Linked Life Data

12196577

Source:http://linkedlifedata.com/resource/pubmed/id/12196577

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
2002-8-27
pubmed:abstractText
The perineuronal net forms the extracellular matrix of many neurons in the CNS, surrounding neuron cell bodies and proximal dendrites in a mesh-like structure with open "holes" at the sites of synaptic contacts. The perineuronal net is first detected late in development, approximately coincident with the transformation of the CNS from an environment conducive to neuronal growth and motility to one that is restrictive, suggesting a role for the perineuronal net in this developmental transition. Perineuronal nets show a great degree of molecular heterogeneity. Using monoclonal antibodies Cat-301, Cat-315, and Cat-316, we have shown previously that although all antibodies recognize chondroitin sulfate proteoglycans of similar sizes, each antibody recognizes perineuronal nets on distinct but overlapping sets of neurons in the adult cat CNS. An understanding of the heterogeneity demonstrated by these antibodies is critical to understanding the organization and function of perineuronal nets. Using aggrecan knock-out mice (cmd), we have now determined that all three antibodies recognize aggrecan. Chemical and enzymatic deglycosylation show that the differences revealed by the three antibodies arise from differential glycosylation of aggrecan. We further demonstrate that aggrecan mRNA is expressed relatively late in development and that neurons themselves are likely the predominant cellular sites of aggrecan expression. This work indicates that neurons can directly regulate the composition of their extracellular matrix by regulated synthesis and differential glycosylation of aggrecan in a cell type-specific manner. These results have important implications for the role of regulated microheterogeneity of glycosylation in the CNS.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1529-2401
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7536-47
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:12196577-Aggrecans, pubmed-meshheading:12196577-Alternative Splicing, pubmed-meshheading:12196577-Animals, pubmed-meshheading:12196577-Antibodies, pubmed-meshheading:12196577-Antibody Specificity, pubmed-meshheading:12196577-Cerebral Cortex, pubmed-meshheading:12196577-Chondroitin Sulfates, pubmed-meshheading:12196577-Epitopes, pubmed-meshheading:12196577-Extracellular Matrix, pubmed-meshheading:12196577-Extracellular Matrix Proteins, pubmed-meshheading:12196577-Glycosylation, pubmed-meshheading:12196577-Lectins, C-Type, pubmed-meshheading:12196577-Neurons, pubmed-meshheading:12196577-Oligosaccharides, pubmed-meshheading:12196577-Proteoglycans, pubmed-meshheading:12196577-RNA, Messenger, pubmed-meshheading:12196577-Rats, pubmed-meshheading:12196577-Spinal Cord, pubmed-meshheading:12196577-Synapses
pubmed:year
2002
pubmed:articleTitle
Aggrecan glycoforms contribute to the molecular heterogeneity of perineuronal nets.
pubmed:affiliation
Department of Neurobiology, Yale University School of Medicine, New Haven, Connecticut 06520, USA. russell.matthews@yale.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.