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The novel carbohydrate epitope L3 is shared by some neural cell adhesion molecules

The monoclonal L3 antibody reacts with an N-glycosidically linked carbohydrate structure on at least nine glycoproteins of adult mouse brain. Three out of the L3 epitope-carrying glycoproteins could be identified as the neural cell adhesion molecules L1 and myelin- associated glycoprotein, and the n...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1987
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114493/
https://www.ncbi.nlm.nih.gov/pubmed/2438289
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collection PubMed
description The monoclonal L3 antibody reacts with an N-glycosidically linked carbohydrate structure on at least nine glycoproteins of adult mouse brain. Three out of the L3 epitope-carrying glycoproteins could be identified as the neural cell adhesion molecules L1 and myelin- associated glycoprotein, and the novel adhesion molecule on glia. Expression of the L3 carbohydrate epitope is regulated independently of the protein backbone of these three glycoproteins. Based on the observation that out of three functionally characterized L3 epitope- carrying glycoproteins three fulfill the operational definition of an adhesion molecule, we would like to suggest that they form a new family of adhesion molecules that is distinct from the L2/HNK-1 carbohydrate epitope family of neural cell adhesion molecules. Interestingly, some members in each family appear to be unique to one family while other members belong to the two families.
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spelling pubmed-21144932008-05-01 The novel carbohydrate epitope L3 is shared by some neural cell adhesion molecules J Cell Biol Articles The monoclonal L3 antibody reacts with an N-glycosidically linked carbohydrate structure on at least nine glycoproteins of adult mouse brain. Three out of the L3 epitope-carrying glycoproteins could be identified as the neural cell adhesion molecules L1 and myelin- associated glycoprotein, and the novel adhesion molecule on glia. Expression of the L3 carbohydrate epitope is regulated independently of the protein backbone of these three glycoproteins. Based on the observation that out of three functionally characterized L3 epitope- carrying glycoproteins three fulfill the operational definition of an adhesion molecule, we would like to suggest that they form a new family of adhesion molecules that is distinct from the L2/HNK-1 carbohydrate epitope family of neural cell adhesion molecules. Interestingly, some members in each family appear to be unique to one family while other members belong to the two families. The Rockefeller University Press 1987-06-01 /pmc/articles/PMC2114493/ /pubmed/2438289 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
The novel carbohydrate epitope L3 is shared by some neural cell adhesion molecules
title The novel carbohydrate epitope L3 is shared by some neural cell adhesion molecules
title_full The novel carbohydrate epitope L3 is shared by some neural cell adhesion molecules
title_fullStr The novel carbohydrate epitope L3 is shared by some neural cell adhesion molecules
title_full_unstemmed The novel carbohydrate epitope L3 is shared by some neural cell adhesion molecules
title_short The novel carbohydrate epitope L3 is shared by some neural cell adhesion molecules
title_sort novel carbohydrate epitope l3 is shared by some neural cell adhesion molecules
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114493/
https://www.ncbi.nlm.nih.gov/pubmed/2438289