Effect of ovarian hormones on lysosomal acid hydrolase activities in rat myometrium.

1977 ◽  
Vol 232 (4) ◽  
pp. E423
Author(s):  
B F Sloane ◽  
J W Bird
Keyword(s):  
Acid Phosphatase ◽  
Cathepsin D ◽  
Hormone Replacement ◽  
Membrane Integrity ◽  
Lysosomal Membrane ◽  
Acid Hydrolase ◽  
Acid Hydrolases ◽  
Lysosomal Acid ◽  
Hypophysectomized Rats ◽  
Estrus Stage

The activities of the lysosomal acid hydrolases-cathespin D, acid phosphatase, beta-N-acetylglucosaminidase, and beta-glucuronidase-were measured in rat myometrium under the following hormonal conditions: during the estrus stage of the estrous cycle (NE); at 1,2, and 3 wk after ovariectomy; and in 3-wk postovariectomized females after hormone replacement therapy with 17 beta-estradiol (E2), progesterone (P), or E2 + P. Activities per milligram protein and per milligram DNA of the enzymes were significantly decreased after ovariectomy and were restored to the NE level or above after injecting E2 or E2 + P. Lysosomal enzyme activities did not change with hormonal state in hypophysectomized rats, suggesting that other hormones are required for mediation of enzyme activity. Acid hydrolase activities in other tissues and nonlysosomal enzyme activites in the myometrium did not fluctuate with hormonal state. Studies of lysosomal membrane integrity suggested that one population of lysosomes richer in cathepsin D and acid phosphatase and another rich in beta-N-acetylglucosaminidase and beta-glucuronidase may be present in rat myometrium. Estrogen seemed to labilize the lysosomal membrane of at least the latter of the two proposed populations of myometrial lysosomes.

scholarly journals Inhibition by oestrogen of collagen breakdown in the involuting rat uterus

1969 ◽  
Vol 112 (5) ◽  
pp. 637-645 ◽  
Author(s):  
J. F. Woessner
Keyword(s):  
Acid Phosphatase ◽  
Cathepsin D ◽  
Post Partum ◽  
Acid Hydrolase ◽  
Acid Hydrolases ◽  
Rat Uterus ◽  
Oestrogen Treatment ◽  
Period 2 ◽  
Normal Rat ◽  
Wet Weight

1. Both the post-partum involution of the rat uterus and the rapid breakdown of collagen that accompanies it are extensively inhibited by oestrogenic hormones. In the normal rat, 85% of the uterine collagen is degraded within 4 days after parturition; in rats treated with 100μg. of 17β-oestradiol/day, only 35% of uterine collagen is broken down in the same period. 2. Similar effects are produced by diethylstilboestrol if the dose is increased tenfold. 3. Collagen breakdown is inhibited to a greater extent than is the loss of wet weight by oestradiol but not by diethylstilboestrol. 4. The oestrogens appear to act by blocking the breakdown of collagen. There is a greatly decreased concentration of free hydroxyproline in the uterus of treated animals. 5. Acid hydrolase concentrations (β-glucuronidase, β-galactosidase, cathepsin D and acid phosphatase) in the uterus are decreased by oestrogen treatment compared with controls, but the total amounts of these enzymes in the uterus are somewhat elevated. Oestrogens do not appear to inhibit collagen breakdown by altering the concentration and total amount of acid hydrolases.

The Properties and Subcellular Localization of Acid Phosphatases in the Colourless Alga, Polytomella Caeca

1974 ◽  
Vol 15 (3) ◽  
pp. 605-618
Author(s):  
ROSEMARY A. COOPER ◽  
I. D. BOWEN ◽  
D. LLOYD
Keyword(s):  
Acid Phosphatase ◽  
Subcellular Localization ◽  
Density Gradients ◽  
Acid Phosphatases ◽  
Acid Hydrolase ◽  
Acid Hydrolases ◽  
Distribution Profile ◽  
Golgi Bodies

