Oligosaccharide Mimics Containing Galactose and Fucose Specifically Label Tumour Cell Surfaces and Inhibit Cell Adhesion to Fibronectin

ChemBioChem ◽  
2005 ◽  
Vol 6 (2) ◽  
pp. 422-431 ◽  
Author(s):  
Evelyn Y.-L. Kim ◽  
Claas Gronewold ◽  
Amitava Chatterjee ◽  
Claus-Wilhelm von der Lieth ◽  
Christian Kliem ◽  
...  



2002 ◽  
Vol 115 (12) ◽  
pp. 2581-2590 ◽  
Author(s):  
Françoise Coussen ◽  
Daniel Choquet ◽  
Michael P. Sheetz ◽  
Harold P. Erickson

Previous studies have shown that small beads coated with FN7-10, a four-domain cell adhesion fragment of fibronectin, bind to cell surfaces and translocate rearward. Here we investigate whether soluble constructs containing two to five FN7-10 units might be sufficient for activity. We have produced a monomer, three forms of dimers, a trimer and a pentamer of FN7-10,on the end of spacer arms. These oligomers could bind small clusters of up to five integrins. Fluorescence microscopy showed that the trimer and pentamer bound strongly to the cell surface, and within 5 minutes were prominently localized to actin fiber bundles. Monomers and dimers showed only diffuse localization. Beads coated with a low concentration (probably one complex per bead) of trimer or pentamer showed prolonged binding and rearward translocation, presumably with the translocating actin cytskeleton. Beads containing monomer or dimer showed only brief binding and diffusive movements. We conclude that clusters of three integrin-binding ligands are necessary and sufficient for coupling to and translocating with the actin cytoskeleton.





Development ◽  
1991 ◽  
Vol 111 (4) ◽  
pp. 1021-1028 ◽  
Author(s):  
C. Hashimoto ◽  
S. Gerttula ◽  
K.V. Anderson

Formation of the Drosophila embryo's dorsal-ventral pattern requires the maternal product of the Toll gene. DNA sequence and genetic analyses together suggested that the Toll gene product is a transmembrane protein which communicates information from an extracytoplasmic compartment to the cytoplasm. Using antibodies as probes, we show that the Toll protein is a 135 × 10(3) Mr glycoprotein which is tightly associated with embryonic membranes. During the syncytial stage when dorsal-ventral polarity is established, the maternal Toll protein is associated with the plasma membrane around the entire embryo. During later embryonic stages, the Toll protein is expressed zygotically on many cell surfaces, possibly to promote cell adhesion. The plasma membrane localization of the Toll protein in the syncytial embryo suggests that transmembrane signaling from the extracellular perivitelline space to the cytoplasm is required for establishment of the embryonic dorsal-ventral pattern.



Pathology ◽  
2003 ◽  
Vol 35 (1) ◽  
pp. 50-55
Author(s):  
Paul J. Neeson ◽  
Peter J. Thurlow ◽  
Gary P. Jamieson ◽  
Chris Bradley


Author(s):  
Katja M. Fisch ◽  
J��rg Haier


1998 ◽  
Vol 17 (2) ◽  
pp. 71-82 ◽  
Author(s):  
Josef Smolle

Objective:To develop an interpretation procedure which estimates simulation parameters (tumour cell motility, tumour cell adhesion, autocrine and paracrine growth control, stroma destruction) of simulated patterns solely based on morphometric features of the morphologic pattern.Methods:A cellular automaton computer simulation program was developed which produces morphologic patterns by growth of a seed of tumour cells. At the beginning of each simulation run certain simulation parameters are assigned to the tumour cells. After the run has been completed, the resulting pattern is evaluated by a set of morphometric features. Simulation parameters and resulting morphometric features of 27,800 simulations were stored in a database and were used for the evaluation of potential relationships.Results:Correlation analysis showed highly significant correlations between morphometric features on the one hand and the preset simulation parameters (tumour cell motility, tumour cell adhesion, autocrine and paracrine growth control, stroma destruction) on the other. Correlation coefficients, however, varied from 0.72 to 0.99. When only one simulation parameter varied while all others were kept constant, morphometric features yielded a highly reliable estimate of the particular simulation parameter. When variability was extended to 4 simulation parameters, morphometric features were less effective in estimating the setting of the parameters. Though in all patterns tested several possible simulation parameter constellations could be ruled out, morphometric features were usually compatible with more than one set of simulation parameters thus preventing a straightforward interpretation.Conclusions:Though simulation parameters significantly and reproducibly influence the resulting morphologic pattern as characterized by morphometric features, estimates of the simulation parameters based on morphometric features yield equivocal results.



1981 ◽  
Vol 60 (3) ◽  
pp. 3P-3P ◽  
Author(s):  
Karol Sikora


1996 ◽  
Vol 74 (11) ◽  
pp. 1762-1766 ◽  
Author(s):  
EA Price ◽  
DR Coombe ◽  
JC Murray


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