extracellular matrix in the trabecular meshwork

Tenascin variants: differential binding to fibronectin and distinct distribution in cell cultures and tissues.

Ectopic Expression of SPARC inXenopusEmbryos Interferes with Tissue Morphogenesis: Identification of a Bioactive Sequence in the C-terminal EF Hand

Contact Info

Product

Resources

About