Signaling of de-adhesion in cellular regulation and motility

Greenwood, Jeffrey A.; Murphy-Ullrich, Joanne E.

doi:10.1002/(sici)1097-0029(19981201)43:5<420::aid-jemt8>3.0.co;2-b

Cited by 99 publications

(70 citation statements)

References 95 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…When exposed to cells in its soluble form, thrombospondin has primarily anti-adhesive effects characterized by a reorganization of stress fibers and loss of focal adhesion plaques as ascertained by interference reflection microscopy (5-7). Vinculin and ␣-actinin, but not the ␣ v ␤ 3 integrin, are selectively redistributed from the restructured focal adhesions in response to thrombospondin (5,8). A 19-amino acid sequence (amino acids [17][18][19][20][21][22][23][24][25][26][27][28][29][30][31][32][33][34][35] in the N-terminal heparin-binding domains of both TSP-1 and TSP-2, referred to as the hep I peptide, has been determined to be sufficient for focal adhesion disassembly (9).…”

Section: Thrombospondin (Tsp)mentioning

confidence: 96%

“…The signaling events stimulated by thrombospondin/hep I interactions with cells are only partially understood. It is known that thrombospondin/hep I binding to endothelial cells stimulates activation of phosphoinositide 3-kinase (PI3K) and generation of phosphatidylinositide (3,4,5)-trisphosphate (PtdIns(3,4,5)P 3 ) (8). Basal levels of cyclic GMP-dependent protein kinase activity are also necessary for thrombospondin-mediated focal adhesion disassembly (10).…”

Section: Thrombospondin (Tsp)mentioning

confidence: 99%

See 1 more Smart Citation

Thrombospondin Mediates Focal Adhesion Disassembly through Interactions with Cell Surface Calreticulin

Goicoechea¹,

Orr²,

Pallero³

et al. 2000

Journal of Biological Chemistry

Self Cite

155

135

View full text Add to dashboard Cite

Thrombospondin induces reorganization of the actin cytoskeleton and restructuring of focal adhesions. This activity is localized to amino acids 17-35 in the N-terminal heparin-binding domain of thrombospondin and can be replicated by a peptide (hep I) with this sequence. Thrombospondin/hep I stimulate focal adhesion disassembly through a mechanism involving phosphoinositide 3-kinase activation. However, the receptor for this thrombospondin sequence is unknown. We now report that calreticulin on the cell surface mediates focal adhesion disassembly by thrombospondin/hep I. A 60-kDa protein from endothelial cell detergent extracts has homology and immunoreactivity to calreticulin, binds a hep I affinity column, and neutralizes thrombospondin/ hep I-mediated focal adhesion disassembly. Calreticulin on the cell surface was confirmed by biotinylation, confocal microscopy, and by fluorescence-activated cell sorting analyses. Thrombospondin and calreticulin potentially bind through the hep I sequence, since thrombospondin-calreticulin complex formation can be blocked specifically by hep I peptide. Antibodies to calreticulin and preincubation of thrombospondin/hep I with glutathione S-transferase-calreticulin block thrombospondin/hep I-mediated focal adhesion disassembly and phosphoinositide 3-kinase activation, suggesting that calreticulin is a component of the thrombospondin-induced signaling cascade that regulates cytoskeletal organization. These data identify both a novel receptor for the N terminus of thrombospondin and a distinct role for cell surface calreticulin in cell adhesion.

show abstract

Section: Thrombospondin (Tsp)mentioning

confidence: 96%

Section: Thrombospondin (Tsp)mentioning

confidence: 99%

Thrombospondin Mediates Focal Adhesion Disassembly through Interactions with Cell Surface Calreticulin

Goicoechea¹,

Orr²,

Pallero³

et al. 2000

Journal of Biological Chemistry

Self Cite

155

135

View full text Add to dashboard Cite

show abstract

“…Thus, TNC can inhibit adhesion (Chiquet-Ehrismann et al, 1988;Lightner and Erickson, 1990) or support weak and transient attachment (Lotz et al, 1989) depending on the cell type. TNC may mediate de-adhesion by shifting cells from strong adhesion to temporary attachment (Greenwood and Murphy-Ullrich, 1998). As we found here, TNC may inhibit strong adhesion at costameres but promote temporary noncostameric attachment of cardiomyocytes.…”

