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Quantitative Micro-Adhesion Assay on Polystyrene Matrices

  • F.-G. Hanisch
  • F. Dressen
  • G. Uhlenbruck
Part of the Springer Laboratory book series (SLM)

Abstract

The interaction of cell surface carbohydrates as carriers of biological information and their complementary carbohydrate binding proteins plays an important role in several cell-cell recognition processes. Receptor-mediated endocytosis of asialoglycoproteins after recognition by hepatic binding protein, homing of cells like the hematopoetic stem cells or lymphocytes, egg-sperm binding, interactions among cells of the immune system (Brandley and Schnaar 1986), controlling of cellular proliferation (Lotan et al. 1985), the recruitment of neutrophils to sites of inflammation (Walz et al. 1990), and myelin formation (Zanetta et al. 1990) are examples of lectin-carbohydrate interactions in higher vertebrates. Moreover, glycoconjugate-lectin interactions have been postulated to participate in the establishment of metastatic lesions (Lotan and Raz 1988). To investigate the expression of lectin receptors on eukaryontic cells, several assays for demonstrating cell-binding to immobilized glycoconjugates have been developed. Cell adhesion to glycolipids immobilized on silica gel thin layer chromatography plates or on PVC plates was examined by Swank-Hill (Swank-Hill et al. 1987) and Blackburn (Blackburn and Schnaar 1983; Blackburn et al. 1986), respectively, while studies with glycoproteins were performed on glycosylated derivatives of polyacrylamide gels (Schnaar 1984) or on nitrocellulose as matrix (Lochner et al. 1990).

Keywords

Cell Binding Human Breast Carcinoma Cell Blue Formazan Chang Liver Cell Relative Centrifugal Force 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1993

Authors and Affiliations

  • F.-G. Hanisch
  • F. Dressen
  • G. Uhlenbruck

There are no affiliations available

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