THE LYSOSOMAL ENZYMES ACID PHOSPHATASE AND β -GLUCURONIDASE IN MUSCLE FOLLOWING A PERIOD OF ISCHAEMIA

1974 ◽  
Vol 52 (1) ◽  
pp. 157-171 ◽  
Author(s):  
AD Shannon ◽  
EP Adams ◽  
FC Courtice
Keyword(s):  
Acid Phosphatase ◽  
Lysosomal Enzymes

scholarly journals Lymphocyte Lysosomes and Lysosomal Enzymes in Chronic Lymphocytic Leukemia

Blood ◽  
1973 ◽  
Vol 41 (4) ◽  
pp. 511-518 ◽  
Author(s):  
Steven D. Douglas ◽  
Georg Cohnen ◽  
Erika KÖnig ◽  
GÜnter Brittinger
Keyword(s):  
Acid Phosphatase ◽  
Lysosomal Enzymes ◽  
Microscopic Level ◽  
Lymphocytic Leukemia ◽  
Electron Microscopic Level ◽  
Acid Hydrolase ◽  
Electron Microscopic ◽  
Normal Cells ◽  
Biochemical Studies ◽  
Cell Profile

Abstract Electron microscopic cytochemical and biochemical studies of lysosomal markers have been performed in unstimulated normal and chronic lymphotic leukemia (CLL) lymphocytes. Decreased activities of the lysosomal enzymes acid phosphatase and β-glucuronidase but not of the nonlysosomal enzyme malate dehydrogenase were observed in CLL lymphocytes as compared to normal cells. At the electron microscopic level, the number of membrane-bounded acid phosphatase-positive organelles was diminished in CLL cells. (Average 1.07 per cell profile in normal cells and 0.17 in CLL lymphocytes). The findings indicate that the diminution of acid hydrolase activities in CLL lymphocytes is most likely due to a reduced number of lysosomes, rather than to a diminished enzyme content of these organelles.

A study of kidney lysosomal acid phosphatase during compensatory renal hyperplasia in rats

1968 ◽  
Vol 46 (3) ◽  
pp. 499-502 ◽  
Author(s):  
B. M. Hegdekar
Keyword(s):  
Acid Phosphatase ◽  
Lysosomal Enzymes ◽  
Soluble Fraction ◽  
Female Rats ◽  
Enzyme Release ◽  
Lysosomal Fraction ◽  
Probable Role ◽  
Long Evans ◽  
Free Activity

Female rats of the Long-Evans hooded strain, 4–6 months old and weighing 275–300 grams, were subjected to unilateral nephrectomy and the acid phosphatase activity in the remaining kidney was studied at the end of 24, 48, 72 hours, and 8 days respectively. Most of the acid phosphatase was found in the particulate fraction in normal kidneys. The enzyme activity in the soluble fraction was found to have increased the second day after the operation, but decreased to the original level by the end of 72 hours. The free activity of the lysosomal fraction also increased by the end of second postoperative day. A change in the permeability of the lysosomal membrane before the enzyme release was observed. The probable role of lysosomal enzymes in the initiation of mitotic divisions during compensatory renal hyperplasia is discussed.

scholarly journals Lysosomal enzymes and vitamin E deficiency

1967 ◽  
Vol 21 (1) ◽  
pp. 147-154 ◽  
Author(s):  
J. Bunyan ◽  
J. Green ◽  
A. T. Diplock ◽  
D. Robinson
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Lysosomal Enzymes ◽  
Hydrolytic Activity ◽  
Liver Necrosis ◽  
Lysosomal Hydrolases ◽  
Vitamin E Deficiency ◽  
Nitrophenyl Phosphate ◽  
Liver And Kidney ◽  
Testicular Degeneration

1. The activities of several lysosomal hydrolases have been measured in tissues of rats with nutritional liver necrosis. Incipient or actual liver necrosis did not alter total, free or unsedimentable activities of cathepsin, β-glucuronidase, β-galactosidase or acid phosphatase of liver and kidney. Free hydrolytic activity towards p-nitrophenyl phosphate was slightly raised in liver, and serum β-galactosidase and β-glucuronidase were moderately elevated. These results suggest that lysosomal hydrolases are not directly implicated in the causation of liver necrosis.2. Testicular degeneration was studied with reference to changes in β-giucuronidase activity. This enzyme activity, total, free and unsedimentable, was raised in deficient rat testis at 6 months old and did not decline even after a year. Raised values were also found in serum.