Section: Imanaka-yoshida Et Almentioning

confidence: 99%

Tenascin-C Modulates Adhesion of Cardiomyocytes to Extracellular Matrix during Tissue Remodeling after Myocardial Infarction

Imanaka‐Yoshida

Hiroe

Nishikawa

et al. 2001

Laboratory Investigation

149

159

View full text Add to dashboard Cite

SUMMARY: Tenascin-C (TNC), an extracellular matrix glycoprotein, plays important roles in tissue remodeling. TNC is not normally expressed in adults but reappears under pathologic conditions. The present study was designed to clarify the contribution of TNC to ventricular remodeling after myocardial infarction. We examined the expression of TNC after experimental myocardial infarction in the rat by immunohistochemistry and in situ hybridization. Within 24 hours of permanent coronary ligation, interstitial fibroblasts in the border zone started to express TNC mRNA. The expression of TNC was down-regulated on Day 7 and was no longer apparent by Day 14 after infarction. During the healing process, TNC protein and TNC-producing cells were found at the edges of the residual myocardium. Some of the TNC-producing cells were immunoreactive for ␣-smooth muscle actin. In culture, TNC increased the number of cardiomyocytes attached to laminin but inhibited the formation of focal contacts at costameres. The results indicate that during the acute phase after myocardial infarction, interstitial cells in the border zone synthesize TNC, which may loosen the strong adhesion of surviving cardiomyocytes to connective tissue and thereby facilitate tissue reorganization. (Lab Invest 2001, 81:1015-1024.T enascins constitute a family of extracellular matrix glycoproteins (Erickson, 1993). The first member found, tenascin-C (TNC), is highly expressed in embryonic tissue during morphogenesis and sparsely expressed in the adult, but reappears during wound healing, regeneration, or cancer invasion (Chiquet-Ehrismann et al, 1986). TNC is transiently expressed in distinct areas in association with active tissue remodeling. Various in vitro findings have indicated that TNC has multiple functions in the regulation of cell migration, proliferation, and apoptosis (Chung et al, 1996;Jones and Jones, 2000). TNC counterbalances cell adhesion to substrata, correlated with cytokinesis and motility, and prevents cells from adhering too tightly to other extracellular matrix proteins (Chiquet-Ehrismann, 1995;Chiquet-Ehrismann et al, 1988;Chung et al, 1996;Murphy-Ullrich et al, 1991;Prieto et al, 1992).In the heart, TNC appears only at very early stages of embryonic development and may play important roles in the differentiation of cardiomyocytes, structural organization of the myocardium, or development of coronary vessels . TNC is not normally expressed in the adult heart but reappears under various pathologic conditions such as dilated cardiomyopathy, myocarditis, or myocardial infarction (Imanaka-Yoshida et al, 1998, 2000Tamura et al, 1996;Willems et al, 1996).To understand its roles in tissue remodeling in the diseased myocardium, we examined the expression of TNC during tissue repair after experimental myocardial infarction in rats. Sequential changes in the localization of the molecule were analyzed by immunohistochemistry, and TNC-producing cells were identified by in situ hybridization (ISH) combined with immunohistochemistry. Additionally, to ...

show abstract

“…Several growth factors, including epidermal growth factor and platelet-derived growth factor, and the matricellular family of extracellular matrix proteins, including thrombospondin (TSP1), 1 tenascin-C, and SPARC, stimulate focal adhesion disassembly characterized by the loss of highly bundled actin stress fibers and the selective depletion of vinculin and ␣-actinin from the focal adhesion plaque (11,12). However, cells remain spread and integrins remain clustered and linked to talin and paxillin, indicating an incomplete loss of adhesion.…”

mentioning

confidence: 99%

Thrombospondin Induces RhoA Inactivation through FAK-dependent Signaling to Stimulate Focal Adhesion Disassembly

Orr¹,

Pallero

Xiong

et al. 2004

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Signaling of de-adhesion in cellular regulation and motility

Cited by 99 publications

References 95 publications

Thrombospondin Mediates Focal Adhesion Disassembly through Interactions with Cell Surface Calreticulin

Thrombospondin Mediates Focal Adhesion Disassembly through Interactions with Cell Surface Calreticulin

Tenascin-C Modulates Adhesion of Cardiomyocytes to Extracellular Matrix during Tissue Remodeling after Myocardial Infarction

Thrombospondin Induces RhoA Inactivation through FAK-dependent Signaling to Stimulate Focal Adhesion Disassembly

Contact Info

Product

Resources

About