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Embryonic Neural Cell Adhesion Molecule in Cerebrospinal Fluid of Younger Children: Age‐Dependent Decrease During the First Year
Author(s) -
Weisgerber Ch.,
Husmann M.,
Frosch M.,
Rheinheimer C.,
Peuckert W.,
Görgen I.,
BitterSuermann D.
Publication year - 1990
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1990.tb05796.x
Subject(s) - neural cell adhesion molecule , monoclonal antibody , gel electrophoresis , glycoprotein , biology , antibody , cell adhesion molecule , microbiology and biotechnology , cell adhesion , biochemistry , chemistry , cell , immunology
Poly‐α‐2,8‐ N ‐acetylneuraminic acid (poly‐α‐2,8‐NeuAc) is developmentally expressed in neural tissue of higher animals, where it is covalently attached to the neural cell adhesion molecule (NCAM), a large integral membrane glycoprotein mediating cell‐cell adhesion during neuronal development. NCAM exists in several molecular forms, of which only embryonic NCAM carries lengthy chains (n > 5) of poly‐α‐2,8‐NeuAc. Chemically identical poly‐α‐2,8‐NeuAc of bacterial origin is an important virulence factor in infections caused by Neisseria meningitidis group B and Escherichia coli K1, the predominant pathogens of bacterial meningitis. A quantitative enzyme‐linked immunoassay was developed using monoclonal antibody (MAb) 735, an MAb specifically recognizing poly‐α‐2,8‐NeuAc, and applied to CSF specimens from younger children. Poly‐α‐2,8‐NeuAc contents were within the range of 20‐0.2 μg/ml, decreasing from day 1 to day 300. Immunoprecipitation, immunoblot with a rabbit anti‐mouse NCAM serum recognizing the protein part of human NCAM by cross‐reactivity, affinity enrichment using immobilized MAb 735, and sodium dodecyl sulfate‐polyacrylamide gel electrophoresis revealed that poly‐α‐2,8‐NeuAc in CSF is bound to human NCAM, probably NCAM‐120.