Intralysosomal pH and release of lysosomal enzymes in the rat liver after exhaustive exercise

1993 ◽  
Vol 74 (4) ◽  
pp. 1628-1634 ◽  
Author(s):  
M. Tsuboi ◽  
K. Harasawa ◽  
T. Izawa ◽  
T. Komabayashi ◽  
H. Fujinami ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Rat Liver ◽  
Cathepsin D ◽  
Lysosomal Enzymes ◽  
Osmotic Fragility ◽  
Exhaustive Exercise ◽  
Ammonia Accumulation ◽  
Exercise Induced ◽  
Beta Glucosidase

The mechanism underlying exhaustive exercise-induced release of lysosomal enzymes was studied in the rat liver. Exhaustive exercise resulted in the release of beta-glucuronidase and cathepsin D, but not beta-glucosidase and acid phosphatase, into the blood and cytosol, suggesting that the release of lysosomal enzymes is not due to disruption of lysosomal membranes. The intralysosomal pH of the liver, which was approximately 5.5 at the resting level, rose significantly after exhaustive exercise to pH 6.3. In vitro, beta-glucuronidase and cathepsin D were released at an intralysosomal pH exceeding 6.2. In contrast, beta-glucosidase and acid phosphatase were not released. The elevation of intralysosomal pH reduced the aggregation of beta-glucuronidase and cathepsin D. The rate of ammonia accumulation increased markedly in the lysosome-enriched subcellular fraction after exercise. There was a positive relationship between the rate of ammonia accumulation and the elevation of intralysosomal pH in vitro. Lysosomes isolated after exhaustive exercise showed significantly increased osmotic fragility. Our findings suggest that, during exhaustive exercise, the accumulation of ammonia in lysosomes leads to the elevation of intralysosomal pH, resulting in the reduced aggregation of certain lysosomal enzymes. Thus, less aggregated lysosomal enzymes may be released into the cytosol through the lysosomal membrane, the permeability of which has been increased.

Effect of cysteamine on the lysosomal enzymes of the hyperprolactinaemic rat pituitary

1990 ◽  
Vol 125 (1) ◽  
pp. 75-80 ◽  
Author(s):  
T. M. Jeitner ◽  
J. R. Oliver
Keyword(s):  
Acid Phosphatase ◽  
Lysosomal Enzyme ◽  
Protease Activity ◽  
Lysosomal Enzymes ◽  
Intact Cells ◽  
Enzyme Degradation ◽  
Rat Pituitary ◽  
Prolactin Content ◽  
Inhibited Acid

ABSTRACT The effect of cysteamine on the activity of lysosomal enzymes and the prolactin content of isolated hyperprolactinaemic cells has been investigated. In broken cell preparations, cysteamine markedly stimulated acid prolactin protease activity. In intact cells, however, cysteamine inhibited acid prolactin protease activity and β-galactosidase. Moreover, the activities of α-mannosidase, acid phosphatase, β-glucuronidase, total arylsulphatase and hexosaminidase were not changed by the addition of cysteamine. Cysteamine significantly depleted the cells of prolactin, and this action was not compromized by the inclusion of either leupeptin, chloroquine or NH4Cl in the incubation media. Taken together, these results indicate that cysteamine does not promote degradation of prolactin and hence depletion of prolactin from the pituitary through a mechanism involving lysosomal enzyme degradation. Journal of Endocrinology (1990) 125, 75–80

Toxin-induced activation of muscle hydrolases

1982 ◽  
Vol 60 (1) ◽  
pp. 87-91
Author(s):  
Roland J. Boegman ◽  
Brenda Scarth
Keyword(s):  
Skeletal Muscle ◽  
Acid Phosphatase ◽  
Lysosomal Enzymes ◽  
Normal Values ◽  
Acid Protease ◽  
Mouse Skeletal Muscle

Application of batrachotoxin, lysolecithin, tetrodotoxin, or veratridine to mouse skeletal muscle results in an increase in the activity of the following lysosomal enzymes: acid protease, acid phosphatase, and N-acetylglucosarninidase. Batrachotoxin caused the greatest increase in lysosomal enzymes while veratridine resulted in the smallest response. The increase in lysosomal enzymes was most marked within 1–2 days after toxin application and returned to normal values after 8–12 days.

scholarly journals Low Concentration of a Dioxin (2, 3, 7, 8 TCDD) Affects the Glycosidases and Acid Phosphatase Activity in Mice Hepatocytes

Dose-Response ◽  
2014 ◽  
Vol 12 (4) ◽  
pp. dose-response.1
Author(s):  
Jyoti Jigyasi ◽  
Rahul Kundu
Keyword(s):  
Acid Phosphatase ◽  
Lysosomal Enzymes ◽  
Low Dose ◽  
Liver Cells ◽  
Low Doses ◽  
Present Communication ◽  
Cellular Apoptosis ◽  
Mice Liver ◽  
Intracellular Ions