The acid p-nitrophenyl phosphatase of homogenates of Polytomella caeca is a latent acid hydrolase, which is partially inhibited by NaF. Its distribution profile in density gradients (which is similar to that of naphthyl AS-TR phosphatase) suggests that this enzyme is partially lysosomal in location. Cytochemical evidence for the localization of acid phosphatases in fine subcellular structures is presented. Naphthyl AS-TR phosphatase is localized in vacuoles, points of focal degradation, Golgi bodies and dispersed throughout the cytosol. β-Glycerophosphatase is confined to large vacuoles and the cytosol. The nature of acid phosphatase-containing organelles in P. caeca is discussed in view of the inability to detect eleven other latent acid hydrolases in cell-free homogenates.

scholarly journals LYSOSOMAL PHYSIOLOGY IN TETRAHYMENA

1974 ◽  
Vol 62 (3) ◽  
pp. 844-859 ◽  
Author(s):  
Thomas L. Rothstein ◽  
J. J. Blum
Keyword(s):  
Acid Phosphatase ◽  
Cyclic Amp ◽  
Cytochalasin B ◽  
Adrenergic System ◽  
Acid Hydrolase ◽  
Dibutyryl Cyclic Amp ◽  
Acid Hydrolases ◽  
Extracellular Release ◽  
Particle Ingestion ◽  
Pharmacologic Agents

The ingestion of 14C-labeled 9,10-dimethyl-1,2-benzanthracene particles, the extracellular release of acid phosphatase, ribonuclease, and α-glucosidase, and the egestion of preingested dimethylbenzanthracene particles by Tetrahymena taken from logarithmically growing cultures and resuspended in a dilute salt solution were followed in the presence of several pharmacologic agents. Serotonin, caffeine, and, to a lesser extent, dibutyryl cyclic AMP increased the rate of particle ingestion, but did not alter the rate of release of the three acid hydrolases studied. Added catecholamines did not affect either particle ingestion or acid hydrolase release, but particle ingestion was inhibited by the catecholamine antagonists, dichloroisoproterenol, desmethylimipramine, reserpine, and phenoxybenzamine. These drugs also increased the release of acid phosphatase and ribonuclease in 5-h incubations. Desmethylimipramine acted within 1 h to increase acid hydrolase release, but the effect of dichloroisoproterenol developed more slowly and was secondary to a change in cellular content of the hydrolases. Desmethylimipramine increased the energy of activation for the release of acid phosphatase, while dichloroisoproterenol did not. Both of these drugs enhanced the egestion of preingested dimethylbenzanthracene particles, supporting the view that acid hydrolase release occurs through a cytoproct egestion mechanism. Particle ingestion was also inhibited by colchicine, vinblastine, and cytochalasin B, but these agents had no effect on acid hydrolase release, thus further differentiating the properties of the ingestion mechanism from those of the egestion mechanism. It appears that both microtubules and microfilaments play a role in the ingestion process and that this process may be controlled in part by a cyclic AMP-mediated serotoninergic and adrenergic system.

scholarly journals Hepatocyte Lysosomal Membrane Stabilization by Olive Leaves against Chemically Induced Hepatocellular Neoplasia in Rats

2011 ◽  
Vol 2011 ◽  
pp. 1-6 ◽  
Author(s):  
N. M. Abdel-Hamid ◽  
M. A. El-Moselhy ◽  
A. El-Baz
Keyword(s):  
Cathepsin D ◽  
Proteolytic Enzymes ◽  
Membrane Integrity ◽  
Lysosomal Membrane ◽  
Diagnostic Tools ◽  
Olive Leaf ◽  
Chemically Induced ◽  
New Strategy ◽  
A Prospective Study ◽  
Lysosomal Membrane Integrity

