Cell Surface Differentiation in the Embryonic Chick Retina

1981 ◽  
pp. 99-122 ◽  
Author(s):  
Joel B. Sheffield ◽  
Mark Lynch
Keyword(s):  
Cell Surface ◽  
Embryonic Chick ◽  
Chick Retina ◽  
Surface Differentiation

Quick freeze-deep etch analysis of microfilaments in the circumferential bundle of retinal pigmented epithelial cells M vitro

1986 ◽  
Vol 44 ◽  
pp. 160-161
Author(s):  
Ryuji Kodama ◽  
Goro Eguchi ◽  
Robert O. Kelley
Keyword(s):  
Epithelial Cells ◽  
Cell Surface ◽  
Embryonic Chick ◽  
Rpe Cells ◽  
Chick Retina ◽  
Lens Cell ◽  
Culture Environment ◽  
Retinal Pigmented Epithelial Cells

Pigmented epithelial cells from embryonic chick retina can transdifferentiate in vitro to express either pigmented (RPE) or lens cell (LC) phenotypes in response to alterations in the external culture environment. These observations suggest that the dedifferentiated phenotype of RPE cells is, at least, bipotential and that expression of either of two differentiated phenotypes is mediated by the cell surface and the associated cytoskeleton.

Functional partitioning of beta1 integrins revealed by activating and inhibitory mAbs

1997 ◽  
Vol 110 (21) ◽  
pp. 2647-2659 ◽  
Author(s):  
M.T. Cruz ◽  
C.L. Dalgard ◽  
M.J. Ignatius
Keyword(s):  
Cell Surface ◽  
Actin Cytoskeleton ◽  
Dermal Fibroblasts ◽  
The Other ◽  
Embryonic Chick ◽  
Cell Surfaces ◽  
Double Labeling ◽  
Focal Contacts ◽  
Functional Partitioning ◽  
Discrete Populations

Integrins exist in different activation states on the surfaces of cells. Addition of the proper signal, ligand, or antibody can alter the activation state of these molecules. We report here the identification of two immunocytochemically distinct populations of beta1 integrins on fixed embryonic chick dermal fibroblasts. One population, recognized by the integrin activating mAb TASC, localizes to discrete regions of the cell, most likely focal contacts. These integrins co-localize with other proteins, such as vinculin and F-actin, and their retention at these sites is dependent on the actin cytoskeleton. The other population, identified with the inhibitory mAb W1B10, is more evenly distributed throughout the cell surface, and its pattern remains unchanged after disruption of the actin cytoskeleton. Double labeling experiments using Fab fragments of TASC alongside whole W1B10 IgG revealed non-overlapping staining patterns. These results show that it is possible to visualize and study discrete populations of integrins on cell surfaces using two different antibodies. We hypothesize that these antibodies report differences in the distribution of receptors in two different states. A model is proposed describing the ligand independent recruitment of integrins based on these findings and results from other labs.

Cell surface differentiation of Chlamydomonas during gametogenesis

1974 ◽  
Vol 36 (2) ◽  
pp. 279-285 ◽  
Author(s):  
Robert J. McLean ◽  
R.Malcolm Brown
Keyword(s):  
Cell Surface ◽  
Surface Differentiation

scholarly journals Complement anaphylatoxin C3a is a potent inducer of embryonic chick retina regeneration

2013 ◽  
Vol 4 (1) ◽  
Author(s):  
Tracy Haynes ◽  
Agustin Luz-Madrigal ◽  
Edimara S. Reis ◽  
Nancy P. Echeverri Ruiz ◽  
Erika Grajales-Esquivel ◽  
...  
Keyword(s):  
Embryonic Chick ◽  
Potent Inducer ◽  
Retina Regeneration ◽  
Chick Retina ◽  
Anaphylatoxin C3a

The effect of neuraminidase- and ribonuclease-susceptible surface anionic groups on the aggregation of embryonic chick neural retina cells

1981 ◽  
Vol 51 (1) ◽  
pp. 229-240
Author(s):  
D.E. Maslow ◽  
J.P. Harlos
Keyword(s):  
Cell Surface ◽  
Surface Charge ◽  
Neural Retina ◽  
Heart Cells ◽  
Cellular Interactions ◽  
Embryonic Chick ◽  
Contact Behaviour ◽  
Negative Surface ◽  
Negative Surface Charge ◽  
Anionic Groups

The role of cell surface charge in cellular interactions has been the subject of conflicting reports. The major contribution to the net cell surface negativity of all mammalian cells studied is made by the sialic acid moieties of the surface glycoproteins, while ribonuclease-susceptible sites have been shown to contribute to the lesser extent on some cell types. Experiments were done to determine whether these anionic groups at the cell periphery affect the aggregation and sorting behaviour of embryonic chick neural retina cells when cultured alone or in combination with embryonic heart cells. The net negative surface charge density, as determined by cell electrophoretic mobility, of neuraminidase- or ribonuclease-treated cells was significantly decreased immediately after incubation with the enzymes, and the treatment with neuraminidase resulted in a reduction in the binding of colloidal iron hydroxide particles at the cell surface. Both enzymes caused reduced aggregate size in gyratory shaker cultures of neural retina and mixed cell suspensions, and fewer neural retina cells adherent to microtest plate surfaces, but no differences were seen in their histological appearance or sorting pattern in mixed shaker culture. The results indicate that the neuraminidase- and ribonuclease-susceptible groups at the periphery of embryonic neural retina cells play a role in some aspects of cell contact behaviour in ways other than reduction in net negative surface charge.

