Changes in expression of a major sialoglycoprotein associated with ascites forms of a mammary adenocarcinoma

Howard, Susan C.; Sherblom, Anne P.; Chesnut, Robert W.; Carraway, Coralie A. Carothers; Carraway, Kermit L.

doi:10.1016/0304-4165(80)90055-0

Cited by 12 publications

(3 citation statements)

References 52 publications

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“…The cultured subline MAT-BIII has a lower level of Muc4/SMC expression compared with rat epithelial cells from lactating mammary gland. Interestingly, when we put the 13762 ascites cells in culture, we observed a downregulation of Muc4/SMC (63). The transmembrane subunit of Muc4/SMC acts as an intramembrane ligand for the receptor tyrosine kinase ErbB2 and potentiates its phosphorylation (64).…”

Section: Muc4/smc Erbb2 and Pea3 Are Up-regulated In 13762 Tumor Cementioning

confidence: 93%

PEA3 Transactivates the Muc4/Sialomucin Complex Promoter in Mammary Epithelial and Tumor Cells

Perez

Barco²,

Fernández

et al. 2003

Journal of Biological Chemistry

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Sialomucin complex (SMC, rat Muc4) is a heterodimeric glycoprotein composed of two subunits, the mucin component ascites sialoglycoprotein ASGP-1 and the transmembrane subunit ASGP-2, which is aberrantly expressed on the surfaces of a variety of tumor cells. Up-regulation of the Muc4/SMC gene in the 13762 sublines of the rat mammary adenocarcinoma correlates with the overexpression of transcription factor PEA3 and the receptor tyrosine kinase ErbB2. Here we report that PEA3 is capable of transactivating the Muc4/ SMC promoter in a dose-dependent manner via direct attachment to a PEA3 binding site. ERM and ER81, the other two members of the PEA3 subfamily of transcription factors, could not transactivate the Muc4/SMC promoter. Transcriptional activation of Muc4/SMC by PEA3 is potentiated by Ras and MEKK1 kinases. These data suggest that expression of PEA3 in mammary tumors leads to up-regulation of Muc4/SMC transcription, the gene product of which may contribute to the metastatic potential of mammary tumors.

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Section: Muc4/smc Erbb2 and Pea3 Are Up-regulated In 13762 Tumor Cementioning

confidence: 93%

PEA3 Transactivates the Muc4/Sialomucin Complex Promoter in Mammary Epithelial and Tumor Cells

Perez

Barco²,

Fernández

et al. 2003

Journal of Biological Chemistry

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“…The sialomucin ascites sialoglycoprotein-I (ASGP-1) is a major constituent of these ascites cells, comprising > 0.5 % of the total cell protein . In contrast, ASGP-1 is virtually absent when the ascites cells are grown in culture (Howard et al, 1980) or as solid tumours (Huggins et al, 1980). ASGP-1 can be extracted from membranes with guanidine hydrochloride (GdnHCl) or urea and purified on CsCl gradients .…”

Section: Introductionmentioning

confidence: 99%

Isolation and partial characterization of ascites sialoglycoprotein-2 of the cell surface sialomucin complex of 13762 rat mammary adenocarcinoma cells

