acid-phosphatase and Carcinoma--Ehrlich-Tumor

Hyperthermia produces marked effects on many biochemical parameters of tumor cells and has been reported to potentiate the effect of many drugs. We therefore evaluated the possible synergistic effect between hyperthermia and cisplatin against solid Ehrlich carcinoma. The study was based on the measurement of some biologic characteristics in tumor tissues, namely: DNA, RNA, and protein content and their rate of synthesis as parameters for nuclear damage; total lipids and cholesterol as parameters for membrane damage; acid-phosphatase and acid-ribonuclease as parameters for lysosomal damage; and tumor volume as a direct parameter for tumor growth.. Treatment of solid Ehrlich carcinoma by hyperthermia at 43 degrees C for 30 min for 3 successive days produced a 41.5% decrease in tumor volume, as well as a significant decrease in nucleic acids, protein contents and their rate of synthesis, in total lipids and cholesterol, and in acid-phosphatase and acid-ribonuclease. Chemotherapeutic management of the tumor by 5 mg/kg x 3 of cisplatin alone showed a continuous increase in tumor volume but at a lower rate than that of the untreated control. However, when cisplatin was given 1 h prior to hyperthermia, the tumor volume was significantly decreased by 82.6%.. The effects observed on all the investigated parameter were intensified when cisplatin was combined with hyperthermia. The results obtained suggest that hyperthermia may enhance the penetration of cisplatin to its target site inside the tumor cells due to a membrane-damaging effect. The enhanced lethality of cisplatin on tumor cells may also be due to the inhibition of DNA repair processes by hyperthermia.

Topics: Acid Phosphatase; Animals; Carcinoma, Ehrlich Tumor; Cisplatin; Combined Modality Therapy; DNA, Neoplasm; Female; Hyperthermia, Induced; Lipids; Mice; Neoplasm Proteins; RNA, Neoplasm

The effect of energy deprivation on autophagocytosis in Ehrlich ascites tumor cells was studied using cytochemical techniques. Autophagocytosis was induced with vinblastine incubation (0.1 mM) and the cellular ATP-level was lowered with 2-deoxy-D-glucose (0.35 mM). Acid phosphatase was used as a marker for lysosomal enzymes and imidazole-buffered osmium tetroxide impregnation in order to study the effects of energy deprivation on the maturation of autophagic vacuole (AV) membranes. Control and vinblastine treated cells maintained their ATP-levels throughout the incubation period tested (120 min). 2-Deoxy-D-glucose alone and with vinblastine decreased the intracellular ATP-level significantly after only 3 min incubation. Most of the AV's in control and vinblastine treated cells contained degraded material and acid phosphatase activity. Their membranes were stained only slightly or not at all with imidazole-buffered osmium tetroxide. 2-Deoxy-D-glucose alone as well as with vinblastine induced in particular an accumulation of early stages of AV's. These vacuoles contained undegraded cytoplasmic material and no acid phosphatase activity and their membranes were stained usually partly with imidazole-buffered osmium tetroxide. The membranes of some early AV's resembled endoplasmic reticulum and still had attached ribosomes. It was concluded that the inhibition of cellular energy production used in the present study did not inhibit autophagic sequestration but retarded the maturation of AV membranes and impaired the functioning of lysosomal hydrolases.

Topics: Acid Phosphatase; Adenosine Triphosphate; Animals; Autophagy; Carcinoma, Ehrlich Tumor; Deoxy Sugars; Deoxyglucose; Mice; Microscopy, Electron; Phagocytosis

The effect of systemic immunologic stimulation on renal expression of the H-2K (class I) and Ia (class II) antigens of the mouse major histocompatibility complex was explored. We previously reported that graft-vs-host (GvH) disease in mice caused an increase in host renal Ia expression. In the present experiments, we demonstrated that Kk antigen expression also increased during GvH. Other immune stimuli (allogeneic tumor grafts or injections of allogeneic spleen cells) caused increased renal Ia (and, where studied, Kk) expression in the epithelium of some renal tubules, as demonstrated by indirect immunofluorescence (IIF) or immunoperoxidase (IIP) staining. The normal interstitial Ia staining was frequently diminished in the kidneys of mice given these stimuli. At least in the case of allogeneic tumor grafts, the changes in renal Ia and H-2K were dependent on host T cells, in that no similar change appeared in nude (nu/nu) mice bearing allogeneic tumor grafts. By histochemical techniques, most of the change was in proximal tubules. In semiquantitative absorption, the total renal Ia was usually increased (two- to 20-fold) in parallel with the IIF or IIP changes. Serial studies revealed that MHC product induction was frequently transient and was not associated with detectable histologic abnormalities. In cultured renal cells, increased Iak and Kk could be demonstrated by IIF after 4 days of culture in supernatants of lymphocytes stimulated with concanavalin A: the activity in these supernatants was probably not interleukin 2, but might have been IFN-gamma, because IFN-gamma also induced this change. We conclude that systemic immunologic stimuli alter MHC product expression in renal tubule epithelium and that this effect can be stimulated in vitro by supernatants of stimulated lymphocytes.

