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Adhesion proteins for a tight neuron-electrode contact.


Sorribas, H; Braun, D; Leder, L; Sonderegger, P; Tiefenauer, L (2001). Adhesion proteins for a tight neuron-electrode contact. Journal of Neuroscience Methods, 104(2):133-141.

Abstract

The neural cell adhesion molecules axonin-1 and NgCAM have been genetically engineered and covalently immobilized on glass and silicon oxide surfaces in their correct orientation. Surfaces treated with these adhesion molecules were used as substrates for culturing dorsal root ganglion neurons. The cleft between the neuron cell membrane and the surface was determined using fluorescence interference contrast (FLIC) microscopy. For comparison, cell--material distances on laminin, RGDC, polylysine and amino-terminated surfaces were measured. When the neurons grow on axonin-1 the cell--surface distance is at a minimum (37 nm) probably because the glycocalyx hinders a closer contact. A selective treatment of extracellular electrodes with axonin-1 could be used to improve the cell-material contact and thus increase extracellularly recorded signals.

The neural cell adhesion molecules axonin-1 and NgCAM have been genetically engineered and covalently immobilized on glass and silicon oxide surfaces in their correct orientation. Surfaces treated with these adhesion molecules were used as substrates for culturing dorsal root ganglion neurons. The cleft between the neuron cell membrane and the surface was determined using fluorescence interference contrast (FLIC) microscopy. For comparison, cell--material distances on laminin, RGDC, polylysine and amino-terminated surfaces were measured. When the neurons grow on axonin-1 the cell--surface distance is at a minimum (37 nm) probably because the glycocalyx hinders a closer contact. A selective treatment of extracellular electrodes with axonin-1 could be used to improve the cell-material contact and thus increase extracellularly recorded signals.

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28 citations in Web of Science®
33 citations in Scopus®
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Additional indexing

Item Type:Journal Article, refereed
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
Dewey Decimal Classification:570 Life sciences; biology
Language:English
Date:15 January 2001
Deposited On:11 Feb 2008 12:20
Last Modified:05 Apr 2016 12:17
Publisher:Elsevier
ISSN:0165-0270
Publisher DOI:10.1016/S0165-0270(00)00333-2
PubMed ID:11164239

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