scholarly journals ENZYME LEVELS OF INDIVIDUAL NEURONS IN RELATION TO LIPOFUSCIN CONTENT

1970 ◽  
Vol 18 (4) ◽  
pp. 268-270 ◽  
Author(s):  
HILDE E. HIRSCH
Keyword(s):  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Nerve Cell ◽  
Lysosomal Enzymes ◽  
Anterior Horn ◽  
Single Neurons ◽  
Histochemical Methods ◽  
Lipofuscin Granules ◽  
Individual Human

By quantitative histochemical methods, activities of (α-naphthyl) acid phosphatase and β-galactosidase, and of malate and lactate dehydrogenase, were measured in individual human anterior horn nerve cell bodies selected for high and low lipofuscin content. No significant differences were found. However, when single neurons were subdivided into pigmented and unpigmented portions, the two lysosomal enzymes were considerably more active, and malate and lactate dehydrogenase less active, in the lipofuscin-rich part of the cell. These results are consistent with the view that lipofuscin granules are derived from lysosomes.

Interpretation of Hyperamylasemia in Diabetic Coma

1973 ◽  
Vol 19 (4) ◽  
pp. 387-389 ◽  
Author(s):  
Francesco Belfiore ◽  
Elena Napoli
Keyword(s):  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Enzyme Activities ◽  
Lysosomal Enzymes ◽  
Amylase Activity ◽  
Diabetic Coma ◽  
Serum Lipase

Abstract In sera of patients with diabetic coma, amylase activity was markedly elevated and closely correlated with the activity of some lysosomal enzymes, including β-glucuronidase, N-acetyl-β-glucosaminidase, and acid phosphatase. All these enzyme activities returned to normal with the normalization of glycemia. Activities of serum lipase, aspartate and alanine aminotransferases, aldolase, and lactate dehydrogenase were not changed. Since liver amylase, although primarily contained in microsomes, shows "latency" and is activated by several agents as are lysosomal enzymes, these findings might be regarded as a further evidence of a similarity between amylase and lysosomal enzymes, and make probable the hypothesis that a process of "activation" occurring in liver might be the cause of increased amylase activity in serum as well as of lysosomal enzymes.

scholarly journals A novel method for the study of autophagy: destruction of hepatocytic lysosomes, but not autophagosomes, by the photosensitizing porphyrin tetra(4-sulphonatophenyl)porphine

1997 ◽  
Vol 321 (1) ◽  
pp. 217-225 ◽  
Author(s):  
Per Eivind STRØMHAUG ◽  
Trond Olav BERG ◽  
Kristian BERG ◽  
Per O. SEGLEN
Keyword(s):  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Proteinase Inhibitor ◽  
Lysosomal Enzymes ◽  
Rat Hepatocytes ◽  
Isolated Hepatocytes ◽  
Major Fraction ◽  
Microtubule Inhibitor ◽  
Novel Method

A photoactivatable porphyrin, tetra(4-sulphonatophenyl)porphine (TPPS4), was shown to accumulate in rat hepatocytes as a linear function of dose after intravenous injection, and to localize predominantly in hepatocytic lysosomes. A major fraction of the lysosomal enzymes acid phosphatase and N-acetyl-β-d-glucosaminidase was inactivated by TPPS4 after 20 h of contact with the drug in vivo in the absence of photoactivation. On exposure of isolated hepatocytes to light, photoactivated TPPS4 caused additional inactivation of the lysosomal enzymes as well as inactivation of intralysosomal lactate dehydrogenase (LDH), a cytosolic enzyme that accumulated in lysosomes as a result of autophagy during a 2 h incubation of hepatocytes at 37 °C in the dark (in the presence of the proteinase inhibitor leupeptin to prevent degradation of intralysosomal LDH). Photoactivation of TPPS4 also induced lysosomal rupture, with a loss of lysosomal enzymes, autophagocytosed LDH, endocytosed 125I-tyramine-cellobiose-asialo-orosomucoid and TPPS4 from the lysosomes. However, LDH-containing autophagosomes, accumulated in the presence of vinblastine (a microtubule inhibitor used to prevent the fusion of lysosomes with autophagosomes or endosomes), were not affected by TPPS4. TPPS4 may thus be useful as a selective lysosomal (or endosomal) perturbant in the study of autophagic–endocytic–lysosomal interactions.

Comparison of human and murine isolates of Schistosoma mansoni from Richard-Toll, Senegal, by isoelectric focusing

1997 ◽  
Vol 71 (2) ◽  
pp. 175-181 ◽  
Author(s):  
M. Sène ◽  
P. Brémond ◽  
J.P. Hervé ◽  
V.R. Southgate ◽  
B. Sellin ◽  
...  
Keyword(s):  
Genetic Variation ◽  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Schistosoma Mansoni ◽  
Isoelectric Focusing ◽  
Glucose Phosphate Isomerase ◽  
Glucose Phosphate ◽  
Enzyme Systems ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Arvicanthis Niloticus

AbstractStudies on human and murine isolates of Schistosoma mansoni, from Richard-Toll, Senegal, were carried out by isoelectric focusing in polyacrylamide gels. Seven enzyme systems; lactate dehydrogenase (LDH), malate dehydrogenase (MDH), glucose-6-phosphate dehydrogenase (G6PD), acid phosphatase (AcP), hexokinase (HK), glucose phosphate isomerase (GPI), and phosphoglucomutase (PGM), were used to compare the two isolates. All systems tested, apart from LDH, were found to be polymorphic for both isolates. Interestingly, one phenotype is more frequent than the remainder. The results show that there is no significant genetic variation between the S. mansoni isolates from man and the rodents, Arvicanthis niloticus and Mastomys huberti.

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.

Aggregation and release in thrombocytes of the duck

1975 ◽  
Vol 229 (1) ◽  
pp. 206-210 ◽  
Author(s):  
RA Stiller ◽  
FA Belamarich ◽  
D Shepro
Keyword(s):  
Acid Phosphatase ◽  
Platelet Aggregation ◽  
Lactate Dehydrogenase ◽  
Adenine Nucleotides ◽  
Intracellular Enzyme ◽  
Release Reaction ◽  
No Release ◽  
Metabolic Pool ◽  
Enzyme Markers ◽  
Induced Aggregation

Avian thromboyctes are aggregated by a number of substances that cause platelet aggregation, and evidence suggests that this response is related to the release of serotonin (5-hydroxytryptamine, 5-HT) from intracellular granules. In this study duck thrombocytes released 5-HT during collagen-induced aggregation, but thrombocytes incubated with 14C-labeled adenine did not release radioactive adenine nucleotides. These results indicate the existence of a metabolic pool of adenine nucleotides that is separate from released constituents of the cell. No unlabeled adenine compounds were detected in the supernatants of aggregated thrombocytes indicating either the rapid alteration of released nucleotides or the absence of a specific release pool of adenine nucleotides. Finally there is no release of the intracellular enzyme markers, lactate dehydrogenase, beta-glucuronidase, and acid phosphatase, during collagen-induced aggregation. These findings suggest that avian thrombocytes exhibit a specific release reaction and that serotonin acts as the functional counterpart of ADP in platelet aggregation.

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.

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