ArticleCellular oncology (Dordrecht, Netherlands)2013
Tumor protein D54 is a negative regulator of extracellular matrix-dependent migration and attachment in oral squamous cell carcinoma-derived cell lines.
Article in Cellular oncology (Dordrecht, Netherlands), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 28 citations in OpenAlex.
- Unpacking the Tumor Protein D52-like Family: Roles in Intracellular Trafficking and Cancer Progression.Cells · 2026Review
- Dual oncogenic roles of TPD52 and TPD52L2 in gastric cancer progression via PI3K/AKT activation and immunosuppressive microenvironment remodeling.Briefings in functional genomics · 2025Article
- Tumor Protein D53 (TPD53): Involvement in Malignant Transformation of Low-Malignant Oral Squamous Cell Carcinoma Cells.Biomedicines · 2024Article
- Genome-wide detection of positive and balancing signatures of selection shared by four domesticated rainbow trout populations (Oncorhynchus mykiss).Genetics, selection, evolution : GSE · 2024Article
- Suprabasin enhances the invasion, migration, and angiogenic ability of oral squamous cell carcinoma cells under hypoxic conditions.Oncology reports · 2023Article
- Patterns of Cannabis- and Substance-Related Congenital General Anomalies in Europe: A Geospatiotemporal and Causal Inferential Study.Pediatric reports · 2023Article
- De novo FZR1 loss-of-function variants cause developmental and epileptic encephalopathies.Brain : a journal of neurology · 2022Article
- Intracellular nanovesicles mediate α5β1 integrin trafficking during cell migration.The Journal of cell biology · 2021Article
- The novel function of tumor protein D54 in regulating pyruvate dehydrogenase and metformin cytotoxicity in breast cancer.Cancer & metabolism · 2019Article
- Proteome-Wide Characterization of Phosphorylation-Induced Conformational Changes in Breast Cancer.Journal of proteome research · 2018Article
- Increased expression of tumor protein D54 is associated with clinical progression and poor prognosis in patients with prostate cancer.Oncology letters · 2017Article
- Tumor Proteins D52 and D54 Have Opposite Effects on the Terminal Differentiation of Chondrocytes.BioMed research international · 2017Article
- Methanol and Butanol Extracts of Paeonia lutea Leaves Repress Metastasis of Squamous Cell Carcinoma.Evidence-based complementary and alternative medicine : eCAM · 2016Article
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6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeTumor protein D54 (TPD54) belongs to the TPD52 family of proteins and is expressed in several types of cancer, including oral squamous cell carcinoma (OSCC). Here, we investigated relationships between various OSCC-related characteristics and TPD54 expression in vitro.
methodsThe expression of TPD54 in several OSCC-derived cell lines and normal, non-malignant, cells was assessed. Based on the results obtained, OSCC-derived SAS cells were subsequently subjected to exogenous over-expression of alternative splice variants (ASVs) of TPD54 and to TPD54 knock-down, mediated by siRNA. Next, the role of TPD54 in cellular growth, apoptosis, invasion, migration and extracellular-matrix (ECM)-dependent migration and attachment was investigated, as also the concomitant expression of integrins and integrin-related proteins by the OSCC-derived cells.
resultsWestern blot analysis and RT-PCR revealed that several TPD54 ASVs were expressed in the OSCC-derived cell lines tested. Neither exogenous ASV over-expression nor TPD54 knock-down modulated the proliferation or invasion of SAS cells in a monolayer culture assay. However, exogenous ASV over-expression did decrease anchorage-independent growth and TPD54 knock-down did increase anchorage-independent growth, irrespective of caspase activities. The same effects were observed on ECM-dependent cellular migration and cell attachment to the ECM. The expression levels of the major α and β integrin subunits, and of E-cadherin, were found to be similar to those observed in the non-transfected control cells, whereas talin1 expression was found to be increased after TPD54 knock-down. Also Akt was found to be activated after TPD54 knock-down, even in the absence of serum stimulation. Very similar effects were observed in the OSCC-derived cell lines HSC 2 and HSC 3.
conclusionsOur results show that TPD54 affects OSCC cell attachment to the ECM, OSCC cell migration, and Akt/PKB activation by modulating integrin activation via a talin1-mediated inside-out signal of the ECM. Based on these results, we suggest that TPD54 may serve as a novel biomarker for OSCC and as a putative target for OSCC therapy.
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