Identification of glycosylphosphatidylinositol-specific phospholipases C in mouse brain membranes.

Using the membrane form of variant surface glycoprotein from Trypanosoma equiperdum labelled with [3H]myristate as a substrate, we identified two glycosylphosphatidylinositol phospholipase C enzymic activities in mouse brain. These activities were associated with particulate membrane fractions. They...

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Main Authors: Fouchier, F, Baltz, T, Rougon, G
Formato: Artigo
Idioma:English
Publicado em: 1990
Assuntos:
Research Article
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC1131579/
https://ncbi.nlm.nih.gov/pubmed/2167064
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spelling pubmed-11315792005-09-07 Identification of glycosylphosphatidylinositol-specific phospholipases C in mouse brain membranes. Fouchier, F Baltz, T Rougon, G Biochem J Research Article Using the membrane form of variant surface glycoprotein from Trypanosoma equiperdum labelled with [3H]myristate as a substrate, we identified two glycosylphosphatidylinositol phospholipase C enzymic activities in mouse brain. These activities were associated with particulate membrane fractions. They were characterized by their pH activity maxima and sensitivity to activators and ion chelators. One of the activities was maximal at acidic pH, stimulated by butanol, sensitive to cation chelator and insensitive to manganese. The activity of the other was maximal at neutral pH, stimulated by the detergent deoxycholate and independent of the presence of cation chelator or calcium. On membrane subfractionation, the acidic butanol-stimulated activity was found mainly associated with the lysosomal compartment, whereas the neutral deoxycholate-stimulated activity sediments with the myelin and plasma membrane compartment. These activities could be differentiated from particulate phosphatidylinositol phospholipases C, whose acidic lysosomal form is sensitive to manganese and insensitive to cation chelator or butanol, whereas the deoxycholate-activated enzymes are Ca2(+)-dependent. 1990-07-15 /pmc/articles/PMC1131579/ /pubmed/2167064 Text en
institution US National Library of Medicine
collection PubMed Central
language English
format Article
topic Research Article
spellingShingle Research Article
Fouchier, F
Baltz, T
Rougon, G
Identification of glycosylphosphatidylinositol-specific phospholipases C in mouse brain membranes.
description Using the membrane form of variant surface glycoprotein from Trypanosoma equiperdum labelled with [3H]myristate as a substrate, we identified two glycosylphosphatidylinositol phospholipase C enzymic activities in mouse brain. These activities were associated with particulate membrane fractions. They were characterized by their pH activity maxima and sensitivity to activators and ion chelators. One of the activities was maximal at acidic pH, stimulated by butanol, sensitive to cation chelator and insensitive to manganese. The activity of the other was maximal at neutral pH, stimulated by the detergent deoxycholate and independent of the presence of cation chelator or calcium. On membrane subfractionation, the acidic butanol-stimulated activity was found mainly associated with the lysosomal compartment, whereas the neutral deoxycholate-stimulated activity sediments with the myelin and plasma membrane compartment. These activities could be differentiated from particulate phosphatidylinositol phospholipases C, whose acidic lysosomal form is sensitive to manganese and insensitive to cation chelator or butanol, whereas the deoxycholate-activated enzymes are Ca2(+)-dependent.
author Fouchier, F
Baltz, T
Rougon, G
author_facet Fouchier, F
Baltz, T
Rougon, G
author_sort Fouchier, F
title Identification of glycosylphosphatidylinositol-specific phospholipases C in mouse brain membranes.
title_short Identification of glycosylphosphatidylinositol-specific phospholipases C in mouse brain membranes.
title_full Identification of glycosylphosphatidylinositol-specific phospholipases C in mouse brain membranes.
title_fullStr Identification of glycosylphosphatidylinositol-specific phospholipases C in mouse brain membranes.
title_full_unstemmed Identification of glycosylphosphatidylinositol-specific phospholipases C in mouse brain membranes.
title_sort identification of glycosylphosphatidylinositol-specific phospholipases c in mouse brain membranes.
publishDate 1990
url https://ncbi.nlm.nih.gov/pmc/articles/PMC1131579/
https://ncbi.nlm.nih.gov/pubmed/2167064
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