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  • 1
    Electronic Resource
    Electronic Resource
    Mimic 1 of MUC1 (1998)
    [s.l.] : Nature Publishing Company
    Nature biotechnology 16 (1998), S. 236-237 
    Details
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] The relationship between tumor immunity and autoimmunity is a complex one. If anti-tumor immune responses are focused on molecules expressed on tumors that could be considered autoantigens, is their capacity to affect tumor rejection compromised by mechanisms that prevent autoimmunity? Could those ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nbt0398-236
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular characterization of the large heavily glycosylated domain glycopeptide from the rat small intestinal Muc2 mucin (1996)
    Springer
    Glycoconjugate journal 13 (1996), S. 823-831 
    Details
    ISSN: 1573-4986
    Keywords: mucin ; rat small intestine ; sulfated oligosaccharides ; mmunolocalization ; goblet cell ; Muc2
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The largest high-glycosylated domain, glycopeptide A, of the ‘insoluble’ mucin complex of the rat small intestine has earlier been purified and characterized (Carlstedtet al., 1993,J Biol Chem 268: 18771–81). A rabbit antiserum raised against deglycosylated glycopeptide A was used to clone part of a mucin showing homology to the human MUC2 mucin (Hanssonet al., 1994,Biochem Biophys Res Commun 198: 181–90). This serum specifically stained goblet cells (paranuclear) in the mouse small intestine. The size of the coding sequence of glycopeptide A was estimated by using reversed transcriptase PCR of mRNA from an inbred rat strain (GOT-W) using primers in the unique central and C-terminal parts of the proposed rat Muc2 sequences. The PCR and Southern blot of the PCR products showed a fragment of about 5.5 kb corresponding to about 1700 amino acids when the known Cys-rich sequences used for the primers were subtracted. This is slightly larger than the size estimated earlier by biochemical studies. The mRNA encoding the rat Muc2 was slightly smaller than the mRNA encoding the human MUC2 in a colorectal cell line. Although the size of glycopeptide A estimated from biochemical results and by PCR is not identical, the results obtained here further support that the ‘insoluble’ mucin of the rat small intestine is encoded by the Muc2 gene. Most of the oligosaccharides in glycopeptide A were either neutral (40%) or sialylated (40%). The remaining ones were sulfated with the sulfate group attached to C-6 ofN-acetylglucosamine linked to C-6 of theN-acetylgalactosaminitol as revealed by tandem mass spectrometry of the perdeuteroacetylated oligosaccharides. Eighteen oligosaccharides were found of which fourteen were characterized and found to be mostly novel. Our findings thus expand the current knowledge of the core peptide of the rat intestinal goblet cell mucin and provide a relatively complete picture of the glycosylation of a defined mucin domain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00702346
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  • 3
    Electronic Resource
    Electronic Resource
    Active proteinase inhibitors associated with human breast epithelial cells (1984)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 26 (1984), S. 157-167 
    Details
    ISSN: 0730-2312
    Keywords: proteinase inhibitors ; alpha-1-antichymotrypsin ; breast epithelial cells ; matrix protection ; gp 68 ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The major glycoproteins synthesized by human breast epithelial cells have been characterized [6,8]. The most consistently observed and prominent component in supernatants of organ cultures of breast surgical specimens and of MCF-7 cells was gp 68 which has been immunologically identified as α-1-antichymotrypsin (Achy). In the present study we demonstrate that this glycoprotein can form an irreversible complex with chymotrypsin, which indicates that it is a functional inhibitor. The 14C-glucosamine-labeled gp 68 forms a stable, 88,000-dalton. enzyme-inhibitor complex with chymotrypsin. The molecule is secreted continuously for 9 days into a chemically defined, serum-free medium. In addition to the de novo synthesized inhibitor, another component is adsorbed from fetal bovine scrum and subsequently released into serum-free medium. This component also forms an irreversible, 88,000-dalton complex with enzyme. The observations establish that two types of inhibitors are associated with human breast epithelial cells, one actively synthesized and the other derived from serum. Both of these molecules may have significant roles in stabilizing cell surface components and in protecting extracellular matrices from untimely degradation.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240260304
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  • 4
    Electronic Resource
    Electronic Resource
    The synthesis of a proteinase inhibitor, α-1-antichymotrypsin, by human breast epithelial cells (1981)
    New York, NY : Wiley-Blackwell
    Journal of Supramolecular Structure and Cellular Biochemistry 17 (1981), S. 69-77 
    Details
    ISSN: 0275-3723
    Keywords: human breast epithelia ; glycoproteins ; proteinase inhibitors ; organ culture ; α-1-antichymotrypsin ; breast adenocarcinoma ; glandular structure ; Chemistry ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The synthesis and release of glycoproteins were studied in organ cultures of human breast surgical specimens and in established breast epithelial cell lines, MCF-7 and MDA-MB-231. Biosynthesis was monitored by the incorporation of 14C-glucosamine. Labeled macromolecules in the culture supernatants were analyzed by biochemical and immunological techniques. One to 8% of the labeled glycoproteins from benign breast and infiltrating ductal carcinoma specimens was precipitated by antibodies produced against human serum 7α-1-antichymotrypsin. Twelve percent of the total glycoproteins from the culture supernatants of the MCF-7 cell line was identified as α-1-antichymo-trypsin. Both the normal serum and the human breast epithelia-derived proteinase inhibitor can be resolved into similar subclasses by two-dimensional gel electrophoresis. MDA-MB-231 and MCF-7 cells which were extensively washed with EDTA, serum-free medium, and phosphate-buffered saline retain this proteinase inhibitor on their cell surfaces. Three to 4% of the total cell-surface iodinated components was immunoprecipitated by these specific antibodies. Since α-1-antichymotrypsin is a potent inhibitor of neutral proteinases such as cathepsin G, the demonstration of its synthesis by benign and malignant breast epithelial cells is of considerable interest. This glycoprotein may represent the epithelia's own protective shield of cell surface components and the cell's attempt to moderate the effects of invading leukocytes. In addition, it may play a regulatory role in the maintenance of three-dimensional glandular structures.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jsscb.380170108
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    Paper (German National Licenses)
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