Correlation between CA19‐9 production <i>in vitro</i> and histological grades of differentiation <i>in vivo</i> in clones isolated from a human pancreatic cancer cell line (SUIT‐2)

Iwamura, Takeshi; Taniguchi, Shoji; Kitamura, Norio; Yamanari, Hideo; Kojima, Akira; Hidaka, Kaori; Setoguchi, Toshiaki; Katsuki, Taketo

doi:10.1111/j.1440-1746.1992.tb01030.x

Cited by 49 publications

(38 citation statements)

References 13 publications

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“…Panc1 is a poorly differentiated human pancreatic adenocarcinoma cell line that expresses low levels of endogenous MUC1 and relatively low levels of other glycoproteins (28). S2-013 is a moderately differentiated human pancreatic tumor cell line that is known to express abundant O-glycosylated mucin-like proteins, including low levels of endogenous MUC1 (23). cDNA constructs encoding FLAG epitope-tagged forms of MUC1 have been described previously (12).…”

Section: Resultsmentioning

confidence: 99%

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Platelet-Derived Growth Factor Receptor β–Mediated Phosphorylation of MUC1 Enhances Invasiveness in Pancreatic Adenocarcinoma Cells

Singh

Wen

Swanson³

et al. 2007

Cancer Research

104

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MUC1 is a heterodimeric transmembrane glycoprotein that is overexpressed and aberrantly glycosylated in ductal adenocarcinomas. Differential phosphorylation of the MUC1 cytoplasmic tail (MUC1CT) has been associated with signaling events that influence the proliferation and metastasis of cancer cells. We identified a novel tyrosine phosphorylation site (HGRYVPP) in the MUC1CT by mass spectrometric analysis of MUC1 from human pancreatic adenocarcinoma cell lines. Analyses in vitro and in vivo showed that plateletderived growth factor receptor B (PDGFRB) catalyzed phosphorylation of this site and of tyrosine in the RDTYHPM site. Stimulation of S2-013.MUC1F cells with PDGF-BB increased nuclear colocalization of MUC1CT and B-catenin. PDGF-BB stimulation had no significant effect on cell proliferation rate; however, it enhanced invasion in vitro through Matrigel and in vivo tumor growth and metastases. Invasive properties of the cells were significantly altered on expression of phosphorylation-abrogating or phosphorylation-mimicking mutations at these sites. We propose that interactions of MUC1 and PDGFRB induce signal transduction events that influence the metastatic properties of pancreatic adenocarcinoma. [Cancer Res 2007;67(11):5201-10]

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Section: Resultsmentioning

confidence: 99%

“…Panc1 was obtained from the American Type Culture Collection. S2-013 is a cloned subline of a human pancreatic tumor cell line (SUIT-2) derived from a liver metastasis (23). Armenian Hamster monoclonal antibody (mAb) CT2 against the MUC1CT was kindly provided by Dr. Sandra J. Gendler (Mayo Clinic, Scottsdale, AZ).…”

Section: Methodsmentioning

confidence: 99%

Platelet-Derived Growth Factor Receptor β–Mediated Phosphorylation of MUC1 Enhances Invasiveness in Pancreatic Adenocarcinoma Cells

Singh

Wen

Swanson³

et al. 2007

Cancer Research

104

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“…The STR profile also showed that they were novel cell lines and free from cell line cross-contamination. The expression of cytokeratin, CA19-9 and CEA (33)(34)(35), and tumorigenicity in mice indicated that they were pancreatic cancer cells. Moreover, the corresponding cell line xenograft tumors preserved similar pathological profiles and differentiation compared with their clinical samples and human primary tumors, which suggested that these low passage tumor cells maintained the clinical characteristics of pancreatic carcinoma, which could represent pancreatic tumor models both in vitro and in vivo, and help in translation of clinical information.…”

Section: Discussionmentioning

confidence: 99%

Intrinsic gemcitabine resistance in a novel pancreatic cancer cell line is associated with cancer stem cell-like phenotype

Fu²,

Ouyang³

et al. 2011

Int J Oncol

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Abstract. Pancreatic ductal adenocarcinoma (PDA) remains one of the most lethal malignancies in the world, often diagnosed at an advanced stage, resistant to conventional chemotherapy and having high invasive and metastatic potential. The mechanism of drug resistance of PDA is still not clear. In the present study, we established two novel pancreatic cancer cell lines PAXC-002 and PAXC-003 from human primary xenograft models. The cell lines were characterized by morphology, karyotype, pancreatic cancer marker and short tandem repeat (STR) analysis, and growth kinetics and tumorigenicity. The in vitro anti-proliferation test revealed that PAXC-002 cell was intrinsically resistant to the standard of care chemotherapy-gemcitabine, compared with that of PAXC-003 and other widely used pancreatic cancer cell lines. Interestingly, the gemcitabine resistant PAXC-002 cell line was more potent in forming colonies in 3-Dimensional matrigel culture conditions and had a higher percentage of CD133 positive cells, which is recognized as a cancer stem cell marker, compared to the gemcitabine-sensitive PAXC-003 cell line. In this study, we present two novel pancreatic cancer cell lines which could be used for gemcitabine resistance investigation, mechanism identification of pancreatic cancer and anticancer drug screening. The preliminary data indicate that the drug resistance of pancreatic carcinoma cells is associated with a cancer stem cell-like phenotype.

