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  • Life and Medical Sciences  (2)
  • Cell separation  (1)
  • Wiley-Blackwell  (3)
  • American Chemical Society
  • Oxford University Press
  • 1995-1999  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Immunogold labeling of oncogenic and tumor related proteins (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 31 (1995), S. 159-173 
    Details
    ISSN: 1059-910X
    Keywords: Immunogold ; Electron microscopy (EM) ; Oncogene ; Mos ; Met ; Ski ; Muc1 ; Mucin ; Immunocytochemistry ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: Immunogold labeling electron microscopy technique has been used to study the ultrastructural localization of oncogenic proteins: Mos, Met, Ski, and the tumor-associated protein, Muc1, as well as their relationship with other tumor-related proteins. By pre- and postembedding immunogold labeling electron microscopy techniques, we showed that the Mos protein pp39mos colocalized with microtubule bundles, suggesting that microtubulin or microtubule-associated protein(s) may be the substrate of Mos. Met protein was labeled at the microvilli of the lumen that are formed in cultured T47D cells, implying its potential involvement in lumen formation. Ski localization experiments revealed a unique globular structure “Ski body” that is present inside the nucleus of interphase chicken embryo fibroblast infected with Ski cDNA FB29 and FB2-29. Ski bodies were also found scattered in the cytoplasm of metaphase FB29 and FB2-29 Ski expressing chicken embryo fibroblasts. In T47D cells, tumor-associated protein Muc1 was associated with both the plasma membrane and the membranes of secretory vesicles in the cytoplasm. In MUC1 infected NIH3T3 cells, however, labeling showed that in addition to the plasma membrane and the membranes of secretory vesicles, some Muc1 gold spheres were seen inside the secretory vesicles, suggesting that the subcellular localization of the protein may vary in different cell types. © 1995 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070310207
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  • 2
    Electronic Resource
    Electronic Resource
    Standardized characterization of gene expression in human colorectal epithelium by two-dimensional electrophoresis (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 2842-2848 
    Details
    ISSN: 0173-0835
    Keywords: Colonic neoplasms ; Rectal neoplasms ; Two-dimensional polyacrylamide gel electrophoresis ; Cell separation ; Antibodies' monoclonal diagnostic use ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: New diagnostic and prognostic markers are needed in colorectal cancer. They can be found by differential analysis at DNA, RNA or protein level. The accuracy of phenotypic comparisons of tumor and normal tissues depends on the purity of the samples. We present an effective method to identify and isolate proteins that are differentially expressed under altered conditions, and a two-dimensional reference protein map of the normal human colonic epithelium Normal colonic mucosa, primary tumors and liver metastases were prepared in the operating room. After washing in an ice-cold medium containing protease inhibitors, crypts were isolated by mechanical preparation without using metalloproteinases. Epithelial cells were then selected using Ber-EP4 Dynabeads. The samples were denaturated before processing for immobilized pH gradient two-dimensional polyacrylamide gel electrophoresis according to SWISS-2DPAGE standards. The samples contained more than 95% epithelial cells as confirmed by fluorescence-activated cell sorting using pan-anticytokeratin antibodies. Cell surfaces were not damaged, as assessed by scanning electronic microscope. A protein reference map of the normal colonic epithelium was defined. Using gel matching, N-terminal sequencing and/or immunoblotting techniques, 60 polypeptides - including proteins specifically expressed in colorectal epithelium - have now been identified. This reproducible method of sample preparation permits the comparison of protein patterns found in various pathological states with the present reference map (http://www.expasy.ch). Some of these patterns might provide diagnostic or prognostic markers, or even molecular targets for therapy in the future.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181520
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular evolution of the vertebrate immune system (1997)
    New York, NY : Wiley-Blackwell
    BioEssays 19 (1997), S. 777-786 
    Details
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Adaptive immunity is unique to the vertebrates, and the molecules involved (including immunoglobulins, T cell receptors and the major histocompatibility complex molecules) seem to have diversified very rapidly early in vertebrate history. Reconstruction of gene phylogenies has yielded insights into the evolutionary origin of a number of molecular systems, including the complement system and the major histocompatibility complex (MHC). These analyses have indicated that the C5 component of complement arose by gene duplication prior to the divergence of C3 and C4, which suggests that the alternative complement pathway was the first to evolve. In the case of the MHC, phylogenetic analysis supports the hypothesis that MHC class II molecules evolved before class I molecules. The fact that the MHC-linked proteasome components that specifically produce peptides for presentation by class I MHC appear to have originated before the separation of jawed and jawless vertebrates suggests that the MHC itself may have been present at this time. Immmune system gene families have evolved by gene duplication, interlocus recombination and (in some cases) positive Darwinian selection favoring diversity at the amino acid level.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bies.950190907
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