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)

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.
 ...
PMID:Creatine: a possible stimulus skeletal cardiac muscle hypertrophy. 12 40

The distribution of cathepsins E and D in various rat tissues and blood cells was determined by immunoprecipitation and by immunohistochemistry with discriminative antibodies specific for each enzyme. While cathepsin D was detected in all of the tissues and blood cells tested (except for erythrocytes), cathepsin E had a relatively limited distribution. The cathepsin E content was highest in the stomach and was succeeded in the following order by the urinary bladder, thymus, spleen, cervical lymph node and bone marrow. Significant amounts of cathepsin E were also found in the colon, rectum, jejunum, skin, lung, kidney and submandibular gland. The other tissues tested had little or no detectable cathepsin E content. Of the blood cells tested, lymphocytes and peritoneal neutrophils contained high levels of cathepsin E. Erythrocytes had cathepsin E only as aspartic proteinases. When the subcellular localization of cathepsin E in the neutrophils was investigated by fractionation of the postnuclear supernatants, the enzyme behaved as a soluble cytosolic enzyme. In contrast, cathepsin D was mainly associated with the granular fraction. The immunohistochemical localization of cathepsins E and D was clearly different in the stomach, large intestines, kidney and urinary bladder, but was similar in the lymph node and spleen. The tissue-fixed macrophages, which were notable in the skeletal and cardiac muscle tissues, submucosal layers of the gastrointestinal tracts, salivary gland, lung and trachea, also exhibited similar intense immunoreactivities demonstrative of both cathepsins E and D.
 ...
PMID:Quantitation and immunohistochemical localization of cathepsins E and D in rat tissues and blood cells. 265 14

The activities of several lysosomal enzymes were assayed in control and in exercise-hypertrophied cardiac muscle of mice (Mus musculus). The repeated running program increased the activity of beta-glucuronidase (16.1%) in mouse cardiac muscle. Decreased activities of beta-N-acetylglucosaminidase (10.8%), acid ribonuclease (10.7%), and arylsulphatase (14.2%) were observed in the hypertrophied myocardium. The activities of acid deoxyribonuclease, cathepsin C, cathepsin D, and p-nitrophenylphosphatase as well as the activities of citrate synthase and cytochrome c oxidase, mitochondrial enzymes, were unaffected in cardiac muscle. We suggest that lysosomal enzyme responses are selective and highly different in physiologically and pathologically induced cardiac hypertrophies.
 ...
PMID:Changes in lysosomal enzyme activities in exercise-induced cardiac hypertrophy of mice. 622 47

The role of cardiac lysosomal and nonlysosomal protease alterations in the development of the cardiomyopathy that occurs in genetically diabetic C57BL/KsJ db/db mice has been examined. The db/db mice and age-matched controls were sacrificed between 7 and 24 weeks of age. Cathepsin D activity, myofibrillar alkaline protease (MAP) activity (including serine protease activity), and Ca2+-activated protease activity were determined by using [3H]acetyl-casein as substrate. There is a significant decrease in cathepsin D, MAP, and serine protease activities in the myocardium of 7- to 20-week old diabetic mice with a rebound of these activities toward normal levels by 24 weeks of age. Cathepsin D and MAP activities are inversely related to heart weight in diabetic mice with the higher levels being recorded in association with the most pronounced decrease in heart weight. In contrast, Ca2+-activated protease activity in the hearts of diabetic mice does not differ significantly from controls throughout the period of observation. The results suggest that both lysosomal cathepsin D and nonlysosomal MAP may mediate the accelerated cardiac muscle degradation that occurs in the late stage of diabetic cardiomyopathy in the db/db mice.
 ...
PMID:Lysosomal and nonlysosomal proteolytic activities in experimental diabetic cardiomyopathy. 632 62

Two-kidney, one clip Goldblatt hypertension of 2, 4 and 8 weeks duration was induced in 100-g male Wistar-Kyoto rats. Nucleic acid content was determined in the isolated cardiac muscle cells from the left ventricle. The profile for several major proteolytic activities in either isolated cardiac muscle cells or left ventricle preparations was also studied, using [3H]acetyl-casein as substrate. From the soluble fraction of the tissue or cell preparation, a pH 6 proteolytic activity, two forms of calcium-activated protease as well as cathepsin D were identifiable by inhibitor assay or DEAE-cellulose chromatography. From the myofibrillar fraction of the same preparation, two kinds of proteolytic activity were detected at alkaline pH: a phenylmethylsulfonyl fluoride (PMSF) inhibitable activity that was serine protease-like and the other a N-ethylmaleimide (NEM) inhibitable activity that resembled Ca2+-activated protease. At 2 weeks of hypertension, there was a significant increase in the pH 6 proteolytic activity as well as the calcium-activated protease I and the NEM-inhibitable alkaline protease activities, while the other identifiable proteolytic activities remained unchanged. Lysosomal cathepsin D showed a rise in activity only after 8 weeks of hypertension. These results may be related to the development of myocyte necrosis and lysis that occur in this model of hypertensive cardiomyopathy.
 ...
PMID:Proteolytic activities in hypertensive cardiomyopathy of rats. 634 96

