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Drosophila fasciclin I is a novel homophilic adhesion molecule that along with fasciclin III can mediate cell sorting

Fasciclin I is a membrane-associated glycoprotein that is regionally expressed on a subset of fasciculating axons during neuronal development in insects; it is expressed on apposing cell surfaces, suggesting a role in specific cell adhesion. In this paper we show that Drosophila fasciclin I is a nov...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1990
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2200178/
https://www.ncbi.nlm.nih.gov/pubmed/2335571
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collection PubMed
description Fasciclin I is a membrane-associated glycoprotein that is regionally expressed on a subset of fasciculating axons during neuronal development in insects; it is expressed on apposing cell surfaces, suggesting a role in specific cell adhesion. In this paper we show that Drosophila fasciclin I is a novel homophilic cell adhesion molecule. When the nonadhesive Drosophila S2 cells are transfected with the fasciclin I cDNA, they form aggregates that are blocked by antisera against fasciclin I. When cells expressing fasciclin I are mixed with cells expressing fasciclin III, another Drosophila homophilic adhesion molecule, the mixture sorts into aggregates homogeneous for either fasciclin I- or fasciclin III-expressing cells. The ability of these two novel adhesion molecules to mediate cell sorting in vitro suggests that they might play a similar role during neuronal development.
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spelling pubmed-22001782008-05-01 Drosophila fasciclin I is a novel homophilic adhesion molecule that along with fasciclin III can mediate cell sorting J Cell Biol Articles Fasciclin I is a membrane-associated glycoprotein that is regionally expressed on a subset of fasciculating axons during neuronal development in insects; it is expressed on apposing cell surfaces, suggesting a role in specific cell adhesion. In this paper we show that Drosophila fasciclin I is a novel homophilic cell adhesion molecule. When the nonadhesive Drosophila S2 cells are transfected with the fasciclin I cDNA, they form aggregates that are blocked by antisera against fasciclin I. When cells expressing fasciclin I are mixed with cells expressing fasciclin III, another Drosophila homophilic adhesion molecule, the mixture sorts into aggregates homogeneous for either fasciclin I- or fasciclin III-expressing cells. The ability of these two novel adhesion molecules to mediate cell sorting in vitro suggests that they might play a similar role during neuronal development. The Rockefeller University Press 1990-05-01 /pmc/articles/PMC2200178/ /pubmed/2335571 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
Drosophila fasciclin I is a novel homophilic adhesion molecule that along with fasciclin III can mediate cell sorting
title Drosophila fasciclin I is a novel homophilic adhesion molecule that along with fasciclin III can mediate cell sorting
title_full Drosophila fasciclin I is a novel homophilic adhesion molecule that along with fasciclin III can mediate cell sorting
title_fullStr Drosophila fasciclin I is a novel homophilic adhesion molecule that along with fasciclin III can mediate cell sorting
title_full_unstemmed Drosophila fasciclin I is a novel homophilic adhesion molecule that along with fasciclin III can mediate cell sorting
title_short Drosophila fasciclin I is a novel homophilic adhesion molecule that along with fasciclin III can mediate cell sorting
title_sort drosophila fasciclin i is a novel homophilic adhesion molecule that along with fasciclin iii can mediate cell sorting
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2200178/
https://www.ncbi.nlm.nih.gov/pubmed/2335571