Sponge aggregation factor: In situ localization by fluorescent monoclonal antibody techniques
| Autor: | Werner E.G. Müller, Monika Gramzow, August Dorn, Renate Steffen |
|---|---|
| Rok vydání: | 1986 |
| Předmět: |
chemistry.chemical_classification
biology medicine.drug_class Glycoconjugate Binding protein Cell Lectin Cell Biology Monoclonal antibody biology.organism_classification Biochemistry Fluorescence Molecular biology Sponge medicine.anatomical_structure chemistry medicine biology.protein Antibody Molecular Biology |
| Zdroj: | Journal of Cellular Biochemistry. 31:251-258 |
| ISSN: | 0730-2312 |
| DOI: | 10.1002/jcb.240310402 |
| Popis: | The aggregation factor (AF) from sponges mediates a heterophilic interaction of homologous cells. Applying electron microscopical means, we succeeded only very rarely in identifying the 90 S AF particle in tissue sections from Geodia cydonium. By means of a fluorescent antibody technique, we have now localized the cell binding domain of the AF in situ. Previous studies in this laboratory have led to the identification of the 47-kDa cell binding protein of the AF, using the monoclonal antibody (mab) 5D2-D11 [Gramzow M, Bachmann M, Zahn RK, Uhlenbruck G, Dorn A, Muller WEG, J Cell Biol, 102: 1344-1349, 1986]. This mab and mab 7D5, directed against a 92-kDa protein in the AF complex, were chosen for the fluorescent studies. By using mab 5D2-D11, the plasma membranes of cells from different regions in the sponge could be brightly stained. However, mab 7D5 reacted only very weakly with the sponge surfaces. By applying the immuno-blotting technique it was furthermore demonstrated that the cell binding protein is present both in the associated form with AF complex and in a free state. Moreover, it was established that the 47-kDa binding protein is not present in homologous glycoconjugates, lectin, or collagen; these components are known to be involved in cell-matrix interaction. |
| Databáze: | OpenAIRE |
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