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Externalization of an endogenous chicken muscle lectin with in vivo development

Chicken-lactose-lectin-I (CLL-I), an endogenous lectin that is developmentally regulated in embryonic muscle, was localized by immunohistochemical techniques in tissue samples taken at various stages of in vivo development and in primary muscle cultures. Lectin, which was diffusely distributed in my...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1981
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2111973/
https://www.ncbi.nlm.nih.gov/pubmed/7309798
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description Chicken-lactose-lectin-I (CLL-I), an endogenous lectin that is developmentally regulated in embryonic muscle, was localized by immunohistochemical techniques in tissue samples taken at various stages of in vivo development and in primary muscle cultures. Lectin, which was diffusely distributed in myoblasts, became localized in myotubes in a distribution similar to that of the sarcoplasmic reticulum and T tubules. Later in development, lectin was predominantly extracellular. This sequence suggests that externalization may have occurred by migration in the T tubules, which are continuous with the extracellular space, although alternative explanations are possible. Only traces of lectin were found in the adult. These studies did not reveal the function of CLL-I in muscle development. However, we infer that it acts by organizing complementary glycoconjugates in the intracellular tubular network, on the muscle surface, and/or in extracellular materials.
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spelling pubmed-21119732008-05-01 Externalization of an endogenous chicken muscle lectin with in vivo development J Cell Biol Articles Chicken-lactose-lectin-I (CLL-I), an endogenous lectin that is developmentally regulated in embryonic muscle, was localized by immunohistochemical techniques in tissue samples taken at various stages of in vivo development and in primary muscle cultures. Lectin, which was diffusely distributed in myoblasts, became localized in myotubes in a distribution similar to that of the sarcoplasmic reticulum and T tubules. Later in development, lectin was predominantly extracellular. This sequence suggests that externalization may have occurred by migration in the T tubules, which are continuous with the extracellular space, although alternative explanations are possible. Only traces of lectin were found in the adult. These studies did not reveal the function of CLL-I in muscle development. However, we infer that it acts by organizing complementary glycoconjugates in the intracellular tubular network, on the muscle surface, and/or in extracellular materials. The Rockefeller University Press 1981-11-01 /pmc/articles/PMC2111973/ /pubmed/7309798 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
Externalization of an endogenous chicken muscle lectin with in vivo development
title Externalization of an endogenous chicken muscle lectin with in vivo development
title_full Externalization of an endogenous chicken muscle lectin with in vivo development
title_fullStr Externalization of an endogenous chicken muscle lectin with in vivo development
title_full_unstemmed Externalization of an endogenous chicken muscle lectin with in vivo development
title_short Externalization of an endogenous chicken muscle lectin with in vivo development
title_sort externalization of an endogenous chicken muscle lectin with in vivo development
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2111973/
https://www.ncbi.nlm.nih.gov/pubmed/7309798