scholarly journals Lysosomal enzymes and vitamin E deficiency

1967 ◽  
Vol 21 (1) ◽  
pp. 127-136 ◽  
Author(s):  
J. Bunyan ◽  
J. Green ◽  
A. T. Diplock ◽  
D. Robinson
Keyword(s):  
Acid Phosphatase ◽  
Subcellular Distribution ◽  
Subcutaneous Tissue ◽  
Hydrolytic Activity ◽  
Breast Muscle ◽  
Lysosomal Hydrolases ◽  
Exudative Diathesis ◽  
Glucuronidase Activity ◽  
Deficiency Diseases ◽  
Increased Activity

1. The activities of several lysosomal hydrolases were measured in the tissues of chicks suffering from nutritional muscular dystrophy, encephalomalacia or exudative diathesis.2. In dystrophic breast muscle, β-glucuronidase was raised five- to six-fold, cathepsin fourfold and acid phosphatase 1.5-fold. No change was found in the subcellular distribution of β-glucuronidase.3. Chicks with encephalomalacia showed no changes in the β-glucuronidase, β-galactosidase, acid phosphatase or β-acetylglucosaminase activities of cerebellum or brain. Subcellular distribution of β-glucuronidase and β-galactosidase in these tissues was also unchanged.4. In exudative diathesis, hydrolases were found in the exudate, and there was increased activity in the subcutaneous tissue first showing haemorrhages. Increased hydrolytic activity was found in liver, spleen and kidney. Breast muscle was not always affected by the exudative condition, but, when it too degenerated, its hydrolase activity increased.5. β-Glucuronidase activity was measured in the serums of chicks suffering from each of the three deficiency diseases. None of the diseases caused a rise in activity.

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.

scholarly journals COMPARATIVE HISTOCHEMICAL LOCALIZATION OF LYSOSOMAL ENZYMES IN RAT TISSUES

1967 ◽  
Vol 15 (2) ◽  
pp. 83-92 ◽  
Author(s):  
MASANDO HAYASHI
Keyword(s):  
Acid Phosphatase ◽  
Mucous Membrane ◽  
Azo Dye ◽  
Lysosomal Enzymes ◽  
Functional Differentiation ◽  
The Other ◽  
Rat Tissues ◽  
Lysosomal Hydrolases ◽  
Intense Reaction ◽  
Glucuronidase Activity

Localization of acid phosphatase, β-glucuronidase and N-acetyl-β-glucosaminidase has been studied in various tissues of the rat with comparable simultaneous coupling azo dye techniques employing naphthol AS-BI compounds as substrates and hexazonium pararosanilin as a capture reagent. These three lysosomal hydrolases were widely distributed in tissues and were generally demonstrated as discrete granules in certain portions of the cytoplasm. Granules stained for each enzyme were localized at identical sites in most, but not all, tissues in which they were present. However, the intensity or number of granules stained for each of the enzymes was found to differ in varying degree among tissues. Acid phosphatase appeared to be more widespread in tissues than the two glycosidases. Distribution of the glycosidases was also found to differ considerably. Cells of the macrophage system, for example, displayed high β-glucuronidase activity, while N-acetyl-β-glucosaminidase was much less active in these cells. The latter enzyme was more active in the epithelium of the mucous membrane. Furthermore, in several tissues, the three enzymes exhibited qualitatively different localization. In these sites, one or two of the enzymes were not or were only faintly demonstrable while the other showed an intense reaction. These findings suggest that a functional differentiation among lysosomes in various tissues may exist.

scholarly journals Lysosomal enzymes and vitamin E deficiency

1967 ◽  
Vol 21 (1) ◽  
pp. 137-145 ◽  
Author(s):  
J. Bunyan ◽  
J. Green ◽  
A. T. Diplock ◽  
D. Robinson
Keyword(s):  
Acid Phosphatase ◽  
Vitamin E ◽  
Lysosomal Enzymes ◽  
Supernatant Fraction ◽  
Galactosidase Activity ◽  
Lysosomal Hydrolases ◽  
Vitamin E Deficiency ◽  
Mean Values ◽  
Glucuronidase Activity ◽  
Peak Value

1. Activities of β-glucuronidase, β-galactosidase, acid phosphatase and cathepsin were measured in the uterine contents of normal rats during gestation and of vitamin E-deficient rats during foetal resorption.2. β-Glucuronidase activity reached a peak value on days 11 and 12, falling to lower values by day 14. Deficient rats showed slightly greater mean values than normal rats on days 11 and 12, but not after that time.3. Vitamin E deficiency did not affect the activities of β-galactosidase, acid phosphatase and cathepsin, all of which showed a slow decrease during pregnancy.4. The supernatant fraction of homogenates of uterine contents from deficient rats showed increased β-glucuronidase and β-galactosidase activity from day 14 to 17, suggesting some degree of rupture of the lysosomal membrane.5. β-Glucuronidase and acid phosphatase activities were raised in the uteruses of some deficient rats towards the end of pregnancy, but serum β-glucuronidase was unaffected.6. Changes in lysosomal hydrolases were not so marked during gestation–resorption as in some other vitamin E deficiency states, such as muscular dystrophy in the chick and rabbit.

