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)

beta-glucuronidase, cathepsin D, acid and alkaline phosphatases were studied in rhesus monkey endometrium during the menstrual cycle (day -6 to day +10) and pre-implantation stages (day +3 to day +6) of gestation, with day 0 considered as the day of ovulation. Acid hydrolases exhibited low levels in proliferative phase endometria followed by their gradual rise in the secretory phase of the menstrual cycle. Despite no shifts in the levels of serum progesterone and estradiol-17 beta, the pre-implantation period was, however, associated with distinct changes in enzyme profiles characterized by lower absolute levels (P less than 0.05) of acid phosphatase and beta-glucuronidase on days 3 to 6 of gestation, whereas cathepsin D activity declined significantly (P less than 0.05) on days 5 and 6. Alkaline phosphatase showed a characteristic rise during the pre-ovulatory period with a gradual lowering of its level in post-ovulatory phase endometria of a non-fertile cycle; in contrast, during early gestation, alkaline phosphatase activity showed a marked elevation (P less than 0.05) on days 5 and 6 of gestation. The significance of these findings is discussed.
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PMID:Endometrial phosphatases, beta-glucuronidase and cathepsin D during menstrual cycle and pre-implantation stages of gestation in the rhesus monkey (Macaca mulatta). 338 45

Rabbits were injected intracerebrally with aluminum salt leading to experimental neurofibrillary change formation as a model of Alzheimer neurofibrillary change. Eleven days after the injection, the brain tissues were excised from the cortex, hippocampus, and cervical region of spinal cord. Five lysosomal enzymes (cathepsin D, beta-glucuronidase, acid phosphatase, acid DNase, alkaline DNase) were assayed and compared with the control. Cathepsin D, acid DNase and beta-glucuronidase activities increased significantly in all 3 areas of aluminum-injected brain. On the other hand, acid phosphatase and alkaline DNase activities remained at the same level. The results showed the lysosomal enzymes did not change in parallel after aluminum administration, suggesting a role of the increased enzymes in the brain with neurofibrillary changes.
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PMID:Activities of lysosomal enzymes in rabbit brain with experimental neurofibrillary changes. 339 97

Live or heat killed (30 min at 56 degrees C) Chlamydia psittaci elementary bodies (EB) were phagocytosed by mouse peritoneal macrophages. Inoculation with killed Chlamydia caused rises in three lysosomal enzyme activities tested, especially in acid phosphatase activity. In contrast, after infection with live Chlamydia, only a negligible increase was seen in acid phosphatase activity, and no change in the activities of beta-glucuronidase and cathepsin D was observed. It was concluded that regulation of lysosomal enzyme synthesis in macrophages may be linked to signals mediated by phago-lysosome fusions.
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PMID:The effect of intracellular Chlamydia psittaci on lysosomal enzyme activities in mouse peritoneal macrophages. 344 38

Considerable progress has been made in the localization of chemical substances within the gas-exchange zones of vertebrate lungs since cytochemical techniques suitable for use with the electron microscope have been developed. The light microscope, an instrument with an effective resolution limit of about 0.2 micron, is ill-suited for studying regions such as these where small tissue elements are arranged in a complex manner. A wide range of acid hydrolases have been detected in the vacuoles and dense bodies of alveolar macrophages by means of cytochemical techniques. The enzymes demonstrated in this way include acid phosphatase, aryl sulphatase, cathepsin D, beta-glucuronidase, acetyl glucosaminidase, nonspecific esterase, dipeptidyl peptidase II and dipeptidyl peptidase IV. Such enzymes are, of course, to be expected in the lysosomes of cells which have a primary phagocytic role. Nevertheless, it must be confessed that very little is yet known about the actual mechanism of phagocytosis or of the fate of the digested material. It is fortunate, however, that some of the tools which are likely to be of value in research on these aspects of macrophage function are currently being developed. Of particular interest in this connection are the immunocytochemical techniques which permit the localization of surface-associated antigens and intracellular contractile proteins. It must be emphasized that phagocytosis is not the only function of macrophages in the gas-exchange zone of the lung. These cells are thought to be involved in the presentation of exogenous antigenic material to the reactive cells of the lymphoid system. Recent research has also indicated that mammalian alveolar macrophages synthesize a diverse range of substances. Furthermore, the elastases associated with pulmonary macrophages are now thought to be involved in the pathogenesis of emphysema. All of the above-mentioned activities are of great biological and clinical significance and, consequently, merit the cytochemists' attention in future. The epithelial lining of the greater part of the pulmonary gas-exchange area is composed of type I pneumonocytes. In terms of ultrastructure, these are very specialized cells; their extensive and highly-attenuated cytoplasmic processes form the outer layer of the air-blood barrier. No special carrier systems have been identified within type I pneumonocytes and this is in keeping with the claims that oxygen is transferred across the alveolar tissue barrier by a process of simple diffusion. Type II pneumonocytes, in contrast, have considerable metabolic activity.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Cytochemistry of the gas-exchange area in vertebrate lungs. 355 66