Calcium channels and GABA receptors in the early embryonic chick retina

1993 ◽  
Vol 24 (12) ◽  
pp. 1600-1614 ◽  
Author(s):  
Masayuki Yamashita ◽  
Yutaka Fukuda
Keyword(s):  
Calcium Channels ◽  
Gaba Receptors ◽  
Embryonic Chick ◽  
Chick Retina

scholarly journals PTP1B Modulates the Association of β-Catenin with N-cadherin through Binding to an Adjacent and Partially Overlapping Target Site

2002 ◽  
Vol 277 (51) ◽  
pp. 49989-49997 ◽  
Author(s):  
Gang Xu ◽  
Carlos Arregui ◽  
Jack Lilien ◽  
Janne Balsamo
Keyword(s):  
Amino Acids ◽  
Cell Surface ◽  
Tyrosine Phosphatase ◽  
Target Site ◽  
Target Domain ◽  
Chick Retina ◽  
Cell Permeable Peptide ◽  
A Cell ◽  
Relationship Of

The nonreceptor tyrosine phosphatase PTP1B associates with the cytoplasmic domain of N-cadherin and may regulate cadherin function through dephosphorylation of β-catenin. We have now identified the domain on N-cadherin to which PTP1B binds and characterized the effect of perturbing this domain on cadherin function. Deletion constructs lacking amino acids 872–891 fail to bind PTP1B. This domain partially overlaps with the β-catenin binding domain. To further define the relationship of these two sites, we used peptides to competein vitrobinding. A peptide representing the most NH2-terminal 8 amino acids of the PTP1B binding site, the region of overlap with the β-catenin target, effectively competes for binding of β-catenin but is much less effective in competing PTP1B, whereas two peptides representing the remaining 12 amino acids have no effect on β-catenin binding but effectively compete for PTP1B binding. Introduction into embryonic chick retina cells of a cell-permeable peptide mimicking the 8 most COOH-terminal amino acids in the PTP1B target domain, the region most distant from the β-catenin target site, prevents binding of PTP1B, increases the pool of free, tyrosine-phosphorylated β-catenin, and results in loss of N-cadherin function. N-cadherin lacking this same region of the PTP1B target site does not associate with PTP1B or β-catenin and is not efficiently expressed at the cell surface of transfected L cells. Thus, interaction of PTP1B with N-cadherin is essential for its association with β-catenin, stable expression at the cell surface, and consequently, cadherin function.

scholarly journals Cell-substratum adhesion in chick neural retina depends upon protein-heparan sulfate interactions.

1985 ◽  
Vol 100 (4) ◽  
pp. 1192-1199 ◽  
Author(s):  
G J Cole ◽  
D Schubert ◽  
L Glaser
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Neural Retina ◽  
Heparan Sulfate Proteoglycan ◽  
Retinal Cell ◽  
Sulfate Proteoglycan ◽  
Heparin Binding ◽  
Embryonic Chick ◽  
Retinal Cells ◽  
Inert Surfaces

Embryonic chick neural retina cells in culture release complexes of proteins and glycosaminoglycans, termed adherons, which stimulate cell-substratum adhesion when adsorbed to nonadhesive surfaces. Two distinct retinal cell surface macromolecules, a 170,000-mol-wt glycoprotein and a heparan sulfate proteoglycan; are components of adherons that can independently promote adhesion when coated on inert surfaces. The 170,000-mol-wt polypeptide contains a heparin-binding domain, as indicated by its retention on heparin-agarose columns and its ability to bind [3H]heparin in solution. The attachment of embryonic chick retinal cells to the 170,000-mol-wt protein also depends upon interactions between the protein and the heparan sulfate proteoglycan, since heparan sulfate in solution disrupts adhesion of chick neural retina cells to glass surfaces coated with the 170,000-mol-wt protein. This adhesion is not impaired by chondroitin sulfate or hyaluronic acid, which indicates that inhibition by heparan sulfate is specific. Polyclonal antisera directed against the cell surface heparan sulfate proteoglycan also inhibit attachment of retinal cells to the 170,000-mol-wt protein, which suggests that cell-adheron binding is mediated in part by interactions between cell surface heparan sulfate proteoglycan and 170,000-mol-wt protein contained in the adheron particles. Previous studies have indicated that this type of cell-substratum adhesion is tissue-specific since retina cells do not attach to muscle adherons. Schubert D., M. LaCorbiere, F. G. Klier, and C. Birdwell, 1983, J. Cell Biol. 96:990-998.

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