Chloroquine-induced lysosomal abnormalities in cultured foetal mouse hearts
Identifieur interne : 003916 ( Main/Exploration ); précédent : 003915; suivant : 003917Chloroquine-induced lysosomal abnormalities in cultured foetal mouse hearts
Auteurs : Robert M. Ridout [États-Unis] ; Robert S. Decker [États-Unis] ; Kern Wildenthal [États-Unis]Source :
- Journal of Molecular and Cellular Cardiology [ 0022-2828 ] ; 1978.
English descriptors
- Teeft :
- Abnormality, Acid hydrolase reaction product, Acid phosphatase, Acid phosphatase activity, Acid phosphatase reaction product, Aryl sulfatase reaction product, Autophagic, Autophagic vacuoles, Biological chemistry, Cacodylate buffer, Cardiac, Cardiac lysosomal enzyme activities, Cardiac lysosomal function, Cardiac lysosomes, Cardiac myofilaments, Cardiac structure, Cathepsin, Cell biology, Cellular cardiology, Chloroquine, Chloroquine treatment, Circulation research, Control chloroquine difference, Creatine kinase, Cultured macrophages, Degradation, Electron microscopy, Enzyme, Enzyme activity, Extensive deposits, Fibroblast, Foetal, Foetal mouse heart, Foetal mouse hearts, Golgi, Heart tissue, Human fibroblasts, Immense vacuoles, Interstitial cells, Laboratory investigation, Lysosomal, Lysosomal abnormalities, Lysosomal activity, Lysosomal alterations, Lysosomal enzyme activities, Lysosomal enzymes, Lysosomal enzymes cathepsin, Lysosomal function, Lysosomal membranes, Lysosomal structure, Lysosome, Many tissues, Morphological changes, Myeloid, Myeloid bodies, Myocytes, Myofilamentous aggregates, Myofilaments, Nmol protein, Organ culture, Phosphatase, Polar lipids, Protein degradation, Recent advances, Ridout etal, Secondary lysosomes, Significant decrease, Total activities, University park press, Uranyl acetate, Vacuole, Wildenthal.
Abstract
Abstract: Chloroquine (100 μm) induces abnormalities of lysosomal structure in cultured mouse hearts. After 1 or 2 days' exposure to the drug, large autophagic vacuoles with myeloid figures and inclusion bodies develop within myocytes and interstitial cells. Secondary lysosomes in interstitial cells occasionally contain cardiac myofilaments. In addition, after 2 days, the amounts of cathepsin D and β-acetylglucosaminidase decrease significantly, along with a significant redistribution of enzyme activity between sedimentable and non-sedimentable fractions. The results suggest that chloroquine is a useful experimental agent for causing lysosomal derangements in cardiac tissues under controlled conditions.
Url:
DOI: 10.1016/0022-2828(78)90041-X
Affiliations:
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Le document en format XML
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<series><title level="j">Journal of Molecular and Cellular Cardiology</title>
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<profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Abnormality</term>
<term>Acid hydrolase reaction product</term>
<term>Acid phosphatase</term>
<term>Acid phosphatase activity</term>
<term>Acid phosphatase reaction product</term>
<term>Aryl sulfatase reaction product</term>
<term>Autophagic</term>
<term>Autophagic vacuoles</term>
<term>Biological chemistry</term>
<term>Cacodylate buffer</term>
<term>Cardiac</term>
<term>Cardiac lysosomal enzyme activities</term>
<term>Cardiac lysosomal function</term>
<term>Cardiac lysosomes</term>
<term>Cardiac myofilaments</term>
<term>Cardiac structure</term>
<term>Cathepsin</term>
<term>Cell biology</term>
<term>Cellular cardiology</term>
<term>Chloroquine</term>
<term>Chloroquine treatment</term>
<term>Circulation research</term>
<term>Control chloroquine difference</term>
<term>Creatine kinase</term>
<term>Cultured macrophages</term>
<term>Degradation</term>
<term>Electron microscopy</term>
<term>Enzyme</term>
<term>Enzyme activity</term>
<term>Extensive deposits</term>
<term>Fibroblast</term>
<term>Foetal</term>
<term>Foetal mouse heart</term>
<term>Foetal mouse hearts</term>
<term>Golgi</term>
<term>Heart tissue</term>
<term>Human fibroblasts</term>
<term>Immense vacuoles</term>
<term>Interstitial cells</term>
<term>Laboratory investigation</term>
<term>Lysosomal</term>
<term>Lysosomal abnormalities</term>
<term>Lysosomal activity</term>
<term>Lysosomal alterations</term>
<term>Lysosomal enzyme activities</term>
<term>Lysosomal enzymes</term>
<term>Lysosomal enzymes cathepsin</term>
<term>Lysosomal function</term>
<term>Lysosomal membranes</term>
<term>Lysosomal structure</term>
<term>Lysosome</term>
<term>Many tissues</term>
<term>Morphological changes</term>
<term>Myeloid</term>
<term>Myeloid bodies</term>
<term>Myocytes</term>
<term>Myofilamentous aggregates</term>
<term>Myofilaments</term>
<term>Nmol protein</term>
<term>Organ culture</term>
<term>Phosphatase</term>
<term>Polar lipids</term>
<term>Protein degradation</term>
<term>Recent advances</term>
<term>Ridout etal</term>
<term>Secondary lysosomes</term>
<term>Significant decrease</term>
<term>Total activities</term>
<term>University park press</term>
<term>Uranyl acetate</term>
<term>Vacuole</term>
<term>Wildenthal</term>
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<front><div type="abstract" xml:lang="en">Abstract: Chloroquine (100 μm) induces abnormalities of lysosomal structure in cultured mouse hearts. After 1 or 2 days' exposure to the drug, large autophagic vacuoles with myeloid figures and inclusion bodies develop within myocytes and interstitial cells. Secondary lysosomes in interstitial cells occasionally contain cardiac myofilaments. In addition, after 2 days, the amounts of cathepsin D and β-acetylglucosaminidase decrease significantly, along with a significant redistribution of enzyme activity between sedimentable and non-sedimentable fractions. The results suggest that chloroquine is a useful experimental agent for causing lysosomal derangements in cardiac tissues under controlled conditions.</div>
</front>
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<name sortKey="Decker, Robert S" sort="Decker, Robert S" uniqKey="Decker R" first="Robert S." last="Decker">Robert S. Decker</name>
<name sortKey="Decker, Robert S" sort="Decker, Robert S" uniqKey="Decker R" first="Robert S." last="Decker">Robert S. Decker</name>
<name sortKey="Decker, Robert S" sort="Decker, Robert S" uniqKey="Decker R" first="Robert S." last="Decker">Robert S. Decker</name>
<name sortKey="Ridout, Robert M" sort="Ridout, Robert M" uniqKey="Ridout R" first="Robert M." last="Ridout">Robert M. Ridout</name>
<name sortKey="Ridout, Robert M" sort="Ridout, Robert M" uniqKey="Ridout R" first="Robert M." last="Ridout">Robert M. Ridout</name>
<name sortKey="Wildenthal, Kern" sort="Wildenthal, Kern" uniqKey="Wildenthal K" first="Kern" last="Wildenthal">Kern Wildenthal</name>
<name sortKey="Wildenthal, Kern" sort="Wildenthal, Kern" uniqKey="Wildenthal K" first="Kern" last="Wildenthal">Kern Wildenthal</name>
<name sortKey="Wildenthal, Kern" sort="Wildenthal, Kern" uniqKey="Wildenthal K" first="Kern" last="Wildenthal">Kern Wildenthal</name>
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