Cargando…

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...

Descripción completa

Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1977
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2111429/
https://www.ncbi.nlm.nih.gov/pubmed/873997
_version_ 1782139729678958592
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