Effect of diltiazem on subcellular distribution of lysosomal enzymes, high-energy phosphate metabolism and mechanical function in the ischemic heart was studied. Ischemia was induced by lowering the afterload pressure of the perfused working rat heart. The activities of cathepsin D, beta,N-acetylglucosaminidase and acid phosphatase were determined in the nonsedimentable and sedimentable fractions after centrifugation of the tissue extract to assess the subcellular distribution of lysosomal enzymes. After ischemia, decreases in the mechanical function and the tissue level of high-energy phosphates were observed. In addition, ischemia caused subcellular redistribution of lysosomal enzymes from the lysosomes to the cytoplasm. Reperfusion of the ischemic heart did not restore the mechanical function and the level of high-energy phosphates completely. Diltiazem (2.21 X 10(-6), 1.11 X 10(-5) and 2.21 X 10(-5) M) was provided for the heart 5 min before the onset of ischemia. Diltiazem preserved high-energy phosphates in the ischemic heart, and inhibited the subcellular redistribution of lysosomal enzymes being caused by ischemia, depending on its concentration. Reperfusion after ischemia with diltiazem recovered the mechanical function that had been decreased by ischemia. These results may indicate that diltiazem can protect the myocardium against ischemic damage.
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PMID:Inhibition of ischemia-induced subcellular redistribution of lysosomal enzymes in the perfused rat heart by the calcium entry blocker, diltiazem. 365 10

Alterations in activity of lysosomal acid phosphatase and cathepsin D, as well as of hepatocyte ultrastructure were studied in rat liver tissue after experimental heart arrest within 10 and 30 min and during the early post-resuscitation period. Cathepsin D free activity in a supernatant fraction as well as both enzymatic activities in lysosomal fraction were increased after 30 min heart arrest. Activity of acid phosphatase and cathepsin D in lysosomes was decreased, while the activity of the free enzymes was increased within 1 and 4 hrs after resuscitation. Triton X-100 (0.025%) caused labilization of lysosomal membranes. Alterations in ultrastructure of hepatocytes were observed within 30 min of the heart arrest and within first hour of the post-resuscitation period. The lysosomal membranes tended to normalization within 24 hrs after the post-resuscitation period, whereas the enzymatic activity remained elevated. Role of lysosomes in regulation of intracellular metabolism is discussed.
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PMID:[Characteristics of the activation of lysosomal enzymes in the rat liver after death and during resuscitation]. 368 1

In order to investigate the relationship between the synovial inflammatory response and lysosomal enzyme activity in osteoarthritis, synovial specimens obtained from 19 osteoarthritic patients and control specimens from 10 normal joints were analysed for cathepsin D and acid phosphatase enzyme levels. In estimating enzyme activities methods previously developed for quantitative enzyme determination in cartilage were modified and applied to synovial tissues for the first time. In addition, samples of osteoarthritic synovium were histologically graded according to their degree of inflammation. It was found that in osteoarthritic synovium cathepsin D and acid phosphatase, which is a general marker for lysosomal enzyme activity, were significantly increased compared with normal control synovium. No significant relationship was found between the degree of synovial tissue inflammation and lysosomal enzyme activity.
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PMID:Biochemical and histological changes in osteoarthritic synovial membrane. 370 18

A quantitative study was carried out on the lysosomal enzyme activities of the bovine corneal endothelium-Descemet's membrane preparation. The corneal endothelium and Descemet's membrane were peeled off together. Cathepsin D was assayed using hemoglobin as substrate; N-acetyl-beta-D-glucosaminidase, beta-glucuronidase, acid phosphatase, and alpha-mannosidase were also examined using p-nitrophenyl derivatives as substrate. The proportions of N-acetyl-beta-D-glucosaminidase, cathepsin D, and beta-glucuronidase of the Descemet's membrane-endothelium complex were particularly high: 11.5%, 12.6%, and 12.5% of the whole cornea, respectively. Corneal endothelial cells also showed high activities of acid phosphatase and alpha-mannosidase (3.8%, and 5.0% of the whole cornea, respectively), while the protein and DNA contents were 0.5% and 0.5% in the complex. Lysosomal enzyme activities in the complex were also compared with those in other ocular tissues and were determined by the same methods at the same time.
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PMID:Lysosomal enzyme activities of the bovine corneal endothelium. 371 Jan 95

The activities of acid phosphatase, N-acetyl-beta-D-glucosaminidase, alpha-mannosidase, alpha-fucosidase, beta-glucuronidase, arylsulfatase, and cathepsin D were biochemically investigated in the bovine cornea by separating the tissue into two layers, epithelium and stroma-endothelium. Acid phosphatase, alpha-mannosidase, alpha-fucosidase, and arylsulfatase disclosed much higher activities in the epithelial layer than in the stroma-endothelial layer. The other enzymes showed little difference in enzyme activity between the two layers.
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PMID:Acid hydrolases in the bovine corneal epithelium. 375 93

The effects of chloroquine treatment on horseradish peroxidase (HRP) uptake and lysosomal enzyme activities in innervated and denervated mouse skeletal muscle have been studied using biochemical, histochemical and ultrastructural techniques. Chloroquine treatment caused a large (59-101%) increase in the activity of cathepsin D in both innervated and denervated muscle. The activity of N-acetyl-beta-D-glucosaminidase also increased slightly in denervated muscle. No effect was observed on acid phosphatase activity. The in vivo uptake of HRP in innervated and denervated muscle was unaffected by chloroquine treatment. The results show that the activities of certain lysosomal enzymes may increase in skeletal muscle without an increase in endocytic activity. This is discussed in comparison to what is seen in denervated and dystrophic muscle. Histochemical and ultrastructural studies showed the HRP uptake to occur segmentally in denervated muscle fibres from untreated as well as chloroquine-treated animals. Ultrastructurally the peroxidase-positive phagosomes occurring in these segments were found to contain increased levels of undegraded material after chloroquine treatment suggesting that these phagosomes are of a lysosomal nature and also participate in autophagic processes.
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PMID:Biochemical and ultrastructural effects of chloroquine on horseradish peroxidase uptake and lysosomal enzyme activities in innervated and denervated mouse skeletal muscle. 376 Sep 8


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