http://link.springer.com/chapter/10.1007/978-1-4614-8090-7_6
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Abstract
The neuron-specific
intercellular adhesion molecule-5 (ICAM-5, telencephalin) is a member of
the ICAM family of adhesion proteins. It has a complex structure with
nine external immunoglobulin domains followed by a transmembrane and a
cytoplasmic domain. The external part binds to β1- and β2-integrins and
the matrix protein vitronectin, whereas its transmembrane domain binds
to presenilins and the cytoplasmic domain to α-actinin and the ERM
family of cytoplasmic proteins. In neurons it is confined to the soma
and dendrites and it is enriched in dendritic filopodia with less
expression in more mature dendritic spines. ICAM-5 strongly stimulates
neurite outgrowth. ICAM-5 is cleaved by matrix metalloproteases upon
activation of glutamate receptors or degraded through endocytosis
resulting in increased spine maturation. Ablation of ICAM-5 expression
increases functional synapse formation. The cleaved soluble fragment of
ICAM-5 is immunosuppressive, which may be important in neuronal
inflammatory diseases.
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