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Tumor cytogenetics revisited: comparative genomic hybridization and spectral karyotyping (1997)

Ried, T. ; Liyanage, Marek ; du Manoir, Stan ; [et al.]

Springer

Journal of molecular medicine 75 (1997), S. 801-814

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ISSN: 1432-1440

Keywords: Key words Fluorescence in situ hybridization ; Comparative genomic hybridization ; Spectral karyotyping ; Chromosome aberrations ; Tumor progression

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Notes: Abstract Fluorescence in situ hybridization techniques allow the visualization and localization of DNA target sequences on the chromosomal and cellular level and have evolved as exceedingly valuable tools in basic chromosome research and cytogenetic diagnostics. Recent advances in molecular cytogenetic approaches, namely comparative genomic hybridization and spectral karyotyping, now allow tumor genomes to be surveyed for chromosomal aberrations in a single experiment and permit identification of tumor-specific chromosomal aberrations with unprecedented accuracy. Comparative genomic hybridization utilizes the hybridization of differentially labeled tumor and reference DNA to generate a map of DNA copy number changes in tumor genomes. Comparative genomic hybridization is an ideal tool for analyzing chromosomal imbalances in archived tumor material and for examining possible correlations between these findings and tumor phenotypes. Spectral karyotyping is based on the simultaneous hybridization of differentially labeled chromosome painting probes (24 in human), followed by spectral imaging that allows the unique display of all human (and other species) chromosomes in different colors. Spectral karyotyping greatly facilitates the characterization of numerical and structural chromosomal aberrations, therefore improving karyotype analysis considerably. We review these new molecular cytogenetic concepts, describe applications of comparative genomic hybridization and spectral karyotyping for the visualization of chromosomal aberrations as they relate to human malignancies and animal models thereof, and provide evidence that fluorescence in situ hybridization has developed as a robust and reliable technique which justifies its translation to cytogenetic diagnostics.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/s001090050169

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Interaction of lung surfactant protein a with alveolar macrophages (1993)

Ohmer-Schröck, Daniela ; Schlatterer, Christina ; Plattner, Helmut ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Microscopy Research and Technique 26 (1993), S. 374-380

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ISSN: 1059-910X

Keywords: C1q ; Calcium ; Specific binding ; SP-A ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Natural Sciences in General

Notes: We analyzed the binding mechanism of human recombinant lung surfactant protein A (SP-A) to rat alveolar macrophages using anti-SP-A antiserum and protein A coated onto gold particles. Results were compared with our recent data on binding and uptake of SP-A-coated colloidal gold particles. The rationale for the current approach was to avoid any possible steric effects on SP-A binding to the cell surface. Binding of unlabeled SP-A depends on the presence of calcium ions in the medium and involves a mannose-specific mechanism. Binding is partly inhibited by the collagenase-resistent fragment of SP-A, representing mainly the globular part of SP-A. Taken together, these facts indicate binding of SP-A via the carbohydrate binding site on the globular region of SP-A. On the other hand, a partial inhibition of SP-A binding by fragments of C1q (representing the collagenous region of C1q) indicates a second binding site for SP-A by the collagen-like portion to the C1q receptor of macrophages. We conclude that two different mechanisms are probably involved in SP-A binding to alveolar macrophages. Specificity of the binding was shown with fluorescein-labeled SP-A. Binding was inhibited by an excess of unlabeled SP-A. Binding and uptake of SP-A are seen only with alveolar macrophages and not with other macrophage populations isolated from rat, such as liver macrophages (Kupffer cells), resident peritoneal macrophages, and peritoneal macrophages activated by Corynebacterium parvum. Therefore, binding sites for SP-A occur exclusively on alveolar macrophages. In addition, the intracellular Ca2+ concentration of the lung macrophages was determined by using the fluorescent dye fura-2/AM. Intracellular [Ca2+] increased immediately after addition of SP-A. This indicates immediate activation of macrophages by SP-A. © 1993 Wiley-Liss, Inc.

Additional Material: 4 Ill.