Metabolic Engineering of Reactive Cell Surfaces for Controlled Cell Adhesion

2001 ◽  
Author(s):  
Carolyn R. Bertozzi
Keyword(s):  
Cell Adhesion ◽  
Metabolic Engineering ◽  
Cell Surfaces ◽  
Reactive Cell

Trimers of the fibronectin cell adhesion domain localize to actin filament bundles and undergo rearward translocation

2002 ◽  
Vol 115 (12) ◽  
pp. 2581-2590 ◽  
Author(s):  
Françoise Coussen ◽  
Daniel Choquet ◽  
Michael P. Sheetz ◽  
Harold P. Erickson
Keyword(s):  
Cell Adhesion ◽  
Fluorescence Microscopy ◽  
Cell Surface ◽  
Actin Cytoskeleton ◽  
Fiber Bundles ◽  
Cell Surfaces ◽  
Actin Fiber ◽  
Filament Bundles ◽  
Necessary And Sufficient ◽  
Small Clusters

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.

Plasma membrane localization of the Toll protein in the syncytial Drosophila embryo: importance of transmembrane signaling for dorsal-ventral pattern formation

Development ◽  
1991 ◽  
Vol 111 (4) ◽  
pp. 1021-1028 ◽  
Author(s):  
C. Hashimoto ◽  
S. Gerttula ◽  
K.V. Anderson
Keyword(s):  
Plasma Membrane ◽  
Cell Adhesion ◽  
Transmembrane Protein ◽  
Drosophila Embryo ◽  
Membrane Localization ◽  
Transmembrane Signaling ◽  
Perivitelline Space ◽  
Cell Surfaces ◽  
Plasma Membrane Localization ◽  
Promote Cell Adhesion

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.

scholarly journals Membrane domains of intestinal epithelial cells: distribution of Na+,K+-ATPase and the membrane skeleton in adult rat intestine during fetal development and after epithelial isolation.

1989 ◽  
Vol 109 (5) ◽  
pp. 2129-2138 ◽  
Author(s):  
H M Amerongen ◽  
J A Mack ◽  
J M Wilson ◽  
M R Neutra
Keyword(s):  
Cell Adhesion ◽  
Basolateral Membrane ◽  
Membrane Skeleton ◽  
Membrane Domain ◽  
Cell Surfaces ◽  
Adult Rat ◽  
Lateral Membrane ◽  
Epithelial Sheets ◽  
Lateral Cell ◽  
Fetal Intestine

The organization of the basolateral membrane domain of highly polarized intestinal absorptive cells was studied in adult rat intestinal mucosa, during development of polarity in fetal intestine, and in isolated epithelial sheets. Semi-thin frozen sections of these tissues were stained with a monoclonal antibody (mAb 4C4) directed against Na+,K+-ATPase, and with other reagents to visualize distributions of the membrane skeleton (fodrin), an epithelial cell adhesion molecule (uvomorulin), an apical membrane enzyme (aminopeptidase), and filamentous actin. In intact adult epithelium, Na+,K+-ATPase, membrane-associated fodrin, and uvomorulin were concentrated in the lateral, but not basal, subdomain. In the stratified epithelium of fetal intestine, both fodrin and uvomorulin were localized in areas of cell-cell contact at 16 and 17 d gestation, a stage when Na+,K+-ATPase was not yet expressed. These molecules were excluded from apical domains and from cell surfaces in contact with basal lamina. When Na+,K+-ATPase appeared at 18-19 d, it was codistributed with fodrin. Detachment of epithelial sheets from adult intestinal mucosa did not disrupt intercellular junctions or lateral cell contacts, but cytoplasmic blebs appeared at basal cell surfaces, and a diffuse pool of fodrin and actin accumulated in them. At the same time, Na+,K+-ATPase moved into the basal membrane subdomain, and extensive endocytosis of basolateral membrane, including Na+,K+-ATPase, occurred. Endocytosis of uvomorulin was not detected and no fodrin was associated with endocytic vesicles. Uvomorulin, along with some membrane-associated fodrin and some Na+,K+-ATPase, remained in the lateral membrane as long as intercellular contacts were maintained. Thus, in this polarized epithelium, interaction of lateral cell-cell adhesion molecules as well as basal cell-substrate interactions are required for maintaining the stability of the lateral membrane skeleton and the position of resident membrane proteins concentrated in the lateral membrane domain.

Cell adhesion molecules in Dictyostelium: Identification with monoclonal antibodies

1983 ◽  
Vol 41 ◽  
pp. 576-579
Author(s):  
S. H. Baronde ◽  
W. R. Springer
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecules ◽  
Cell Adhesion Molecules ◽  
Complex Problem ◽  
Cell Surfaces ◽  
Direct Role ◽  
Slime Molds ◽  
Cellular Slime ◽  
Eukaryotic Organisms ◽  
Multicellular Organisms

Cells in multicellular organisms occupy specific positions in relation to each other. This is brought about by a complex series of factors, one of which is believed to be the interaction of molecules on cell surfaces with those on other cells or the extracellular matrix. The molecules presumed to mediate these functions have been designated cell adhesion molecules and cell recognition molecules. The former indicates that they play a direct role in the adhesion process, while the latter indicates that they mediate the selectivity of adhesion. One molecule might serve both a recognition and an adhesion function but, given the complexity of cell surfaces, recognition and adhesion could also be separate, and possibly sequential, processes.We have chosen to study the problem of cell-cell adhesion in cellular slime molds because these relatively simple eukaryotic organisms have many properties that facilitate experimental work on this complex problem:

scholarly journals Fibronectin glycosylation modulates fibroblast adhesion and spreading.

1986 ◽  
Vol 103 (5) ◽  
pp. 1663-1670 ◽  
Author(s):  
G E Jones ◽  
R G Arumugham ◽  
M L Tanzer
Keyword(s):  
Cell Adhesion ◽  
Biological Functions ◽  
Cell Surfaces ◽  
Fibroblastic Cell ◽  
Cultured Fibroblasts ◽  
Fibroblast Adhesion ◽  
Coated Surfaces ◽  
Composite Data

The role of the carbohydrate residues of fibronectin concerning the specificities of that glycoprotein to interact with fibroblastic cell surfaces, gelatin, and heparin was examined. Tunicamycin was used to produce carbohydrate-depleted fibronectin; it was synthesized by cultured fibroblasts. Unglycosylated and glycosylated fibronectins were analyzed for their ability to bind gelatin and heparin, using affinity columns. Fibronectin-coated surfaces were used to quantitatively measure cell adhesion and spreading. The results showed that the lack of carbohydrates significantly increased the interaction of the protein with gelatin and markedly enhanced its ability to promote adhesion and spreading of fibroblasts. In contrast, the binding of fibronectin to heparin was not influenced by glycosylation. The composite data indicate that the Asn-linked oligosaccharides of fibronectin act as modulators of biological functions of the glycoprotein.

scholarly journals Cell sorting-out is modulated by both the specificity and amount of different cell adhesion molecules (CAMs) expressed on cell surfaces.

1989 ◽  
Vol 86 (18) ◽  
pp. 7043-7047 ◽  
Author(s):  
D. R. Friedlander ◽  
R. M. Mege ◽  
B. A. Cunningham ◽  
G. M. Edelman
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecules ◽  
Cell Sorting ◽  
Cell Adhesion Molecules ◽  
Cell Surfaces

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 ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Tumour Cell ◽  
Cell Surfaces
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