UT-MUC-1, a New Mucoepidermoid Carcinoma Cell Line, and Its Radiosensitivity

Grénman, Reidar; Pekkola‐Heino, Kirsi; Joensuu, Heikki; Aitasalo, Kalle; Klemi, Pekka; Lakkala, Taina

doi:10.1001/archotol.1992.01880050096023

Cited by 35 publications

(23 citation statements)

References 19 publications

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“…The UT-SCC series was established from SCC and the UT-MUC-1 cell line from a mucoepidermoid carcinoma of the head and neck in the University of Turku. 2,16 The UM-SCC cell lines were established in the University of Michigan by Dr. T.E. Carey.…”

Section: Methodsmentioning

confidence: 99%

Sublethal damage repair capacity in carcinoma cell lines with p53 mutations

et al. 1998

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Section: Methodsmentioning

confidence: 99%

Sublethal damage repair capacity in carcinoma cell lines with p53 mutations

et al. 1998

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“…Human HNSCC cell lines (n = 34) were established at the time of operation from HNSCCs (27). The clinical data of the corresponding tumors are shown in Table 1.…”

Section: Translational Relevancementioning

confidence: 99%

Expression Profiles and Clinical Correlations of Degradome Components in the Tumor Microenvironment of Head and Neck Squamous Cell Carcinoma

Stokes

Joutsa

Ala-aho

et al. 2010

Clinical Cancer Research

106

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Purpose: Head and neck squamous cell carcinomas (HNSCC) are characterized by high morbidity and mortality, largely due to the high invasive and metastatic potential of these tumors, high recurrence rates, and low treatment responses. Proteinases have been implicated in several aspects of tumor growth and metastasis in a broad range of tumors including HNSCC.Experimental Design: Comprehensive expression profiling of proteinases [matrix metalloproteinases (MMPs), A disintegrin and metalloproteinase (ADAMs), and ADAMs with thrombospondin motif (ADAMTSs)] and their inhibitors [tissue inhibitor of metalloproteinases (TIMPs)] was done using quantitative real-time reverse transcription-PCR analysis of a large cohort of tissue samples representing the tumor (n = 83), the invasive margin (n = 41), and the adjacent tissue (n = 41) from 83 HNSCC patients, along with normal tissue controls (n = 13), as well as cell lines established from tumors of 34 HNSCC patients.Results: The results show specifically elevated gene expression of several proteinases, including MMP1, MMP3, MMP10, and MMP13 within tumor tissue and peritumoral adjacent tissue. In addition, the results identify several novel HNSCC-associated proteinases, including ADAM8, ADAM9, ADAM17, ADAM28, ADAMTS1, ADAMTS8, and ADAMTS15. There were also significant differences in proteinase expression based on clinical parameters, i.e., tumor location, grade, and local invasion. MMP13 expression was significantly higher in large (>4 cm) locally invasive tumors (P < 0.05). MMP9 expression was significantly decreased in tumors with regional metastasis, whereas increased expression of ADAM8 was noted in the metastatic tumors (P < 0.001 for both).Conclusions: These findings suggest the HNSCC degradome as a valuable source of diagnostic, predictive, and prognostic molecular markers for these malignant tumors. Clin Cancer Res; 16(7); 2022-35. ©2010 AACR.Head and neck squamous cell carcinoma (HNSCC) can be defined as a malignant tumor derived from the squamous epithelial cells that line the upper aerodigestive tract, which extends from the surface of the lips to the cervical surface of the esophagus. HNSCC is the fifth most common cancer worldwide and, in 2002, was the cause of over 300,000 deaths worldwide (1). The overall survival rates of HNSCC patients (∼50%) have remained unaltered for over 20 years. The presence of lymph node metastases is the single most important predictive factor for HNSCC patients resulting in a 50% decrease in survival (2, 3).The degradome comprises both the complete set of proteases (also known as peptidases and proteinases) expressed by a cell, tissue, or organism at a given time, and the substrate repertoire of a given proteinase (4). There is a well-established association between matrix proteolysis and cancer invasion and metastasis, and the proteinases of every class have been linked to malignancy and invasion of tumor cells (5). However, through the study of transgenic models and the identification of further proteinases and proteinase s...

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“…Further evidence for the importance of Mect1-Maml2 expression in the tumorigenicity and continued viability of human mucoepidermoid tumors can also be inferred from the detection of the fusion oncogene in the H292 and H3118 MEC tumor cell lines (Tonon et al, 2003) that were derived from patient biopsy samples obtained 22 and 10 years ago, respectively, and which have undergone extensive population doublings in our laboratory. We recently obtained an additional MEC tumor cell line, designated UT-MUC-1 (a kind gift from Dr Grenman), which was generated 15 years ago from a patient with a poorly differentiated mucoepidermoid carcinoma (Grenman et al, 1992) and, using RT-PCR methods (Tonon et al, 2003), we also detected the Mect1-Maml2 fusion transcript (data not shown). Therefore, while there have been only three MEC tumor cell lines isolated and reported to date, the presence of sustained Mect1-Maml2 expression in each case suggests an important role in maintaining tumor cell growth.…”

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Sustained expression of Mect1-Maml2 is essential for tumor cell growth in salivary gland cancers carrying the t(11;19) translocation

et al. 2006

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Mucoepidermoid (MEC) salivary gland tumors arise from a t(11;19) rearrangement which generates a fusion oncogene, Mect1-Maml2, that functions to activate CREB-responsive target genes. To determine if sustained expression of Mect1-Maml2 is required for tumor cell growth, we first showed that ectopic expression of Mect1-Maml2 in rat epithelial RK3E cells is tumorigenic in vivo in nude mice and that excised xenografts continue to express the fusion oncogene. We then generated a hairpin RNAi vector that selectively suppressed the fusion peptide and showed that ectopic expression in either parotid or pulmonary MEC tumor cell lines containing the t(11;19) rearrangement resulted in at least 90% colony growth inhibition. In contrast, single nucleotide changes within this RNAi sequence abolished the ability to suppress Mect1-Maml2 protein and abolished all growth inhibition of these MEC tumor lines. In addition, the RNAi-specific vector had no effect on colony growth of non-MEC tumors including a lung tumor or two other salivary gland cell lines that do not express Mect1-Maml2. We also generated a mutant Mect1-Maml2 expression plasmid that carried silent nucleotide changes within the RNAi target sequence and observed that co-transfection of this mutant, but not wild-type Mect1-Maml2, could partially rescue RNAi growth inhibition in the MEC tumor line. The recent detection of acquired fusion oncogenes in epithelial solid tumors has suggested new possibilities for the diagnosis and therapy of these cancers. Our data show that the 'gain-of-function' activity from aberrant Mect1-Maml2 expression is a candidate therapeutic target for this group of malignant salivary gland tumors.

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UT-MUC-1, a New Mucoepidermoid Carcinoma Cell Line, and Its Radiosensitivity

Cited by 35 publications

References 19 publications

Sublethal damage repair capacity in carcinoma cell lines with p53 mutations

Sublethal damage repair capacity in carcinoma cell lines with p53 mutations

Expression Profiles and Clinical Correlations of Degradome Components in the Tumor Microenvironment of Head and Neck Squamous Cell Carcinoma

Sustained expression of Mect1-Maml2 is essential for tumor cell growth in salivary gland cancers carrying the t(11;19) translocation

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