Hull

Sheng

Vanderpuye

et al. 1990

Biochemical Journal

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Sialomucins are the dominant components of the cell surfaces of some carcinoma ascites cells and have been postulated to inhibit recognition of tumours by the immune system. The sialomucin ASGP-1 (ascites sialoglycoprotein-1) of the 13762 rat mammary adenocarcinoma is associated with the cell surface as a complex with a concanavalin-A-binding glycoprotein called ASGP-2. This sialomucin complex has been purified from ascites cell microvilli by extraction with Triton X-100 and CsCl density-gradient centrifugation. ASGP-1 (which has been purified previously) and ASGP-2 were dissociated in 6 M-guanidine hydrochloride and separated by gel filtration. The molecular mass of the undenatured detergent complex of ASGP-2, estimated by gel filtration and velocity sedimentation in Triton X-100, was 148 kDa. Since the apparent molecular mass by SDS/polyacrylamide-gel electrophoresis was about 120 kDa, ASGP-2 must be a monomer as extracted from the membrane. Studies of its chemical composition indicate that it contains about 45% carbohydrate by weight, including both mannose and galactosamine. Alkaline borohydride treatment of ASGP-2 converted approx. half of the N-acetylgalactosamine to N-acetylgalactosaminitol, demonstrating the presence of O-linked oligosaccharides. Analyses of mannose-labelled Pronase glycopeptides from ASGP-2 by lectin-affinity chromatography on concanavalin A and leucocyte-agglutinating phytohaemagglutinin suggested that 40% of the label was present in high-mannose/hybrid oligosaccharides, 20% in triantennary oligosaccharides substituted on the C-2 and C-4 mannose positions and 40% in tri- or tetra-antennary oligosaccharides substituted on C-2 and C-6. The presence of polylactosamine sequences on these oligosaccharides was suggested by lectin blots and by precipitation from detergent extracts with tomato lectin. From chemical analyses and lectin-affinity studies, we estimate that ASGP-2 contains four high-mannose and 13 complex N-glycosylated oligosaccharides, plus small amounts of polylactosamine and O-linked oligosaccharides. The presence of four different classes of oligosaccharides on this glycoprotein suggests that it will be an interesting model system for biosynthetic comparisons of the different glycosylation pathways.

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“…A further consideration may be that the comparison of CMT64 and selected lines was made by methods that are applicable to cultured cells, which may fail to express characteristics that are important in metastatic behaviour. Host factors can markedly influence surface protein composition as was seen between the ascites and cultured cells of each of the TA3 and 13762 cell lines (Howard et al, 1980). The basic characterization of the CMT64 and sublines pointed to host factor involvement in subcutaneous tumour growth and metastatic spread to the lungs .…”

Section: Comparison Of Cmt64 and Sublines Cmt167 And Cmti81mentioning

confidence: 99%

Cell surface properties of high‐ and low‐metastatic cell lines selected from a spontaneous mouse lung carcinoma

Steele¹,

Rowlatt²,

Sandall³

et al. 1983

Intl Journal of Cancer

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The surface oligosaccharide residues, glycoproteins and sialyl components of CMT64 lung carcinoma cells and high-metastatic sublines CMT167 and CMT181 have been studied in culture. (1) The total cellular sialic acid content did not differ appreciably between the three lines. However, the accessibility of surface sialyl groups, measured by metabolic incorporation of [3H]NAcmannosamine followed by neuraminidase hydrolysis, was decreased from 42% in CMT64 to 25% hydrolyzed in CMT181. (2) The major plasma membrane glycoproteins of the lines were radiolabelled by lactoperoxidase iodination, metabolic incorporation of [3H]fucose or labelling in the terminal sialyl residues by the NaIO4-NaB[3H]4 method and the labelled glycoproteins were analyzed by two-dimensional gel electrophoresis. Each labelling technique identified a complex pattern of glycoproteins including a prominently labelled group of high-molecular-weight acidic sialoglycoproteins: GP200/4.9-5.1 (apparent molecular weight X 10(-3)/pl of iodoprotein); GP150/5.1-5.6; GP130/5.0-5.6; GP110/5.0; GP100/4.8 and GP100/5.0-5.4. (3) The neuraminidase-susceptible glycoproteins on CMT64 and CMT181 were identified in the isoelectric focusing separation of the two-dimensional gel separation by the charge difference caused by desialylation. The glycoproteins most susceptible to neuraminidase were the high-molecular-weight acidic glycoproteins which showed marked charge heterogeneity: GP150/5.1-5.6, GP130/5.0-5.6; GP100/5.0-5.4 and GP100/4.8. (4) Using these procedures we did not detect modifications between CMT181 and CMT64 and we conclude that the cultured cells of the sublines do not display marked surface glycoprotein alterations that reflect their enhanced spontaneous metastatic potential.

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Changes in expression of a major sialoglycoprotein associated with ascites forms of a mammary adenocarcinoma

Cited by 12 publications

References 52 publications

PEA3 Transactivates the Muc4/Sialomucin Complex Promoter in Mammary Epithelial and Tumor Cells

PEA3 Transactivates the Muc4/Sialomucin Complex Promoter in Mammary Epithelial and Tumor Cells

Isolation and partial characterization of ascites sialoglycoprotein-2 of the cell surface sialomucin complex of 13762 rat mammary adenocarcinoma cells

Cell surface properties of high‐ and low‐metastatic cell lines selected from a spontaneous mouse lung carcinoma

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