scholarly journals Enzyme Histochemical Studies of Adipose Tissue in Porcine Yellow Fat Disease

1974 ◽  
Vol 11 (6) ◽  
pp. 465-476 ◽  
Author(s):  
L. H. J. C. Danse ◽  
W. A. Steenbergen-Botterweg
Keyword(s):  
Enzyme Activity ◽  
Adipose Tissue ◽  
Acid Phosphatase ◽  
Nonspecific Esterase ◽  
Cell Structures ◽  
Increased Activity

Adipose tissue of piglets with yellow fat disease had increased activity of nonspecific esterase, 5-nucleotidase, and acid phosphatase. Since these enzymes are associated with different cell structures and damage to these structures can result in increased enzyme activity, they are criteria for pathogenetic study of yellow fat disease.

scholarly journals BETA GLUCURONIDASE-RICH CYTOPLASMIC PARTICLES IN ANDROGEN-STIMULATED MOUSE KIDNEY

1963 ◽  
Vol 16 (2) ◽  
pp. 253-258 ◽  
Author(s):  
Andrew G. Plaut ◽  
William H. Fishman
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Specific Activity ◽  
Mouse Kidney ◽  
The Other ◽  
Mouse Testis ◽  
Glucuronidase Activity ◽  
Other Hand ◽  
Fraction I ◽  
Gonadotropic Hormones

Androgens produced by stimulating mouse testis with gonadotropic hormones cause a rise in renal ß-glucuronidase but not an increase in acid or alkaline phosphatase. All subcellular components increase in ß-glucuronidase activity, with a relatively greater increment in particulate enzyme as compared with that free in the cytoplasm (non-sedimentable). A small percentage of recovered ß-glucuronidase, acid phosphatase, and alkaline phosphatase is found in material which rises to the surface during centrifugation in sucrose media (fraction I). The specific activity of ß-glucuronidase and acid phosphatase in this fraction is normally quite high with respect to the homogenate, while that of alkaline phosphatase is not. On the other hand, the fraction I material from androgen-stimulated mice exhibits a further increase in specific activity with respect to ß-glucuronidase and not acid phosphatase. It thus appears that there is an independence in the behavior of individual enzymes in response to physiologic stimuli in spite of obvious morphologic proximity.

Acid phosphatase in Gaucher's disease.

1980 ◽  
Vol 26 (3) ◽  
pp. 371-382
Author(s):  
D B Robinson ◽  
R H Glew
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Purification And Characterization ◽  
Gaucher's Disease ◽  
Gaucher’S Disease ◽  
Intracellular Location ◽  
Increased Activity ◽  
Serum Acid Phosphatase

Abstract Increased acid phosphatase activity in the serum and tissues of patients with Gaucher's disease has now been recognized for two decades, but as yet no relation has been established between the enzyme and the etiology and progress of the disease. Here, we review results obtained by various investigators, ranging from a consideration of the methods used for the evaluation of serum acid phosphatase in Gaucher's disease to the most recent findings regarding the purification and characterization of two acid phosphatase isoenzymes from the spleen from patients with Gaucher's disease. We also discuss the intracellular location of tissue acid phosphatase in patients with Gaucher's disease and its contribution to the increased activity in serum.

Pituitary adrenal interactions in shorn sheep exposed to cold, wet conditions

1969 ◽  
Vol 20 (1) ◽  
pp. 99 ◽  
Author(s):  
BA Panaretto ◽  
KA Ferguson
Keyword(s):  
Acid Phosphatase ◽  
Enzymatic Activity ◽  
Phosphatase Activity ◽  
Cold Exposure ◽  
Acid Phosphatase Activity ◽  
Adrenal Glands ◽  
Adrenocortical Insufficiency ◽  
Acth Stimulation ◽  
Glucuronidase Activity ◽  
Exposure Levels

Newly shorn sheep were exposed to a cold (3°C) wet environment for 8 days; six out of 10 untreated animals died but there were no deaths in a group of 10 that was treated with cortisone. In two other experiments, nine out of 15 control sheep died, but only four out of 15 sheep treated with adrenocorticotrophin (ACTH). In a final experiment approximately one-third of exposed controls died compared with one-tenth of sheep treated with dexamethasone trimethylacetate. A significantly greater proportion (P < 0.05) of sheep given ACTH or 1.5 mg or more of dexamethasone trimethylacetate per kg had rectal temperatures higher than 37.8°C during the first 96 hr of exposure than the comparable controls. The adrenal glands of sheep that died in the cortisone and ACTH experiments were heavier than those taken from survivors that were killed after the experiment; macroscopically, the cortices of some of the adrenals from sheep that succumbed were haemorrhagic and resembled the glands seen in the Waterhouse-Friderichsen syndrome in man; all were heavily infiltrated with lipid when compared with the cortices of survivors. ß-Glucuronidase activity in the serum of cortisone-treated sheep (and in untreated survivors) was elevated during the first 2–3 days of exposure and returned to pre-exposure levels; untreated sheep that succumbed showed continuously increasing enzymatic activity. Acid phosphatase activity was initially depressed in steroid-treated sheep and returned to pre-exposure levels, whereas activity increased continuously in controls that died. Total leucocytes were lower during the first 72 hr of exposure in sheep treated with 1.5–2 mg dexamethasone trimethylacetate per kg, compared with untreated controls. We suggest that the enlarged, fat-laden haemorrhagic adrenals found in sheep that died from cold exposure resulted from excessive ACTH stimulation prior to death. The results suggested a state of adrenocortical insufficiency during the first 96 hr of cold exposure.

