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Neuron-specific membrane glycoproteins promoting neurite fasciculation in Aplysia californica
We have generated a library of mouse monoclonal antibodies against membrane proteins of the nervous system of the marine snail Aplysia californica. Two of these antibodies, 4E8 and 3D9, recognize a group of membrane glycoproteins with molecular masses of 100-150 kD. We have called these proteins ap1...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1990
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2116364/ https://www.ncbi.nlm.nih.gov/pubmed/2277077 |
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collection | PubMed |
description | We have generated a library of mouse monoclonal antibodies against membrane proteins of the nervous system of the marine snail Aplysia californica. Two of these antibodies, 4E8 and 3D9, recognize a group of membrane glycoproteins with molecular masses of 100-150 kD. We have called these proteins ap100, from the molecular mass of the most abundant species. Based on Western blots, these proteins appear to be specific for the nervous system. They are enriched in the neuropil of central nervous system ganglia, and are present on the surface of neurites and growth cones of neurons in culture. They are not expressed on the surface of nonneuronal cells. Staining of living cells with fluorescently labeled mAb demonstrates that the epitope(s) are on the outside of the cell. The antibodies against the proteins defasciculate growing axons and alter the morphology of growth cones, but affect much less adhesion between neuritic shafts. In addition, the level of expression of these molecules appears to correlate with the degree of fasciculation of neurites. These observations suggest that the ap100 proteins are cell adhesion molecules that play a role in axon growth in the nervous system of Aplysia. The fact that they are enriched in the neuropil and possibly in varicosities suggest that they may also be relevant for the structure of mature synapses. |
format | Text |
id | pubmed-2116364 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1990 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21163642008-05-01 Neuron-specific membrane glycoproteins promoting neurite fasciculation in Aplysia californica J Cell Biol Articles We have generated a library of mouse monoclonal antibodies against membrane proteins of the nervous system of the marine snail Aplysia californica. Two of these antibodies, 4E8 and 3D9, recognize a group of membrane glycoproteins with molecular masses of 100-150 kD. We have called these proteins ap100, from the molecular mass of the most abundant species. Based on Western blots, these proteins appear to be specific for the nervous system. They are enriched in the neuropil of central nervous system ganglia, and are present on the surface of neurites and growth cones of neurons in culture. They are not expressed on the surface of nonneuronal cells. Staining of living cells with fluorescently labeled mAb demonstrates that the epitope(s) are on the outside of the cell. The antibodies against the proteins defasciculate growing axons and alter the morphology of growth cones, but affect much less adhesion between neuritic shafts. In addition, the level of expression of these molecules appears to correlate with the degree of fasciculation of neurites. These observations suggest that the ap100 proteins are cell adhesion molecules that play a role in axon growth in the nervous system of Aplysia. The fact that they are enriched in the neuropil and possibly in varicosities suggest that they may also be relevant for the structure of mature synapses. The Rockefeller University Press 1990-12-01 /pmc/articles/PMC2116364/ /pubmed/2277077 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 Neuron-specific membrane glycoproteins promoting neurite fasciculation in Aplysia californica |
title | Neuron-specific membrane glycoproteins promoting neurite fasciculation in Aplysia californica |
title_full | Neuron-specific membrane glycoproteins promoting neurite fasciculation in Aplysia californica |
title_fullStr | Neuron-specific membrane glycoproteins promoting neurite fasciculation in Aplysia californica |
title_full_unstemmed | Neuron-specific membrane glycoproteins promoting neurite fasciculation in Aplysia californica |
title_short | Neuron-specific membrane glycoproteins promoting neurite fasciculation in Aplysia californica |
title_sort | neuron-specific membrane glycoproteins promoting neurite fasciculation in aplysia californica |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2116364/ https://www.ncbi.nlm.nih.gov/pubmed/2277077 |