Margaret M Lotz

Learn More
Cell-substratum adhesion strengths have been quantified using fibroblasts and glioma cells binding to two extracellular matrix proteins, fibronectin and tenascin. A centrifugal force-based adhesion assay was used for the adhesive strength measurements, and the corresponding morphology of the adhesions was visualized by interference reflection microscopy.(More)
In this study, the putative laminin receptor function of the a6ß4 integrin was assessed. For this purpose, we used a human cell line, referred to as clone A, that was derived from a highly invasive, colon adenocarcinoma. This cell line, which expresses the a6ß4 integrin, adheres to the ES and not to the PI fragment of laminin. The adhesion of clone A cells(More)
The tx6~l integrin is expressed on the mac-rophage surface in an inactive state and requires cellular activation with PMA or cytokines to function as a laminin receptor In the present study, the role of the ix6 subunit cyto-plasmic domain in ot6/51 integrin activation was examined. The use of P388D1 cells, an ct6-integrin deficient macrophage cell line,(More)
Cell-substratum adhesion strengths have been quantified using fibroblasts and glioma cells binding to two extracellular matrix proteins, fibronec-tin and tenascin. A centrifugal force-based adhesion assay was used for the adhesive strength measurements , and the corresponding morphology of the adhesions was visualized by interference reflection micros-copy.(More)
  • 1