Present communication reports the effects of environmentally available, low doses of tetra chloro di benzo-p-dioxin (2,3,7,8 TCDD) to lysosomal enzymes in mice liver. The study tests the hypothesis, in vivo exposure of low dose TCDD provokes dose and duration dependent toxic effects to key lysosomal enzymes and thereby causes cellular apoptotic changes. Three groups of female Swiss albino mice were subjected to two doses of TCDD (0.004 mg/kg bw/d, 0.04 mg/kg bw/d) for 2, 4 and 6 days of exposure durations. The results indicated significant exposure duration dependent effects of TCDD in mice liver cells. The results suggested that TCDD possibly induced an increase in intracellular ions or ROS which in turn altered different physiological activities by affecting different metabolic pathway of the liver cells. The altered functions of key lysosomal enzymes by TCDD may also evoke the process of cellular apoptosis.

scholarly journals Source of a Lysosomal Enzymes Acid Phosphatase, in Hemorrhagic Shock

1972 ◽  
Vol 175 (1) ◽  
pp. 19-25 ◽  
Author(s):  
H. Gerald Clermont ◽  
James T. Adams ◽  
James S. Williams
Keyword(s):  
Acid Phosphatase ◽  
Hemorrhagic Shock ◽  
Lysosomal Enzymes

scholarly journals A non-autophagic pathway for diversion of ER secretory proteins to lysosomes.

1992 ◽  
Vol 119 (1) ◽  
pp. 85-97 ◽  
Author(s):  
T Noda ◽  
M G Farquhar
Keyword(s):  
Acid Phosphatase ◽  
Lysosomal Enzymes ◽  
Direct Conversion ◽  
Secretory Proteins ◽  
Beta Subunits ◽  
Enzyme Cytochemistry ◽  
Thyrotrophic Hormone ◽  
Er Membrane

Intracisternal granules (ICG) develop in the rough ER of hyperstimulated thyrotrophs or thyroid hormone-secreting cells of the anterior pituitary gland. To determine the fate of these granules, we carried out morphological and immunocytochemical studies on pituitaries of thyroxine-treated, thyroidectomized rats. Under these conditions the ER of thyrotrophs is dramatically dilated and contains abundant ICG; the latter contain beta subunits of thyrotrophic hormone (TSH-beta). Based on purely morphologic criteria, intermediates were identified that appeared to represent stages in the transformation of a part rough/part smooth ER cisterna into a lysosome. Using immunocytochemical and cytochemical markers, two major types of intermediates were distinguished: type 1 lacked ribosomes but were labeled with antibodies against both ER markers (PDI, KDEL, ER membrane proteins) and a lysosomal membrane marker, lgp120. They also were reactive for the lysosomal enzyme, acid phosphatase, by enzyme cytochemistry. Type 2 intermediates were weakly reactive for ER markers and contained both lgp120 and lysosomal enzymes (cathepsin D, acid phosphatase). Taken together these results suggest that in hyperstimulated thyrotrophs part rough/part smooth ER elements containing ICG lose their ribosomes, their membrane is modified, and they sequentially acquire a lysosome-type membrane and lysosomal enzymes. The findings are compatible with the conclusion that a pathway exists by which under certain conditions, secretory proteins present in the ER as well as ER membrane and content proteins can be degraded by direct conversion of ER cisternae into lysosomes.

scholarly journals Enzymes and proteins in bile Variations in output in rat cannula bile during and after depletion of the bile-salt pool

1981 ◽  
Vol 196 (1) ◽  
pp. 11-16 ◽  
Author(s):  
P P Godfrey ◽  
M J Warner ◽  
R Coleman
Keyword(s):  
Plasma Membrane ◽  
Acid Phosphatase ◽  
Bile Salt ◽  
Bile Salts ◽  
Lysosomal Enzymes ◽  
Protein Concentration ◽  
Enterohepatic Circulation ◽  
Cell Damage ◽  
Membrane Enzymes ◽  
Rat Bile

The protein concentration in bile from several species is reported. The changes in output of protein, bile salts and several enzymes have been followed in rat bile over a 48 h cannulation period. Bile-salt concentration dropped rapidly owing to interruption of the enterohepatic circulation but the output of protein, lysosomal enzymes [acid phosphatase (EC 3.1.3.2) and beta-D-glucuronidase (EC 3.2.1.31)] and plasma-membrane enzymes [5′-nucleotidase (EC 3.1.3.5) and phosphodiesterase I (EC 3.1.4.1)] was maintained. Liver cell damage, monitored by output of lactate dehydrogenase, was very low throughout. Protein, lysosomal enzymes and plasma-membrane enzymes showed different patterns of output with time, but all showed a net increase between 12 and 24 h. The output of lysosomal and plasma-membrane enzymes was between 1 and 5% of the total liver complement over the first 24 h; if inhibition by biliary components is taken into account the output of some of these enzymes, particularly acid phosphatase, may be greater. Ultracentrifugation of bile showed that as the concentration of bile salts decreases the proportion of plasma-membrane enzymes in a sedimentable form increases. The results are discussed in relation to other studies of biliary proteins and to studies of the perturbation of membranes and cells with bile salts.

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