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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...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1987
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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. |
format | Text |
id | pubmed-2114493 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1987 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
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 |