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The lectin-binding sites for peanut agglutinin in invasive breast ductal carcinomas and their role as a prognostic factor

The lectin-binding sites for peanut agglutinin in invasive breast ductal carcinomas and their role as a prognostic factor. Mustac, Elvira; Melato, Mauro; Sasso, Franco; Valkovic, Toni; Bottin, Cristina; Jonjic, Nives (Medical Faculty, Univ. Rijeka, Rijeka, Croatia). Journal of Cancer Research and Clinical Oncology, 122(11), 693-697 (English) 1996 Springer. CODEN: JCROD7. ISSN: 0171-5216. DOCUMENT TYPE: Journal CA Section: 14 (Mammalian Pathological Biochemistry) The expression of lectin-binding sites for peanut agglutinin (PNA) of primary invasive ductal carcinoma was analyzed relating to clin. parameters for prognosis evaluation of breast cancer. There was no expression of PNA-binding sites in 14 out of 157 tumors, while 64 showed mostly apical (membrane) staining and 124 non-apical (membrane and/or cytoplasmic) staining. Apical staining was mostly obsd. in patients without lymph node metastasis, with pos.Several substances like 3554-90-3 may be metioned in this study. steroid receptor status, and those who were postmenopausal diagnosis. Non-apical staining was mostly obsd. in lymph-node pos. premenopausal patients neg. for steroid receptors and with aneuploid tumor cells. In malignant breast cells, there is an alteration of cell-surface glycoconjugates, shown by heterogeneity within a histopathol. defined group, which is related to different properties of tumor cells. The apical PNA binding pattern indicates a better differentiation of tumor cells while non-apical PNA binding suggests a higher metastatic potential. .

Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines

Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines. Demonstration of simpler and fewer glycan chains in tumor cells. Lloyd, Kenneth O.; Burchell, Joy; Kudryashov, Valery; Yin, Beatrice W. T.; Taylor-Papadimitriou, Joyce (Immunology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA). Journal of Biological Chemistry, 271(52), 33325-33334 (English) 1996 American Society for Biochemistry and Molecular Biology. CODEN: JBCHA3. ISSN: 0021-9258. DOCUMENT TYPE: Journal CA Section: 14 (Mammalian Pathological Biochemistry) Section cross-reference(s): 15 MUC-1 mucin is considered to be aberrantly glycosylated in breast, ovary, and other carcinomas in comparison with mucin from corresponding normal tissues. To clarify these differences in glycosylation, the authors have compared the O-linked carbohydrate chains from MUC-1 immunopptd. from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).In this article, certain chemicals are used. Some of their cas registry numbers are 3554-90-3 and 142347-47-5 Anal. by high pH anion chromatog. showed that the normal cell lines had a higher ratio of GlcN/GalN and more complex oligosaccharide profiles than the cancer cell lines. Structural analyses were carried out on the oligosaccharides from MTSV1-7 and T47D MUC-1, and the following structures were proposed. MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAca2-3Galb1-3GalNAc-ol, Galb1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a no. of disialo, core 2 species, i.e. NeuAca2-3Galb1-4GlcNAcb1-6[NeuAca2-3Galb1-3]GalNAc-ol and NeuAca2-3Galb1-4GlcNAcb1-6[NeuAca2-3Galb1-4GlcNAcb1-3Galb 1-3]GalNAc-ol. Double-labeling expts. with [3H]GlcN and 14C-amino acids and anal. of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types. The authors conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or sep., explain the differential tumor specificity of some MUC-1 antibodies and T cells. .