Characterization of SynCAM surface trafficking using a SynCAM derived ligand with high homophilic binding affinity
Biochemical and Biophysical Research Communications. 2007-08-01; 359(3): 655-659
DOI: 10.1016/j.bbrc.2007.05.152
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1. Biochem Biophys Res Commun. 2007 Aug 3;359(3):655-9. Epub 2007 May 30.
Characterization of SynCAM surface trafficking using a SynCAM derived ligand with
high homophilic binding affinity.
Breillat C(1), Thoumine O, Choquet D.
Author information:
(1)UMR CNRS 5091, Institut François Magendie, Université Bordeaux 2, 33077
Bordeaux, France.
In order to better probe SynCAM function in neurons, we produced a fusion protein
between the extracellular domain of SynCAM1 and the constant fragment of human
IgG (SynCAM-Fc). Whether in soluble form or immobilized on latex microspheres,
the chimera bound specifically to the surface of hippocampal neurons and
recruited endogenous SynCAM molecules. SynCAM-Fc was also used in combination
with Quantum Dots to follow the mobility of transfected SynCAM receptors at the
neuronal surface. Both immobile and highly mobile SynCAM were found. Thus,
SynCAM-Fc behaves as a high affinity ligand that can be used to study the
function of SynCAM at the neuronal membrane.
DOI: 10.1016/j.bbrc.2007.05.152
PMID: 17548061 [Indexed for MEDLINE]