Structural differences in the cell binding region of human fibronectin molecules isolated from cultured normal and tumor‐derived human cells

Borsi, Laura; Allemanni, Giorgio; Castellani, Patrizia; Rosellini, C; Vinci, Angela Di; Zardi, Luciano

doi:10.1016/0014-5793(85)80045-4

Cited by 14 publications

(5 citation statements)

References 28 publications

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“…Owing to the availability of domain-specific MAbs, different fibronectin isoforms have been identified according to their tissue origin. Thus, there is fibronectin, termed oncofetal fibronectin, which is produced in high amount by fetal and tumor tissues but not adult normal tissues, and fibronectin produced by normal tissues and present in plasma (Matsuura and Hakomori, 1985;Borsi et al, 1985;Castellani et al, 1986;Zardi et al, 1987;Carnemolla et al, 1989;Loridon-Rosa et al, 1990). Sappino et al (1988) demonstrated the presence of a-smc-actin-positive myofibroblasts in human malignant breast tissues without, however, investigating the type of fibronectin they might produce.…”

Section: Discussionmentioning

confidence: 99%

Fetal myofibroblast‐like cells isolated from post‐radiation fibrosis in human breast cancer

Brouty‐Boyé¹,

Raux²,

Azzarone

et al. 1991

Intl Journal of Cancer

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Cells were isolated from post-radiation fibrosis biopsies of patients with recurrent breast carcinoma. These cells were identified as fibroblasts and compared with fibroblasts from normal breast tissues for their proliferative activities, chromosome number and for the presence of various components of the extracellular matrix and cytoskeleton. The proliferative activity of the fibrosis-derived fibroblasts did not significantly differ from that of normal breast fibroblasts. Both cell types required serum to grow and did not form colonies in soft agar. Cells from 2 of the 3 fibroses analyzed displayed aneuploid karyotypes with multiple structural abnormalities. All of the fibroblastic cells produced types I, III and V collagen, fibronectin and vimentin. However, in contrast to normal breast fibroblasts, fibrosis-derived cells produced high amounts of oncofetal fibronectin. In addition, fibrosis of fibroblasts also expressed the alpha-actin isoform which is specific for smooth-muscle cells. These results suggest that post-radiation fibrosis in malignant breast contains atypical fibroblasts with fetal and myofibroblastic characteristics.

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Section: Discussionmentioning

confidence: 99%

Fetal myofibroblast‐like cells isolated from post‐radiation fibrosis in human breast cancer

Brouty‐Boyé¹,

Raux²,

Azzarone

et al. 1991

Intl Journal of Cancer

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“…Neither depression in the synthesis (Mahdavi and Hynes, 1978Hynes, , 1979, nor increased degradation of Fn Mautner and Hynes, 1977), can apparently explain these differences. Though Fn produced by transformed cells may be altered by its glycosylation (Wagner ef al., 1981), phosphorylation (Ali and Hunter, 1981) and antigenic properties (Borsi et al, 1985), it binds to normal cells 1 2…”

Section: Discussionmentioning

confidence: 99%

Lack of fibronectin‐binding plasma membrane proteins may explain defective pericellular matrix formation in transformed fibroblasts and fibrosarcoma cells

Virtanen

Lehto

Vartio

1987

Intl Journal of Cancer

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Affinity of iodinated fibronectin (Fn) and its defined proteolytic fragments to electrophoretically separated polypeptides of normal and malignant cells was studied in an overlay assay. Cellular 125I-Fn and a major 125I-Fn fragment (Mr 120,000-140,000), containing the cell-binding site, revealed in fibroblasts Mr 170,000, Mr 140,000, and Mr 47,000 Fn-binding polypeptides of which the first two could also be found in the plasma membrane preparations. Binding of 125I-Fns to Mr 170,000 and Mr 140,000 polypeptides was inhibited by the synthetic peptide Arg-Gly-Asp-Ser and to all 3 polypeptides by Fns and Mr 120,000-140,000 fibronectin fragment. Both fibrosarcoma cells and SV40-virus-transformed fibroblasts appeared to lack the Mr 140,000 Fn-binding polypeptide. Binding was similar when Fn from normal fibroblasts or fibrosarcoma cells was used in the assay, while plasma 125I-Fn had weaker affinity towards the Mr 140,000 polypeptide. Instead, proteolytic Fn-fragments, lacking the cell binding site, did not bind to any proteins in the assay. Radioactive cell-surface labelling showed differences in the corresponding surface polypeptide profiles of normal and malignant cells. The results suggest that the failure of pericellular matrix deposition in malignant cells could be due to either defective surface exposition or defective binding property of the Fn-receptor-like polypeptides.

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“…EDB-FN is expressed in a variety of solid tumors and lymphomas [ 12 , 13 ], e.g., liver cancer, breast cancer, lung cancer, colorectal cancer, melanoma, Hodgkin and non-Hodgkin lymphoma, glioma, and head and neck cancer [ 14 ]. Additionally, EDB-FN is not only expressed in tumor cells but also in tumor-associated fibroblasts and neovascular endothelial cells in the tumor microenvironment [ 15 , 16 ]. EDB-FN is related to the stability of tumor tissue structure and tumor angiogenesis [ 17 ] and has a positive correlation with the progression and malignancy of various tumors [ 18 ].…”

Section: Introductionmentioning

confidence: 99%

CAR-T-Cell Therapy for Solid Tumors Positive for Fibronectin Extra Domain B

Zhang

Liu

Yang

et al. 2022

Cells

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(1) Background: The lack of specific targets has slowed the progress of CAR-T in treating solid tumors. Recent studies have revealed that EDB-FN (fibronectin extra domain B) may be an effective target for CAR-T treatment of solid tumors; EDB-FN is expressed in tumor and embryonic tissues, and antibody–cytokine fusion proteins targeting EDB-FN have been developed. However, the therapeutic effects of BBz CAR-engineered T-cells targeting EDB-FN in solid tumors have not been evaluated. (2) Results: In this study, we constructed a BBz CAR construct targeting EDB-FN, and the CAR molecule was expressed on the surface of T-cells by lentiviral transduction. In vitro, CAR-T-cells can be activated to express perforin and granzyme and lyse EDB-positive cells (U-87 MG cells, A549 cells, and HUVECs) and have no toxicity to EDB-negative cells (MCF-7). Compared to T-cells, CAR-T-cells can release cytokines after coculture with EDB-positive cell lines. In vivo, CAR-T-cells inhibited the progression of U-87 MG subcutaneous tumors and significantly reduced the blood vessel density in tumor tissue compared to T-cells, without obvious toxicity to mouse tissues and organs. Furthermore, CAR-T-cells overexpressing BiTE targeting EDB-FN can significantly improve their antitumor activity in vitro. (3) Conclusions: These results demonstrate that CAR-T-cells have specific antitumor and angiogenic activities in vivo and in vitro, suggesting that EDB-FN may be a potential solid tumor target for CAR-T therapy.

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Structural differences in the cell binding region of human fibronectin molecules isolated from cultured normal and tumor‐derived human cells

Cited by 14 publications

References 28 publications

Fetal myofibroblast‐like cells isolated from post‐radiation fibrosis in human breast cancer

Fetal myofibroblast‐like cells isolated from post‐radiation fibrosis in human breast cancer

Lack of fibronectin‐binding plasma membrane proteins may explain defective pericellular matrix formation in transformed fibroblasts and fibrosarcoma cells

CAR-T-Cell Therapy for Solid Tumors Positive for Fibronectin Extra Domain B

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