Direct evidence that Neural Cell Adhesion Molecule (NCAM) polysialylation increases intermembrane repulsion and abrogates adhesion Journal Article


Authors: Johnson, C. P.; Fujimoto, I.; Rutishauser, U.; Leckband, D. E.
Article Title: Direct evidence that Neural Cell Adhesion Molecule (NCAM) polysialylation increases intermembrane repulsion and abrogates adhesion
Abstract: Molecular force measurements quantified the impact of polysialylation on the adhesive properties both of membrane-bound neural cell adhesion molecule (NCAM) and of other proteins on the same membrane. These results show quantitatively that NCAM polysialylation increases the range and magnitude of intermembrane repulsion. The repulsion is sufficient to overwhelm both homophilic NCAM and cadherin attraction at physiological ionic strength, and it abrogates the protein-mediated intermembrane adhesion. The steric repulsion is ionic strength dependent and decreases substantially at high monovalent salt concentrations with a concomitant increase in the intermembrane attraction. The magnitude of the repulsion also depends on the amount of polysialic acid (PSA) on the membranes, and the PSA-dependent attenuation of cadherin adhesion increases with increasing PSA-NCAM:cadherin ratios. These findings agree qualitatively with independent reports based on cell adhesion studies and reveal the likely molecular mechanism by which NCAM polysialylation regulates cell adhesion and intermembrane space.
Keywords: nonhuman; proteins; animal cell; animals; protein protein interaction; fluorescence correlation spectroscopy; protein binding; structure-activity relationship; animalia; nerve cell adhesion molecule; polysialic acid; molecular structure; cell interaction; cadherin; cell adhesion; sodium chloride; acids; neurology; sialic acids; chickens; cho cells; cricetinae; cells; adhesion; neural cell adhesion molecules; sialylation; biological membranes; hydrodynamics; salts; concentration (process); ionic strength; monovalent cation; intermembrane space; neural cell adhesion molecules (ncam); polysialylation
Journal Title: Journal of Biological Chemistry
Volume: 280
Issue: 1
ISSN: 0021-9258
Publisher: American Society for Biochemistry and Molecular Biology  
Date Published: 2005-01-07
Start Page: 137
End Page: 145
Language: English
DOI: 10.1074/jbc.M410216200
PUBMED: 15504723
PROVIDER: scopus
DOI/URL:
Notes: --- - "Cited By (since 1996): 98" - "Export Date: 24 October 2012" - "CODEN: JBCHA" - "Source: Scopus"
Altmetric
Citation Impact
BMJ Impact Analytics
MSK Authors