Extensive efforts are exerted looking for safe and effective chemotherapy for hepatocellular carcinoma (HCC). Specific and sensitive early biomarkers for HCC still in query. Present work to study proteolytic activity and lysosomal membrane integrity by hepatocarcinogen, trichloroacetic acid (TCA), in Wistar rats against aqueous olive leaf extract (AOLE).TCA showed neoplastic changes as oval- or irregular-shaped hepatocytes and transformed, vesiculated, and binucleated liver cells. The nuclei were pleomorphic and hyperchromatic. These changes were considerably reduced by AOLE. The results added, probably for the first time, that TCA-induced HCC through disruption of hepatocellular proteolytic enzymes as upregulation of papain, free cathepsin-D and nonsignificant destabilization of lysosomal membrane integrity, a prerequisite for cancer invasion and metastasis. AOLE introduced a promising therapeutic value in liver cancer, mostly through elevating lysosomal membrane integrity. The study substantiated four main points: (1) the usefulness of proteolysis and lysosomalmembrane integrity in early prediction of HCC. (2) TCA carcinogenesis is possibly mediated by lysosomal membrane destabilization, through cathepsin-D disruption, which could be reversed by AOLE administration. (3) A new strategy for management of HCC, using dietary olive leaf system may be a helpful phytotherapeutic trend. (4) A prospective study on serum proteolytic enzyme activity may introduce novel diagnostic tools.

scholarly journals Further observations on the activation of lysosomal acid α-glucosidase by cortisone derivatives

1973 ◽  
Vol 132 (3) ◽  
pp. 435-438 ◽  
Author(s):  
E. J. Bourne ◽  
K. Clarke ◽  
J. B. Pridham ◽  
J. J. M. Rowe
Keyword(s):  
Acid Phosphatase ◽  
Rat Liver ◽  
Lysosomal Membrane ◽  
Cortisone Acetate ◽  
Lysosomal Acid ◽  
Liver Slices ◽  
Liver Lysosomes ◽  
Membrane Bound ◽  
Isolated Liver

1. Cortisone acetate activates the acid α-glucosidase in rat liver slices and in isolated liver lysosomes. 2. The reaction is steroid specific and moreover does not occur with lysosomal acid phosphatase or β-galactosidase. 3. After pretreatment of the lysosomes with cortisone, substrate (maltose) binding to the soluble lysosomal acid α-glucosidase is not affected, but the steroid does increase the Vmax. value. Membrane-bound enzyme is not activated by cortisone. 4. 4-[14C]Cortisone is preferentially bound to the lysosomal membrane and the possible involvement of this structure in the activation phenomenon is discussed.

DIFFERING PATTERNS OF ACID PHOSPHATASE AND CATHEPSIN D ACTIVITIES IN THE RAT VENTRAL PROSTATE GLAND DURING CASTRATION-INDUCED PROSTATIC INVOLUTION

1972 ◽  
Vol 69 (4) ◽  
pp. 747-761 ◽  
Author(s):  
Heikki J. Helminen ◽  
Jan L. E. Ericsson ◽  
Bengt Arborgh
Keyword(s):  
Acid Phosphatase ◽  
Cathepsin D ◽  
De Novo ◽  
Prostate Gland ◽  
Cell Activity ◽  
Total Activity ◽  
Ventral Prostate ◽  
Acid Hydrolases ◽  
Rat Ventral Prostate ◽  
Specific Activities

ABSTRACT The activities of acid phosphatase and cathepsin D in the rat's ventral prostate lobe were investigated under normal conditions and during castration-induced involution. The specific activities of the acid hydrolases were higher in the prostatic »tissue« fraction than in the »secretion« fraction of the gland, and the total activities of acid phosphatase and cathepsin D in the »secretion« were increased up to about 24 % and 8 %, respectively, of the activities in the whole lobe. During involution, the specific activities of both hydrolases in the tissue showed a rapid increase, while total activity and activity »per cell« (on a DNA basis) of acid phosphatase declined, while the total activity of cathepsin D remained essentially unaltered at first and ultimately decreased; the activity of cathepsin D »per cell« was first increased and later showed a slight decrease. Cycloheximide administration retarded the gross atrophy and decrease in protein and DNA content, and was associated with a lowered total, specific and »per cell« activity of cathepsin D, and an »increased« total activity of acid phosphatase. The observations are compatible with an increased de novo synthesis of cathepsin D and a decreased synthesis of acid phosphatase during prostatic involution. The findings were interpreted as indicating that in the ventral prostate lobe of the rat, acid phosphatase is in part a secretory (and hormonesensitive) enzyme, and in part a »conventional« lysosomal enzyme, while cathepsin D is predominantly an enzyme which is bound to conventional lysosomes.

