Regulation of cell adhesion by polysialic acid: Effects on cadherin, IgCAM and integrin function and independence from NCAM binding or signaling activity Meeting Abstract

  


Authors: Fujimoto, I.; Bruses, J. L.; Rutishauser, U.
Abstract Title: Regulation of cell adhesion by polysialic acid: Effects on cadherin, IgCAM and integrin function and independence from NCAM binding or signaling activity
Meeting Title: 31st Annual Meeting of the Society for Neuroscience
Abstract: The polysialylation of NCAM in vertebrates is known to promote the outgrowth and accurate guidance of axons. These effects are believed to involve the attenuation of cell interactions that are not mediated through NCAM's own adhesion properties. Possible mechanisms for this global effect on cell interaction include an inhibition of cell apposition based on PSA's biophysical properties, perturbation of CAM-CAM interactions in the plane of the membrane, and alteration of signaling pathways generated by NCAM. To test these alternatives, this study uses a quantitative cell detachment assay together with cells engineered to display different adhesion receptors together with a variety of polysialylated NCAM polypeptide isoforms and domain deletion mutations. The results obtained indicate that regulation occurs with adhesion receptors as diverse as an IgCAM, a cadherin and an integrin, and does not require NCAM functional domains other than those minimally required for polysialylation. These findings are most consistent with the cell apposition mechanism for PSA action, as this model predicts that the inhibitory effects of PSA-NCAM on cell adhesion should be independent of the nature of the adhesion system and of any intrinsic binding or signaling properties of the NCAM polypeptide itself.
Keywords: meeting abstract; cell apposition
Journal Title: Society for Neuroscience Abstracts
Volume: 27
Issue: 2
Meeting Dates: 2001 Nov 10-15
Meeting Location: San Diego, CA
ISSN: 0190-5295
Publisher: Society for Neuroscience  
Date Published: 2001-01-01
Start Page: 1540
Language: English
ACCESSION: BCI:BCI200100538356
PROVIDER: biosis
Notes: Meeting Abstract: 591.14 -- Source: Biosis