DMCA
Mutations in the L1 neural cell adhesion molecule, a transmembrane
BibTeX
@MISC{Moulding_mutationsin,
author = {Hugh D. Moulding and Robert L. Martuza and Samuel D. Rabkin},
title = {Mutations in the L1 neural cell adhesion molecule, a transmembrane},
year = {}
}
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Abstract
glycoprotein, cause a spectrum of congenital neurological syndromes, ranging from hydrocephalus to mental retardation. Many of these mutations are single amino acid changes that are distributed throughout the various domains of the protein. Defective herpes simplex virus vectors were used to express L1 protein with the clinical missense mutations R184Q and D598N in the Ig2 and Ig6 extracellular domains, respectively, and S1194L in the cytoplasmic domain. All three mutant proteins were expressed at similar levels in infected cells. Neurite outgrowth of cerebellar granule cells was stimulated on astrocytes expressing wild-type or S1194L L1, whereas those expressing R184Q and D598N L1 failed to increase neurite length. Live cell immunofluorescent staining of L1 demonstrated that most defective vector-infected cells did not express R184Q or D598N L1 on their cell surface. This greatly diminished cell-surface expression
Keyphrases
l1 neural cell adhesion molecule d598n l1 ig6 extracellular domain clinical missense mutation r184q l1 protein diminished cell-surface expression cell surface similar level cytoplasmic domain infected cell cerebellar granule cell various domain defective herpes simplex virus vector mutant protein s1194l l1 neurite outgrowth live cell immunofluorescent staining defective vector-infected cell mental retardation neurite length congenital neurological syndrome single amino acid change
