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Relationships between levels of membrane-bound glucuronidase and the associated protein egasyn in mouse tissues
Mouse beta-glucuronidase has a dual intracellular localization, being present in both endoplasmic reticulum and lysosomes of several tissues. Previous studies demonstrated that the protein egasyn is complexed with microsomal but not lysosomal glucuronidase and that a mutant lacking egasyn is deficie...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1977
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2111429/ https://www.ncbi.nlm.nih.gov/pubmed/873997 |
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collection | PubMed |
description | Mouse beta-glucuronidase has a dual intracellular localization, being present in both endoplasmic reticulum and lysosomes of several tissues. Previous studies demonstrated that the protein egasyn is complexed with microsomal but not lysosomal glucuronidase and that a mutant lacking egasyn is deficient in microsomal, but not lysosomal, glucuronidase. By means of a recently developed radioimmunoassay for egasyn, the relationship between microsomal glucuronidase levels and egasyn levels has been examined in various adult tissues, during postnatal development in liver, and after androgen induction of glucuronidase in kidney. The results indicate that the relative availability of egasyn determines the balance between glucuronidase incorporation into membranes and that into lysosomes. |
format | Text |
id | pubmed-2111429 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1977 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21114292008-05-01 Relationships between levels of membrane-bound glucuronidase and the associated protein egasyn in mouse tissues J Cell Biol Articles Mouse beta-glucuronidase has a dual intracellular localization, being present in both endoplasmic reticulum and lysosomes of several tissues. Previous studies demonstrated that the protein egasyn is complexed with microsomal but not lysosomal glucuronidase and that a mutant lacking egasyn is deficient in microsomal, but not lysosomal, glucuronidase. By means of a recently developed radioimmunoassay for egasyn, the relationship between microsomal glucuronidase levels and egasyn levels has been examined in various adult tissues, during postnatal development in liver, and after androgen induction of glucuronidase in kidney. The results indicate that the relative availability of egasyn determines the balance between glucuronidase incorporation into membranes and that into lysosomes. The Rockefeller University Press 1977-06-01 /pmc/articles/PMC2111429/ /pubmed/873997 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 Relationships between levels of membrane-bound glucuronidase and the associated protein egasyn in mouse tissues |
title | Relationships between levels of membrane-bound glucuronidase and the associated protein egasyn in mouse tissues |
title_full | Relationships between levels of membrane-bound glucuronidase and the associated protein egasyn in mouse tissues |
title_fullStr | Relationships between levels of membrane-bound glucuronidase and the associated protein egasyn in mouse tissues |
title_full_unstemmed | Relationships between levels of membrane-bound glucuronidase and the associated protein egasyn in mouse tissues |
title_short | Relationships between levels of membrane-bound glucuronidase and the associated protein egasyn in mouse tissues |
title_sort | relationships between levels of membrane-bound glucuronidase and the associated protein egasyn in mouse tissues |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2111429/ https://www.ncbi.nlm.nih.gov/pubmed/873997 |