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)

These experiments test whether creatine, a product of muscular contraction, stimulates myofibrillar protein synthesis. It was found that skeletal muscle cells formed both in vitro and in vivo and cardiac muscle cells formed in vivo synthesize myofibrillar proteins faster when supplied creatine in vitro. The rates of synthesis and/or accumulation of three myofibrillar proteins-myosin heavy chain actin, and creatine kinase-were stimulated by creatine. In contrast, the rates of synthesis of total protein and of deoxyribonucleic acid (DNA) and the activities of several nonmyofibrillar enzymes were not altered by creatine. These include lactic dehydrogenase, cathepsin D, acid phosphatase, and beta-acetylglucosaminidase. It is concluded that creatine selectively stimulated the rate of synthesis of contractile proteins in skeletal and cardiac muscle in vitro and may play a role in muscle hypertrophy.
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PMID:Creatine: a possible stimulus skeletal cardiac muscle hypertrophy. 12 40

We studied the effects of prolonged running exercise (5 days a week, 1.5 h per day at a speed of 17.6 m/min) on the activity of some acid hydrolases (beta-glucuronidase, beta-N-acetylglucosaminidase, acid phosphatase and cathepsin D) and three enzymes of energy metabolism (cytochrome c oxidase, lactate dehydrogenase and creatine kinase) in the distal and in the proximal, the predominantly white and red parts, respectively, of the vastus lateralis-muscle from mice. The acid hydrolase activity levels were 1.24--1.69 higher in untrained red muscle compared to untrained white muscle. The light training applied increased the activity of beta-glucuronidase in both red and white muscle. No other significant training effects were observed in the enzyme activities measured.
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PMID:beta-Glucuronidase activity in trained red and white skeletal muscle of mice. 21 65

In fetal mouse hearts in organ culture the rate of protein synthesis was substantially reduced and the rate of protein degradation slightly increased by hydrocortisone in the absence of insulin, but in the presence of insulin the steroid caused a small increase in protein synthesis and a significant reduction in protein degradation. Hydrocortisone promoted the net uptake (or reduced the net release) of branched-chain amino acids independent of insulin and independent of simultaneous changes in protein balance. The specific activities of the lysosomal enzymes cathepsin D and glucosaminidase were reduced by hydrocortisone in all media, whereas the specific activity of creatine kinase increased when the medium contained insulin but decreased in the absence of insulin. It is concluded that hydrocortisone regulates cardiac protein balance via alterations both in synthesis and in degradation. Some of the hormone's myocardial effects are influenced by insulin so that hydrocortisone is anabolic in its presence but catabolic in its absence.
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PMID:Regulation of cardiac protein balance by hydrocortisone: interaction with insulin. 62 46

Cats of either sex anesthetized with sodium pentobarbital (30 mg/kg, IV) were subjected to sham pericardial tamponade or pericardial tamponade for five hours. Five cats underwent sham pericardial tamponade and six cats were subjected to pericardial tamponade which reduced the mean arterial blood pressure to approximately 40 mm Hg. Pericardial tamponade produced a 44-51% and a 28-38% decrease in the myocardial activities of cathepsin D and creatine phosphokinase (CPK), respectively. Observation of cellular and subcellular structure of left ventricular tissue of two sham operated cats and two cats after tamponade revealed myocardial injury in cats subjected to tamponade. Tissue stained with hematoxylin-basic fuchsin-picric acid stain showed extensive crimson-red basic fuchsin staining in cats subjected to pericardial tamponade and the absence of staining in cardiac tissue of sham-operated cats. Electron micrographs of cardiac tissue of cats subjected to acute pericardial tamponade revealed extensive vacuolization and extreme contracture. These results indicate ischemic injury with loss of cellular and subcellular enzymes in hearts of cats after five hours of pericardial tamponade sufficient to reduce the mean arterial blood pressure to about 40 mm Hg.
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PMID:Pericardial tamponade-induced myocardial ischemic injury. 70 32

The ability of increased circulating activities of lysosomal hydrolases to disrupt myocardial cellular membranes was studied in anesthetized cats. Increased activities of lysosomal hydrolases were achieved by splanchnic artery occlusion (SAO) shock or by infusion of liver extract (LE). Myocardial ischemia (MI) was produced by ligation of the left coronary artery. Coronary artery ligation resulted in sustained S-T segment elevation associated with significant increases in plasma creatine phosphokinase (CPK) activity within 5 hours. Combinations of SAO or LE infusion did not modify the increase in either the plasma CPK activity or the S-T segment following MI. However, SAO shock or infusion of LE increased CPK loss from normal and ischemic myocardium, the loss being greater when MI was combined with infusion of LE or SAO shock. Similarly, MI plus SAO shock increased the loss of the lysosomal protease cathepsin D from normal and ischemic myocardial tissue. Moreover, cats subjected to MI and given LE inhibited increased mortality and decreased clearance of infused lysosomal hydrolases. These results indicate that conditions affecting increased plasma levels of hydrolases promote increased disruption of normal and ischemic myocardial tissue. These findings are consistent with the concept that hydrolases originating in the splanchnic viscera during shock play a role in enhancing damage to normal and ischemic myocardial tissue following coronary artery occlusion.
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PMID:Influence of increased circulating levels of splanchnic lysosomal enzymes on the response to myocardial ischemia. 113 31

The purpose of the present study was to analyze the effectiveness of different biochemical markers used clinically or proposed for the post mortem diagnosis of myocardial infarction in medico-legal practice. We analyzed seven biochemical parameters (CK, CK-MB, LDH, myoglobin, myosin, cathepsin D and total proteins) in pericardial fluid, vitreous humor and femoral vein serum from 34 cadavers. The results were compared with data from macro- and microscopic studies. Our results suggest that biochemical markers are applicable in cases in which the lack of morphological data makes diagnosis uncertain, and are helpful in ruling out myocardial infarction. The sample material of choice for biochemical tests is the pericardial fluid, and the most informative markers are myoglobin, myosin, CK-MB and cathepsin D.
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PMID:Biochemical and morphological markers in the post mortem diagnosis of ischemic heart distress. 213 59