Renin-like activity in the heart and aorta of rats being slightly modified by binephrectomy, its variations in DOCA hypertension and infarcted ventricular muscle were studied. The daily i.p. administration of DOCA 12 mg/kg body weight for 35 days in male adult rats resulted in a significant decrease of renin activity in plasma and tissues of the heart, aorta, hypothalamus and hypophysis. In contrast to renin-like activity, cathepsin D measured in the same animals increased in all organs, except for the plasma. Similar changes of renin-like activity were observed in salt-loaded animals with 1.7% sodium chloride solution ad libitum for 35 days. In the infarcted myocardial ventricular muscle of the rats and rabbits, the tissue isorenin showed a tendency to decrease, associated with a significant increase in cathepsin D activity. Like in aorta, isorenin seems to be a different enzymatic entity of cathepsin D in the myocardial tissue. The measurement of isorenin content of the vascular endothelium and cardiac muscle fibers seems to reveal much higher amounts in the coronary vascular endothelium than in the myocardial fibres. The activation of the enzymatic angiotensin forming mechanisms in the coronary vascular bed could be one of the risk factors in myocardial infarction.
 ...
PMID:A comparative study of the renin-like activity in the heart and vascular system under various experimental conditions. 642 49

The activities of beta-glucuronidase and cathepsin D and the protein concentration were assayed from brain, kidney, liver, cardiac muscle and skeletal muscle (m. rectus femoris) samples from mice (Mus musculus) 1, 3, and 6 days after intermittent exhaustive (duration 100-145 min) and submaximal prolonged (duration 9 hr) running on treadmill. The activity of beta-glucuronidase in skeletal muscle strongly increased being the highest 3 days after both exertions. Cathepsin D activity also slightly increased. In cardiac muscle beta-glucuronidase activity was unaffected. Cathepsin D activity slightly increased 3 days after intermittent exhaustive exercise. The specific activities of beta-glucuronidase and cathepsin D in the liver increased 1 day after the both exertions. Simultaneously the protein concentration decreased. In the kidney beta-glucuronidase activity and protein concentration were unaffected but cathepsin D activity decreased 1 day after intermittent exhaustive exercise. In the brain protein concentration transiently decreased 3 days after the exertions. beta-Glucuronidase activity transiently decreased 1 day after intermittent exercise thereafter increasing 6 days afterwards above the control level. Cathepsin D activity decreased 1 day after intermittent exercise but was unaffected after prolonged submaximal exercise. Physical stress affected to varying extent the acid hydrolase activities in all organs studied.
 ...
PMID:Acid hydrolase activity in tissues of mice after physical stress. 664 Nov 64

Male NMRI-mice, aged 3, 6, 9, and 12 months, were made to run for a period of 4 4 at a speed of 13.5 m/min on a motor-driven treadmill, 5 days after exertion, selected enzymatic estimates of acid and alkaline proteolytic as well as energy metabolic capacities were analyzed from the cardiac muscle and from the red and white parts of m. quadriceps femoris (MQF). The activities of alkaline and myofibrillar proteases increased most considerably in skeletal muscles with age. Cathepsin D and beta-glucuronidase activities were less affected in both muscles. Prolonged running increased the activities of cathepsin D, dipeptidyl aminopeptidase I and beta-glucuronidase in the white and, especially in the red part of MQF. This stimulation of acid hydrolytic capacity was more prominent at the ages of 3 and 6 months than in the older animals. The estimates of alkaline proteolytic or energy metabolic capacities were not affected by prolonged running. In cardiac muscle, no significant changes were recorded in acid hydrolytic or energy metabolic capacity. Histological observation showed no necrosis or other pathological phenomena in the proximal part of m. rectus femoris after excretion. We suggest that the increased acid proteolytic capacity is involved in subcellular regenerative processes of skeletal muscle fibres. The smaller lysosomal response of older mice may indicate a reduced potential capacity for cellular repair.
 ...
PMID:Effects of age and prolonged running on proteolytic capacity in mouse cardiac and skeletal muscles. 702 79

Acid hydrolase activities in skeletal and cardiac muscle were studied 5, 10 and 20 days after exhaustive intermittent running by untrained and endurance-trained mice. Exhaustion increased the activities of cathepsin D, beta-glucuronidase and ribonuclease, but not that of p-nitrophenylphosphatase in skeletal muscle of untrained mice. Activities were highest on the fifth day after exhaustion and decreased during the following two weeks. More intensive loading produced no changes in acid hydrolytic capacity in skeletal muscle of endurance-trained mice. Acid hydrolase activities in cardiac muscle of both untrained and trained mice were unaffected by exhaustive running. It is suggested that exhaustive running causes both lethal and sublethal hypoxic fiber injuries in the skeletal muscle of untrained mice but not in that of endurance-trained mice or in the cardiac muscle of animals of either group. These injuries manifest themselves as fiber necrosis (lethal) and as increased acid hydrolytic capacity in surviving fibers (sublethal).
 ...
PMID:Acid hydrolase activities in mouse cardiac and skeletal muscle following exhaustive exercise. 719 24