Influence of micro and submicro poly(lactic-glycolic acid) fibers on sensory neural cell locomotion and neurite growth

2013 ◽  
Vol 101 (7) ◽  
pp. 1200-1208 ◽  
Author(s):  
Carmen Binder ◽  
Vincent Milleret ◽  
Heike Hall ◽  
Daniel Eberli ◽  
Tessa Lühmann
Keyword(s):  
Glycolic Acid ◽  
Neurite Growth ◽  
Neural Cell ◽  
Cell Locomotion ◽  
Sensory Neural

Galectin-3 promotes neural cell adhesion and neurite growth

1998 ◽  
Vol 54 (5) ◽  
pp. 639-654 ◽  
Author(s):  
Penka Pesheva ◽  
Stephan Kuklinski ◽  
Brigitte Schmitz ◽  
Rainer Probstmeier
Keyword(s):  
Cell Adhesion ◽  
Neurite Growth ◽  
Neural Cell ◽  
Neural Cell Adhesion ◽  
Galectin 3

scholarly journals Interactions of the chondroitin sulfate proteoglycan phosphacan, the extracellular domain of a receptor-type protein tyrosine phosphatase, with neurons, glia, and neural cell adhesion molecules.

1994 ◽  
Vol 127 (6) ◽  
pp. 1703-1715 ◽  
Author(s):  
P Milev ◽  
D R Friedlander ◽  
T Sakurai ◽  
L Karthikeyan ◽  
M Flad ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Chondroitin Sulfate ◽  
Adhesion Molecules ◽  
Cell Adhesion Molecules ◽  
Tyrosine Phosphatase ◽  
Neurite Growth ◽  
Neural Cell ◽  
Neural Cell Adhesion Molecules ◽  
Neural Cell Adhesion ◽  
The Central Nervous System

Phosphacan is a chondroitin sulfate proteoglycan produced by glial cells in the central nervous system, and represents the extracellular domain of a receptor-type protein tyrosine phosphatase (RPTP zeta/beta). We previously demonstrated that soluble phosphacan inhibited the aggregation of microbeads coated with N-CAM or Ng-CAM, and have now found that soluble 125I-phosphacan bound reversibly to these neural cell adhesion molecules, but not to a number of other cell surface and extracellular matrix proteins. The binding was saturable, and Scatchard plots indicated a single high affinity binding site with a Kd of approximately 0.1 nM. Binding was reduced by approximately 15% after chondroitinase treatment, and free chondroitin sulfate was only moderately inhibitory, indicating that the phosphacan core glycoprotein accounts for most of the binding activity. Immunocytochemical studies of embryonic rat spinal phosphacan, Ng-CAM, and N-CAM have overlapping distributions. When dissociated neurons were incubated on dishes coated with combinations of phosphacan and Ng-CAM, neuronal adhesion and neurite growth were inhibited. 125I-phosphacan bound to neurons, and the binding was inhibited by antibodies against Ng-CAM and N-CAM, suggesting that these CAMs are major receptors for phosphacan on neurons. C6 glioma cells, which express phosphacan, adhered to dishes coated with Ng-CAM, and low concentrations of phosphacan inhibited adhesion to Ng-CAM but not to laminin and fibronectin. Our studies suggest that by binding to neural cell adhesion molecules, and possibly also by competing for ligands of the transmembrane phosphatase, phosphacan may play a major role in modulating neuronal and glial adhesion, neurite growth, and signal transduction during the development of the central nervous system.

Evolution of the Sensory/Neural Cell Types

2021 ◽  
pp. 101-128
Author(s):  
Sally Leys ◽  
Jasmine L. Mah ◽  
Emma K.J. Esposito
Keyword(s):  
Cell Types ◽  
Neural Cell ◽  
Sensory Neural

Scanning Electron Microscopy of Dried and Acid Treated Shells of Difflugia

1973 ◽  
Vol 31 ◽  
pp. 448-449
Author(s):  
Barry S. Eckert ◽  
S. M. McGee-Russell
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Critical Point ◽  
Point Method ◽  
External Structure ◽  
Cell Locomotion ◽  
Single Opening ◽  
Scanning Electron

Difflugia lobostoma is a shelled amoeba. The shell is an external structure of considerable mass which presents the animal with special restrictions in cell locomotion which are met by the development of active pseudopodial lobopodia containing, apparently, an organized system of thick and thin microfilaments (Eckert and McGee-Russell, 1972). The shell is constructed of sand grains picked up from the environment, and cemented into place with a secretion. There is a single opening through which lobopods extend. The organization of the shell was studied by scanning electron microscopy (SEM).Intact shells or animals with shells were dried by the critical point method of Anderson (1966) or air dried, after primary fixation in glutaraldehyde.

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