The interaction of tenascin-C with fibronectin modulates the migration and specific metalloprotease activity in human mesothelioma cell lines of different histotype

Giuffrida, A. M.; Scarpa, Susanna; Birarelli, P; Modesti, Andrea

doi:10.3892/ijo.25.3.745

Cited by 9 publications

(7 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…By contrast, the restricted expression pattern of the antigens in normal tissues and the strong expression in many tumor types make L19 and F16 ideal candidates for antibody-based pharmacodelivery applications. To our knowledge, only few immunohistochemical reports on the expression of EDB domain of fibronectin and A1 domain of tenascin-C in lung cancer and in mesothelioma have been published so far [45][46][47][48][49][50][51][52][53][54][55][56]. The vast majority of the normal lung specimens gave only a faint staining or no detectable staining (levels 0-1).…”

Section: Discussionmentioning

confidence: 97%

Comparative immunohistochemistry of L19 and F16 in non-small cell lung cancer and mesothelioma: Two human antibodies investigated in clinical trials in patients with cancer

et al. 2009

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 97%

Comparative immunohistochemistry of L19 and F16 in non-small cell lung cancer and mesothelioma: Two human antibodies investigated in clinical trials in patients with cancer

et al. 2009

View full text Add to dashboard Cite

“…Numerous studies have revealed that tenascin-C plays a certain role in tumor progression including tumorigenesis, proliferation, invasion, metastasis and angiogenesis. (14,15,18,19,22,(32)(33)(34)(35)(36)(37)(38) It is widely acknowledged that tenascin-C disrupts the binding of fibronectin to the integrin α 5 β 1 /syndecan-4 complex at the cell surface, which causes morphological change of cultured cells and promotes cell proliferation. (22,39,40) However, in this study, no significant differences exist in cell morphology or proliferation between the control and tenascin-C-knockdown glioblastoma cells.…”

Section: Discussionmentioning

confidence: 99%

Endogenous tenascin‐C enhances glioblastoma invasion with reactive change of surrounding brain tissue

Hirata

Arakawa²,

Shirahata³

et al. 2009

Cancer Science

View full text Add to dashboard Cite

Tenascin-C is an extracellular matrix glycoprotein implicated in embryogenesis, wound healing and tumor progression. We previously revealed that tenascin-C expression is correlated with the prognosis of patients with glioblastoma. However, the exact role of endogenous tenascin-C in regulation of glioblastoma proliferation and invasion remains to be established. We show here that endogenous tenascin-C facilitates glioblastoma invasion, followed by reactive change of the surrounding brain tissue. Although shRNA-mediated knockdown of endogenous tenascin-C does not affect proliferation of glioblastoma cells, it abolishes cell migration on a two-dimensional substrate and tumor invasion with brain tissue changes in a xenograft model. The tyrosine phosphorylation of focal adhesion kinase, a cytoplasmic tyrosine kinase that associates with integrins, was decreased in tenascin-C-knockdown cells. In the analysis of clinical samples, tenascin-C expression correlates with the volume of peritumoral reactive change detected by magnetic resonance imaging. Interestingly, glioblastoma cells with high tenascin-C expression infiltrate brain tissue in an autocrine manner. Our results suggest that endogenous tenascin-C contributes the invasive nature of glioblastoma and the compositional change of brain tissue, which renders tenascin-C as a prime candidate for anti-invasion therapy for glioblastoma.

show abstract

“…The binding of fibronectin (Fn), a extracellular matrix protein, to integrins has been showed to alter expression of several genes, and to regulate adhesion, migration, proliferation and apoptosis of epithelial cells [Harkonen et al, 1995; Matter and Ruoslahti, 2001; Ohke et al, 2001; Giuffrida et al, 2004; Jarvis and Bryers, 2005; Yamazaki et al, 2005]. Signal transduction from integrins after binding of matrix protein proceeds via several intermediate pathways, such as alteration in calcium influx [Canti et al, 2005], changes in inositol phosphate metabolism [Jones et al, 2005; Ruzzi et al, 2005], and activation of multiple protein tyrosine kinases, including focal adhesion kinase(FAK) and certain MAP kinases [Wierzbicka‐Patynowski and Schwarzbauer, 2002].…”

Section: Discussionmentioning

confidence: 99%

Wound repair and proliferation of bronchial epithelial cells regulated by CTNNAL1

Xiang

Tan

Zhang

et al. 2007

J of Cellular Biochemistry

View full text Add to dashboard Cite

Adhesion molecules play vital roles in airway hyperresponsiveness (AHR) or airway inflammation. Our previous study indicated that adhesion molecule catenin alpha-like 1 (CTNNAL1) is relevant closely to asthma susceptibility, but its biological function or significance is still unclear. In the present study, we observed the temporal and spatial distribution of CTNNAL1 expression in mouse lung tissue with the OVA-sensitized asthma model and found that the level of CTNNAL1 mRNA showed a prominent negative correlation with pulmonary resistance (R(L)). To study the function of CTNNAL1 in airway, effects of CTNNAL1 on proliferation and wound repair activity of human bronchial epithelial cells (HBEC) was investigated with antisense oligonucleotide (ASO) technique. The results showed that: (1) CTNNAL1 ASO could decelerate the repairing velocity and proliferation of HBEC; (2) CTNNAL1 expression was increased on the edge cells of mechanic wounded area in culture; (3) extracellular matrix component fibronectin (Fn) obviously promoted wound repair activity and proliferation of HBEC, which could be blocked by CTNNAL1 ASO; (4) Western blot showed that Fn could promote FAK phosphorylation, which also be inhibited by CTNNAL1 ASO. In conclusion, the level of CTNNAL1 mRNA expression is highly correlated to airway resistance; CTNNAL1 may contribute to the wound repair and proliferation of HBEC. Furthermore, it may serve to Fn mediated cell-extracellular adhesion and its signal transduction.

show abstract

The interaction of tenascin-C with fibronectin modulates the migration and specific metalloprotease activity in human mesothelioma cell lines of different histotype

Cited by 9 publications

References 0 publications

Comparative immunohistochemistry of L19 and F16 in non-small cell lung cancer and mesothelioma: Two human antibodies investigated in clinical trials in patients with cancer

Comparative immunohistochemistry of L19 and F16 in non-small cell lung cancer and mesothelioma: Two human antibodies investigated in clinical trials in patients with cancer

Endogenous tenascin‐C enhances glioblastoma invasion with reactive change of surrounding brain tissue

Wound repair and proliferation of bronchial epithelial cells regulated by CTNNAL1

Contact Info

Product

Resources

About