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

A number of investigations have reported that prostacyclin or prostacyclin analogues protect the ischaemic myocardium when administered early after myocardial ischaemia. Thus far, there are no reports describing whether these substances exert a cardioprotective effect when administered later than 0.5 h after coronary artery occlusion. Adult cats were subjected to acute coronary artery ligation for 5 h and administered the vehicle or ZK 36 374 (iloprost) (1.19 micrograms X kg-1 X min-1), a prostacyclin analogue, beginning at 0.5, 2 or 4 h. Compared with the MI-vehicle cats, ZK 36 374 prevented a decrease in myocardial creatine kinase specific activity, the loss of free amino nitrogen and the fall in percentage bound cathepsin D in the ischaemic area when infusion was started at 0.5 or 2 h (P less than 0.05). In addition ZK 36 374 started at 4 h still showed a significant protective effect against myocardial creatine kinase specific activity and amino nitrogen concentrations but not against cathepsin D. In a separate group of animals, regional myocardial blood flow and late coronary resistance were determined with radioactive labelled 15 +/- 1 micron microspheres. ZK 36 374 consistently reduced late diastolic coronary vascular resistance and increased coronary blood flow in nonischaemic regions of the myocardium (P less than 0.05) but only attenuated the further increase in late coronary resistance in the ischaemic myocardial regions. The infarcted area (NTB-staining) amounted to 9% of the total left ventricle after 5 h and was not reduced by ZK 36 374 (P greater than 0.05). In conclusion, ZK 36 374 exerted a significant biochemical cardioprotective effect when administered to 0.5, 2 or 4 h. The mechanism of cardioprotection does not appear to be due to increased myocardial perfusion but rather to some direct cellular action whose exact nature has yet to be elucidated.
Cardiovasc Res 1984 Mar
PMID:Early and late administration of a PGI2-analogue, ZK 36 374 (iloprost): effects on myocardial preservation, collateral blood flow and infarct size. 620 Feb 29

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.
Cardiovasc Res 1983 Jul
PMID:Influence of chlorpromazine on lysosomal alterations during myocardial ischaemia. 688 16

We have developed a sensitive double antibody radioimmunoassay for measuring canine cardiac cathepsin D. Radioiodinated cathepsin D was prepared by chloramine T oxidation using a highly purified source of enzyme. High avidity antiserum to the canine cardiac enzyme was raised in rabbits. Antibody-bound cathepsin D was separated from free enzyme using goat anti-rabbit IgG second antibody. The least amount of immunoreactive enzyme measurable in the radioimmunoassay was 2.4 ng.cm-3 as determined by antibody titration. The assay was linear for concentrations of enzyme in the range of 10 to 120 ng.cm-3. Within-assay and between-assay variations were 12%. The radioimmunoassay described was used to measure the immunoreactive cathepsin D content of the 100 000 x g supernatant fraction of canine myocardial homogenates.
Cardiovasc Res 1981 Feb
PMID:A double antibody radioimmunoassay for canine cardiac cathepsin D. 726 Sep 78

We tested the hypothesis that ischemic postconditioning (IPost) induces autophagy and the activation of autophagy contributes to the cardioprotective effects against ischemia/reperfusion injury in rat hearts. Rats were subjected to IPost established by 3 cycles of 10-second reperfusion followed by 10-second ischemia at the end of 30-minute ischemia. The activation of autophagy was assessed by the morphological and biochemical examinations after 120-minute reperfusion in ventricular tissue. To investigate the contribution of autophagy to IPost, the rats were pretreated with the autophagy inhibitor 3-methyl-adenine (3-MA). We found that IPost increased the formation of autophagic vacuoles, the autophagic-related protein levels of LC3-II, Beclin1, lysosome-associated membrane protein 2, and cathepsin D, and the mRNA level of LC3 and Beclin1 in the risk zone of the postconditioned hearts. Furthermore, 3-MA treatment significantly reversed the reduction effect of IPost on infarct volume, and in the meantime, inhibited the induction of LC3 and Beclin1. In addition, 3-MA treatment inhibited the antiapoptotic-related protein levels of Bcl-2 and increased the apoptotic-related protein levels of Bad. Taken together, these results indicate that the protective effects of IPost are associated with the activation of autophagy in rat hearts.
J Cardiovasc Pharmacol 2013 May
PMID:Activation of autophagy in ischemic postconditioning contributes to cardioprotective effects against ischemia/reperfusion injury in rat hearts. 2336 9

Cathepsins are proteolytic enzymes typically located within the lysosomes of macrophages. Once released, they can enhance the inflammatory process in atherosclerosis. Cathepsin X aids in the migration of T-lymphocytes and the release of cytokines. Cathepsin D modifies low-density lipoprotein to promote its uptake by macrophages and its subsequent foam cell formation. Furthermore, cathepsin D regulates apoptosis. Cathepsin B degrades the extracellular matrix within the arterial intima. Together, they increase plaque vulnerability. This evidence suggests that cathepsins play an important role in the pathogenesis of atherosclerosis.
Am J Cardiovasc Dis 2016
PMID:The function of cathepsins B, D, and X in atherosclerosis. 2807 76


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