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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2008-3-18
pubmed:abstractText
Using structure based genome mining targeting vascular endothelial and platelet derived growth factor immunoglobulin (Ig) like folds, we have identified a sequence corresponding to a single transmembrane protein with two Ig domains, which we cloned from a human brain cDNA library. The cDNA is identical to hepatocyte cell adhesion molecule (hepaCAM), which was originally described as a tumor suppressor gene in liver. Here, we show that the protein is predominantly expressed in the mouse and human nervous system. In liver, the expression is very low in humans, and is not detected in mice. To identify the central nervous system (CNS) regions and cell types expressing the protein, we performed a LacZ reporter gene assay on heterozygous mice in which one copy of the gene encoding the novel protein had been replaced with beta-galactosidase. beta-galactosidase expression was prominent in white matter tracts of the CNS. Furthermore, expression was detected in ependymal cells of the brain ventricular zones and the central canal of the spinal cord. Double labeling experiments showed expression mainly in CNPase positive oligodendrocytes (OL). Since the protein is predominantly expressed in the CNS glial cells, we named the molecule glial cell adhesion molecule (GlialCAM). A potential role for GlialCAM in myelination was supported by its up-regulation during postnatal mouse brain development, where it was concomitantly expressed with myelin basic protein (MBP). In addition, in vitro, GlialCAM was observed in various developmental stages of OL and in astrocytes in processes and at cell contact sites. In A2B5 positive OL, GlialCAM colocalizes with GAP43 in OL growth cone like structures. Overall, the data presented here indicate a potential function for GlialCAM in glial cell biology.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0894-1491
pubmed:author
pubmed:copyrightInfo
(c) 2008 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
56
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
633-45
pubmed:meshHeading
pubmed-meshheading:18293412-2',3'-Cyclic-Nucleotide Phosphodiesterases, pubmed-meshheading:18293412-Age Factors, pubmed-meshheading:18293412-Animals, pubmed-meshheading:18293412-Animals, Newborn, pubmed-meshheading:18293412-Cell Adhesion Molecules, pubmed-meshheading:18293412-Cells, Cultured, pubmed-meshheading:18293412-Central Nervous System, pubmed-meshheading:18293412-Cloning, Molecular, pubmed-meshheading:18293412-GAP-43 Protein, pubmed-meshheading:18293412-Gangliosides, pubmed-meshheading:18293412-Gene Expression, pubmed-meshheading:18293412-Gene Expression Regulation, Developmental, pubmed-meshheading:18293412-Humans, pubmed-meshheading:18293412-Mice, pubmed-meshheading:18293412-Mice, Inbred C57BL, pubmed-meshheading:18293412-Mice, Knockout, pubmed-meshheading:18293412-Myelin Basic Proteins, pubmed-meshheading:18293412-Neuroglia, pubmed-meshheading:18293412-Rats, pubmed-meshheading:18293412-Rats, Sprague-Dawley
pubmed:year
2008
pubmed:articleTitle
GlialCAM, an immunoglobulin-like cell adhesion molecule is expressed in glial cells of the central nervous system.
pubmed:affiliation
Protein and Cell Sciences, Merck Serono, Geneva Research Center, Geneva, Switzerland.
pubmed:publicationType
Journal Article