scholarly journals Requirement of the Human GARP Complex for Mannose 6-phosphate-receptor-dependent Sorting of Cathepsin D to Lysosomes

2008 ◽  
Vol 19 (6) ◽  
pp. 2350-2362 ◽  
Author(s):  
F. Javier Pérez-Victoria ◽  
Gonzalo A. Mardones ◽  
Juan S. Bonifacino
Keyword(s):  
Shiga Toxin ◽  
Cathepsin D ◽  
Culture Medium ◽  
Retrograde Transport ◽  
Acid Hydrolase ◽  
Acid Hydrolases ◽  
General Role ◽  
B Subunit ◽  
Mannose 6 Phosphate ◽  
Garp Complex

The biosynthetic sorting of acid hydrolases to lysosomes relies on transmembrane, mannose 6-phosphate receptors (MPRs) that cycle between the TGN and endosomes. Herein we report that maintenance of this cycling requires the function of the mammalian Golgi-associated retrograde protein (GARP) complex. Depletion of any of the three GARP subunits, Vps52, Vps53, or Vps54, by RNAi impairs sorting of the precursor of the acid hydrolase, cathepsin D, to lysosomes and leads to its secretion into the culture medium. As a consequence, lysosomes become swollen, likely due to a buildup of undegraded materials. Missorting of cathepsin D in GARP-depleted cells results from accumulation of recycling MPRs in a population of light, small vesicles downstream of endosomes. These vesicles might correspond to intermediates in retrograde transport from endosomes to the TGN. Depletion of GARP subunits also blocks the retrograde transport of the TGN protein, TGN46, and the B subunit of Shiga toxin. These observations indicate that the mammalian GARP complex plays a general role in the delivery of retrograde cargo into the TGN. We also report that a Vps54 mutant protein in the Wobbler mouse strain is active in retrograde transport, thus explaining the viability of these mutant mice.

scholarly journals LYSOSOMES IN SKELETAL MUSCLE TISSUE

1970 ◽  
Vol 45 (2) ◽  
pp. 321-333 ◽  
Author(s):  
Peter G. Canonico ◽  
John W. C. Bird
Keyword(s):  
Skeletal Muscle ◽  
Acid Phosphatase ◽  
Connective Tissue ◽  
Phosphatase Activity ◽  
Cathepsin D ◽  
Acid Phosphatase Activity ◽  
Equilibrium Density ◽  
Acid Hydrolases ◽  
Triton Wr 1339 ◽  
Arylsulfatase Activity

Postnuclear supernates from homogenates of skeletal muscle from rats subjected to starvation, injections of Triton WR-1339, dextran-500, and dextran + corticosterone were fractionated by means of rate and isopycnic zonal centrifugation in sucrose—0.02 M KCl gradients. Zonal fractions were analyzed for protein, RNA, cytochrome oxidase, and up to six acid hydrolases. The results indicate the presence of two groups of lysosome-like particles. One group contributes approximately 95% of the cathepsin D and acid phosphatase activity and 75% of the acid ribonuclease, ß-glucuronidase, and arylsulfatase activity in muscle. It is characterized by a modal equilibrium density of 1.18 that is decreased by starvation, but is not shifted by dextran-500 or Triton WR-1339. The second group has a higher proportion of acid ribonuclease, ß-glucuronidase, and arylsulftase; the equilibrium density can be shifted by dextran-500 and Triton WR-1339. It is suggested that this group of lysosomes is derived from macrophages and other connective tissue cells, whereas the former group represents lysosome-like particles from muscle cells.