The enzymatic activity of creatine phosphokinase and the lysosomal enzymes cathepsin D and acid phosphatase was followed during skeletal muscle regeneration after partial excision to the gastrocnemius muscle in the rat. For each time interval (1, 2, 5, 14 and 45 days) following injury, the activity of the regenerated muscle was compared with the activity in the contralateral sham operated muscle. The specific activity of creatine phosphokinase of the regenerated muscle showed a significant decrease (25%) during the first 2 days post injury and thereafter was comparable to that of the uninjured control muscle. The activity of cathepsin D was 2.3-4-fold significantly higher in the regenerated muscle than in the control intact muscle from day 1 until day 14 post-injury. At 45 days after partial excision, the activity of this enzyme was comparable to a normal muscle. However, the activity of another lysosomal enzyme (acid phosphatase) did not show any distinct changes from the level of this enzyme in the uninjured muscle during the course of muscle regeneration. It is suggested that elevation of lysosomal enzymes in skeletal muscle may not be confined to conditions of muscle wasting and degradation but also to differentiation and development processes such as during muscle regeneration following injury.
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PMID:Proteolytic enzyme activities during regeneration of the rat gastrocnemius muscle. 224 25

We examined the effects of tiapamil, a Ca2+ antagonist, on infarct size, lymphatic enzyme release, and arrhythmias in reperfused, ischemic canine hearts. Three-hour reperfusion of the left anterior descending coronary artery, which had been ligated for 3 h, significantly increased cardiac lymphatic release of lactate dehydrogenase (LDH), cathepsin D and creatine phosphokinase (CPK), and the incidence of ventricular premature contractions (VPCs), the increases being markedly higher than those in ligation period. Tiapamil, at the i.v. dose of 3 mg/kg/h for 6 h during the ligation and reperfusion periods markedly reduced these increases in lymphatic levels of LDH and cathepsin D and in VPCs, and significantly decreased infarct size. Tiapamil treatment only during the ligation period had similar preserving effects, but tiapamil treatment only during reperfusion did not. These results suggest that blockade of the Ca2+ channel must be achieved during the early phase of an ischemic episode in order to prevent myocardial deterioration during reperfusion.
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PMID:Protection by the calcium antagonist tiapamil, against cardiac lymphatic enzyme leakage and arrhythmias in canine hearts during reperfusion. 241

The development of a model of chronic myocardial ischemic injury (MII) in rabbits by administering increasing doses of isoproterenol (ISO) is described. Repeated s.c. injections of increasing doses of ISO (0.5 mg/kg, on day 1 to 15.5 mg/kg, on day 15) resulted in an increase in serum glucose, free fatty acids and creatine phosphokinase. Examination of hearts from ISO-treated rabbits revealed marked hypertrophy of the left ventricle and an increase in total water content. Biochemical analysis showed an increase in left ventricular hydroxyproline and a decrease in ATP and glycogen content following ISO-treatment. Ion measurements revealed extensive accumulation of Na and Ca, with the Ca being preferentially accumulated in the mitochondria. Measurement of subcellular organelle marker enzymes showed decreases in the sarcolemmal Na+-K+-stimulated (ouabain-sensitive), mitochondrial (azide-sensitive) and sarcoplasmic reticulum ATPase activities in the ISO-treated animals. Analysis of lysosomal enzyme activities in myocardial homogenates showed significant decreases in the latency of N-acetyl-beta-glucosaminidase and cathepsin D. The above biochemical alterations in ISO-induced MII generally parallel changes previously seen in the rabbit following acute coronary artery ligation. The present model allows the study of MII uncomplicated by some uncertainties arising from the surgical or anesthetic procedures employed in acute "open-chest" preparations and would permit long-term follow-up studies of pharmacological interventions. The susceptibility of the rabbit to experimental atherosclerosis should allow the development of an experimental model of MII which more closely approximates the clinical situation.
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PMID:Myocardial ischemic injury induced by isoproterenol in the rabbit: biochemical and chemical alterations. 385 Jul 74

We studied the potential therapeutic value of the chemically stable carbacyclin analogue ZK 36 375 during acute myocardial ischemia and compared the cardiovascular and anti- and disaggregatory effects of the compound in vitro and ex vivo. In anesthetized cats the left anterior descending coronary artery was ligated, and 30 min later an intravenous infusion of ZK 36 375 (3.6 micrograms/kg X min) or vehicle was initiated and continued for 4.5 h. ZK 36 375 reduced the ST-segment elevation at 2-5 h (p less than 0.01) when compared to vehicle-treated cats. ZK 36 375 significantly inhibited both the loss of creatine phosphokinase--specific activity and the decrease in the percentage of bound cathepsin D in the infarcted area of the myocardium (p less than 0.05). ZK 36 375 did not reverse ischemia-induced formation of platelet aggregates in vivo and was found ex vivo to be two to three orders of magnitude less active in preventing platelet aggregation, redispersing platelet aggregates, and relaxing bovine coronary arteries than prostacyclin (PGI2) or its (5E) stereoisomer ZK 36 374. It is concluded that ZK 36 375 has a significant cardioprotective activity in acute myocardial ischemia of the cat that can be dissociated from antiplatelet effects in vivo.
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PMID:Dissociation of antiplatelet effects from myocardial cytoprotective activity during acute myocardial ischemia in cats by a new carbacyclin derivative (ZK 36 375). 618 28


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