Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.23.5 (cathepsin D)
 4,130 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of chlorpromazine on lysosomal enzymes and the release of enzymes from lysosomes of bovine retinal pigment epithelial cells were studied in vitro, using cathepsin D, arylsulfatase, and acid phosphatase as lysosomal marker enzymes. Chlorpromazine had little effect on the enzyme activity of cathepsin D and arylsulfatase and slightly decreased that of acid phosphatase. Chlorpromazine accelerated considerably the release of cathepsin D and arylsulfatase, but only minimally affected the release of acid phosphatase. The release of these enzymes from lysosomes depended on the dose of chlorpromazine.
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PMID:Effect of chlorpromazine in vitro on release of enzymes from lysosomes of the bovine retinal pigment epithelium. 669 26

Ligation of the circumflex artery of anaesthetised, open-chest rabbits caused a progressive increase in nonsedimentable cathepsin D activity in severely ischaemic myocardium and an anatomical redistribution of the enzyme from lysosomes into the cytosol, along with progressive ultrastructural signs of cellular damage and necrosis. Chlorpromazine pretreatment (15 mg X kg-1 intravenously) reduced the increase in nonsedimentable cathepsin D activity slightly, but no appreciable protective effect on the anatomical redistribution of the enzyme or the development of ultrastructural signs of necrosis could be detected. It is concluded that in this experimental model of myocardial infarction, high concentrations of chlorpromazine have a mild stabilising action on lysosomes, but the drug has minimal if any effect in protecting the heart from ischaemic damage.
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PMID:Influence of chlorpromazine on lysosomal alterations during myocardial ischaemia. 688 16