scholarly journals THE INFLUENCE OF THE MODE OF NUTRITION ON THE DIGESTIVE SYSTEM OF OCHROMONAS MALHAMENSIS

1969 ◽  
Vol 43 (3) ◽  
pp. 396-409 ◽  
Author(s):  
H. J. Stoltze ◽  
N. S. T. Lui ◽  
O. R. Anderson ◽  
O. A. Roels
Keyword(s):  
Defined Medium ◽  
Complete Medium ◽  
Acid Hydrolase ◽  
Acid Hydrolases ◽  
Cytoplasmic Staining ◽  
Cytoplasmic Matrix ◽  
Lysosomal Acid ◽  
E Coli ◽  
Enzymic Reaction ◽  
In Cells

The intracellular distribution and level of acid hydrolases in Ochromonas malhamensis were studied in cells grown osmotrophically in a defined medium, in a carbon-free starvation medium, and during phagotrophy in each of these media. By cytochemical techniques, little enzymic reaction product was observed in the vacuoles of osmotrophic cells grown in the defined medium. Starved cells, however, contained autophagic vacuoles and cannibalized other Ochromonas cells. Dense enzymic reaction product was observed in the digestive vacuoles and in the Golgi cisternae of these starved cells. Moreover, starved cells and cells grown in a nutritionally complete medium ingested Escherichia coli which appeared in digestive vacuoles containing enzymic reaction product. Biochemical assays for lysosomal acid phosphatase (E.C. 3.1.3.2 orthophosphoric monoester phosphohydrolase) and acid ribonuclease (E.C. 2.7.7.16 ribonucleate nucleotido-2'-transferase) were done on Ochromonas cultures in the same experimental treatments and under identical assay conditions as the cytochemical study. During starvation, the acid hydrolase specific activities were consistently twice those found in cells grown in an osmotrophic complete medium. Ochromonas fed E. coli showed no increase in acid hydrolase specific activity as compared to controls not fed E. coli. The latency of lysosomal acid hydrolases in cells fixed with glutaraldehyde was reduced, suggesting that this fixative increases lysosomal membrane permeability and may release enzymes or their reaction products into the cytoplasmic matrix during cytochemical analysis. This could explain the cytoplasmic staining artifact sometimes observed with glutaraldehyde-fixed cells when studied by the Gomori technique. This study confirms that Ochromonas malhamensis, a phytoflagellate, does produce digestive vacuoles and can ingest bacteria, thereby fulfilling its role as a heterotroph in an aquatic food chain. When Ochromonas is grown in a nutritionally complete osmotrophic medium, phagocytosis causes appearance of acid hydrolases in the digestive vacuoles, whereas the total activity of the enzymes remains unchanged. An organic carbon-free medium strongly stimulates acid hydrolaes activity and causes these enzymes to appear in the digestive vacuoles whether phagocytosis occurs or not.

scholarly journals LYSOSOMAL ACID HYDROLASES IN MICE INFECTED WITH BCG

1965 ◽  
Vol 121 (5) ◽  
pp. 727-738 ◽  
Author(s):  
Kazuhisa Saito ◽  
Emanuel Suter
Keyword(s):  
Acid Phosphatase ◽  
Liver Homogenate ◽  
Subcellular Fractions ◽  
The Other ◽  
Acid Phosphatases ◽  
Acid Hydrolases ◽  
Lysosomal Acid

Experiments are reported dealing with the increase of lysosomal acid hydrolases induced by BCG infection. Acid hydrolases were determined quantitatively in peritoneal MP, liver homogenate, and plasma of normal and BCG-infected mice. A significant increase of acid phosphatase, ß-glucuronidase, and cathepsin was found in MP and liver homogenate of BCG-infected mice. In plasma also a significant increase of acid phosphatase and ß-glucuronidase was noticed. The results of the determination of the enzymes in centrifugally separated subcellular fractions of liver homogenate indicated clearly that the acid hydrolases associated mainly with the "large granular" fraction, which consists of mitochondria, lysosomes, and microsomes and that infection with BCG caused significant increase of the enzymes specifically in this fraction. Differences in the pattern of location among centrifugally separated fraction of liver homogenate were observed between acid phosphatase and the other two acid hydrolases. MP cultured in vitro doubled their acid phosphatases content within 24 hours, whereas ß-glucuronidase rather decreased in the same cells.

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