scholarly journals Vitamin E and stress

1967 ◽  
Vol 21 (1) ◽  
pp. 103-114 ◽  
Author(s):  
A. T. Diplock ◽  
J. Bunyan ◽  
D. Mchale ◽  
J. Green
Keyword(s):  
Amino Acids ◽  
Vitamin E ◽  
Muscular Dystrophy ◽  
Selenium Deficiency ◽  
Mean Value ◽  
Exudative Diathesis ◽  
High Incidence ◽  
Sulphur Amino Acids ◽  
Deficiency Diseases

1. The metabolism of small amounts of [5-Me-14C]D-α-tocopherol and [5-Me-3H]D-α- tocopherol has been studied in the vitamin E-deficient chick. Small doses of the labelled tocopherol were given to chicks, which were then subjected to stress by giving them diets formulated to produce encephalomalacia, exudative diathesis or muscular dystrophy.2. Tocopherol concentrations in the cerebella and brains of chicks with incipient encephalomacia were the same as those in normal chicks in which the dietary fat stress was absent.3. α-Tocopherol delayed the onset of encephalomalacia by a mean value of 3.5 days when its concentration in the cerebellum was about 2 × 10−7g/g of lipid. This concentration is considerably below the usual effective concentrations of antioxidants in vitro.4. Selenium deficiency, under conditions leading to a high incidence of exudative diathesis, was not associated with lowered tocopherol levels and did not result in detectable destruction of tocopherol.5. Nor was there any destruction of tocopherol or significant effect on its metabolism in the processes leading to muscular dystrophy: on the contrary, the affected muscles of dystrophic chicks, which had received a diet deficient in sulphur amino acids, contained significantly more tocopherol than muscles from control birds.6. These results do not support the hypothesis that lipid peroxidation is a causative process in the aetiology of vitamin E-deficiency diseases in the chick. The relationships between unsaturated lipid, Se, sulphur amino acids and tocopherol in the chick require further exploration.

Studies on gut ultrastructure and digestive physiology in Cyathostoma lari (Nematoda: Strongylida)

Parasitology ◽  
1971 ◽  
Vol 62 (2) ◽  
pp. 273-283 ◽  
Author(s):  
J. Barry Colam
Keyword(s):  
Acid Phosphatase ◽  
United States Public Health ◽  
Buccal Capsule ◽  
The United States ◽  
Digestive Physiology ◽  
Lysosomal Hydrolases ◽  
Prosthetic Group ◽  
Distal Surface ◽  
Group A ◽  
Contact Digestion

Histological, histochemical and ultrastructural methods have been used to study the gut structure and digestive physiology in the parasitic nematode Cyathostomalari E. Banchard, 1849. The nematode is parasitic in the orbito-nasal sinuses of its host and feeds exclusively upon blood.Three gland cells are present in the oesophagus, one in each sector. The two subventral gland ducts open into the lumen of the oesophagus at the level of the nerve ring, and the dorsal gland duct into the base of the buccal capsule. It is suggested that the latter gland may produce an anticoagulin, histolytic and/or haemolytic secretions, histochemically-inactive in situ. The intestine is syncytial, with no differentiation into secretory components, and its distal surface is provided with a prominent brush border of long microvilli.A non-specific esterase, thought to originate in the oesophageal gland secretions, causes haemolysis of ingested erythrocytes. The major part of haemoglobin digestion is extracellular, partly by a process of contact digestion on the microvilli, initiated by the esterase, and the protein is then further broken down by an exopeptidase of the ‘leucine aminopeptidase’ type, and the products absorbed into the gastrodermis possibly with the aid of an acid phosphatase present on or in the microvilli. An insoluble iron-containing compound, which is not haematin, results from breakdown of the prosthetic group. A smaller proportion of haemoglobin is taken up by the gastrodermis and digested intracellularly by the action of lysosomal hydrolases. An endopeptidase and an acid phosphatase are present in the gastrodermis, possibly in sacs of GER which are suggested to be primary lysosomes and which fuse with the endocytosed heterophagosomes. The insoluble pigment haematin results from digestion within the heterolysosomes, and this gives rise to the iron-containing gastrodermal pigment granules. The products of extracellular digestion are absorbed by the gastrodermis where they are synthetized into lipid by a lipase, which probably resides in whorls of GER.This investigation was supported in part by Research Grant AI 06295 of the United States Public Health Service. The final manuscript was prepared during the tenure of a Postdoctoral Fellowship from the British Egg Marketing Board. I wish to extend my gratitude to Dr J. B. Jennings for advice and encouragement throughout this work.

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