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“…The first, Panc-1, is a poorly differentiated human pancreatic adenocarcinoma cell line that expresses low levels of endogenous MUC1 and relatively low levels of other glycoproteins (37). The second, S2-013, is a moderately differentiated human pancreatic tumor cell line that is known to express O-glycosylated mucin-like proteins, including low levels of endogenous MUC1 (38).…”

Section: Transfection Of Cell Lines and Expression Of Muc1 Deletionmentioning

confidence: 99%

Nuclear Association of the Cytoplasmic Tail of MUC1 and β-Catenin

Wen

Caffrey

Wheelock

et al. 2003

Journal of Biological Chemistry

163

166

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MUC1, an integral membrane mucin associated with the metastatic phenotype, is overexpressed by most human carcinoma cells. The MUC1 cytoplasmic tail (CT) is postulated to function in morphogenetic signal transduction via interactions with Grb2/Sos, c-Src, and ␤-catenin. We investigated intracellular trafficking of the MUC1 CT, using epitope-tagged constructs that were overexpressed in human pancreatic cancer cell lines S2-013 and Panc-1. The MUC1 CT was detected at the inner cell surface, in the cytosol, and in the nucleus of cells overexpressing MUC1. Fragments of the MUC1 CT were associated with ␤-catenin in both cytoplasm and nuclei. Overexpression of MUC1 increased steady state levels of nuclear ␤-catenin but decreased nuclear levels of plakoglobin (␥-catenin). There was no detectable association between plakoglobin and the MUC1 CT. Coimmunoprecipitation experiments revealed that the cytoplasmic and nuclear association of MUC1 CT and ␤-catenin was not affected by disruption of Ca 2؉ -dependent intercellular cadherin interactions. These results demonstrate nuclear localization of fragments of MUC1 CT in association with ␤-catenin and raise the possibility that overexpression of the MUC1 CT stabilizes ␤-catenin and enhances levels of nuclear ␤-catenin during disruption of cadherin-mediated cell-cell adhesion.Human MUC1 is a large, type I transmembrane protein normally expressed on the apical surface of ductal epithelia (1). Full-length MUC1 is synthesized as a single polypeptide chain, which undergoes an early proteolytic cleavage (probably in the endoplasmic reticulum) creating two subunits that remain associated during its post-translational processing and transport to the cell surface (2). The larger of the two fragments contains most of the extracellular domain, including the signal sequence and a tandem repeat domain (3-5). The smaller subunit contains a short extracellular domain, transmembrane domain, and cytoplasmic tail (CT), 1 which are highly conserved across species (88% identity with murine transmembrane and CT sequence) (6). The function of MUC1 is partially elucidated for normal and transformed cells. The extracellular fragment plays a significant role in configuring the adhesive and antiadhesive properties of cells and is believed to contribute to the establishment of molecular structures that protect the cell surface in the relatively harsh environment encountered by different ductal epithelia (7). However, the function of the intracellular portion of the MUC1 cytoplasmic tail (CT) is not known. Indirect evidence suggests that the MUC1 CT is involved in signal transduction, as it contains potential docking sites for Grb2/Sos and ␤-catenin, and can be phosphorylated by GSK-3␤, c-Src, EGFR, and PKC-␦ (7-16). This, together with the general transmembrane structure of the MUC1 molecule, suggests a potential role in morphogenetic signaling; however, little is known about mechanisms by which the MUC1 CT functions in this capacity, and nothing has been reported with regard to the relationship between...

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Correlation between CA19‐9 production in vitro and histological grades of differentiation in vivo in clones isolated from a human pancreatic cancer cell line (SUIT‐2)

Cited by 49 publications

References 13 publications

Platelet-Derived Growth Factor Receptor β–Mediated Phosphorylation of MUC1 Enhances Invasiveness in Pancreatic Adenocarcinoma Cells

Platelet-Derived Growth Factor Receptor β–Mediated Phosphorylation of MUC1 Enhances Invasiveness in Pancreatic Adenocarcinoma Cells

Intrinsic gemcitabine resistance in a novel pancreatic cancer cell line is associated with cancer stem cell-like phenotype

Nuclear Association of the Cytoplasmic Tail of MUC1 and β-Catenin

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