Topics: Acid Phosphatase; Animals; Carcinoma, Ehrlich Tumor; Cells, Cultured; Female; Fluorescent Antibody Technique; Graft vs Host Disease; H-2 Antigens; Histocompatibility Antigens Class II; Immunization; Immunoenzyme Techniques; Kidney; Lymphocyte Transfusion; Mice; Mice, Inbred A; Mice, Inbred BALB C; Mice, Inbred C3H; Mice, Inbred C57BL; Mice, Inbred DBA; Mice, Nude; Neoplasm Transplantation

The results of a study on the effect of neodymium pulsed laser radiation on Ehrlich ascites tumor lysosomes are discussed. Tumor cell suspension was exposed in vitro to 10 pulses of laser irradiation with fluences of 10, 25 and 100 J/cm2, at a wavelength of 1.06 microns and a pulse duration of 1 microsecond. A rise in the free and total activities of acid phosphatase in the fraction of isolated lysosomes was registered one or four hours after exposure, particularly, at fluences of 10 and 25 J/cm2. However, laser radiation did not affect acid phosphatase activity in preparations of solubilized enzyme. Special experiments involving the use of detergents showed the increased activity of acid phosphatase in isolated lysosome fraction to be due to labilization of cytoplasmic membranes of tumor cells.

Topics: Acid Phosphatase; Animals; Carcinoma, Ehrlich Tumor; Cell Membrane; Female; Free Radicals; In Vitro Techniques; Laser Therapy; Lysosomes; Mice; Mice, Inbred Strains

In this work we report on the isolation of two plasma membrane fractions of a glycogen-free substrain of Ehrlich-Lettré ascites cells, a light fraction sedimenting in a sucrose gradient at 1.10 g/ml, and a heavy fraction sedimenting at nuclei by a combination of short-term swelling and mild Dounce homogenization. A 12 000 X g postnuclear pellet (PII) containing major portions of the plasma membrane marker enymes, 5'-nucleotidase, ouabain-sensitive (Na+ + K+)-ATPase and the alkaline phosphatase, was prepared by differential centrifugation. The two plasma membrane fractions were obtained by centrifugation on a discontinuous sucrose gradient, from which they were further purified on a linear sucrose gradient applying sedimentation velocity conditions only. Enrichment factors for the three marker enzymes were between 5- and 14-fold for the light fraction and between 3- and 7-fold for the heavy fraction with an overall yield of 1--4% and 0.5--1.7%, respectively, of cellular protein. Contamination of both fractions with nuclear material was minor. Mitochondrial contamination was about 8% for the light material and somewhat higher for the heavy material. In the light fraction, co-sedimentation of lysosomal and Golgi marker enzymes was detected. The presence of membrane structures of these organelles could not be confirmed definitely by electron microscopy. Differences in sialic acid content and phospholipid composition within the two fractions, especially in the relative proportion of lecithin to sphingomyelin, suggests differences in membrane fluidity. The light material showed mostly unit membrane vesicles in thin-section and freeze-etch electron microscopy, whereas the heavy fraction mainly consisted of sheet-like membrane fragments.

Topics: 5'-Nucleotidase; Acid Phosphatase; Alkaline Phosphatase; Animals; Carcinoma, Ehrlich Tumor; Cell Fractionation; Cell Membrane; Freeze Etching; Glycogen; Male; Mice; Microscopy, Electron; Nucleotidases; Phospholipids; Sodium-Potassium-Exchanging ATPase

An increase in the number of hepatocellular lysosomes was not detected in mice bearing the solid or ascites forms of Sarcoma 180 or Ehrlich's tumour. Despite this, biochemical studies showed significant increases in acid phosphatase, cathepsin-D and beta-galactosidase. This difference between morphological and biochemical observations is explained by the fact that only gross increases in lysosome population are likely to be detected in the small samples examined with the electron microscope, but by biochemical methods whereby many grams of tissue are analysed finer changes may be detected. As far as is known at present there is an increase in hepatocellular lysosomes and/or lysosomal enzymes in tumour-bearing mice, rats and man and no exception to this exists.

Topics: Acid Phosphatase; Animals; beta-Galactosidase; Carcinoma, Ehrlich Tumor; Cathepsins; Liver; Lysosomes; Mice; Proteins; Sarcoma 180

The effect of chemotherapy combined with immunostimulants on the activities of macrophages in mice was studied. The number of macrophages and exudate cells in the peritoneal cavity increased 3 days after ip injection with mitomycin-C, cyclophosphamide, and 5-fluorouracil together with OK-432 or yeast cell wall and decreased to normal level after 9 days, while the number of the cells remained decreased in mice receiving multi-drugs alone. Acid phosphatase activity of the macrophages of mice was elevated after the simultaneous injection of yeast cell wall and OK-432, and high activity was preserved in the macrophages of mice receiving yeast cell wall even after 9 days. Spreading of these cells was also enhanced. Macrophage activities examined by these assays were maximal in every respect 6 days after combination therapy. Cytostatic activity of the cells was strengthened after 6 days by combined use of OK-432 or yeast cell wall. Role of the activated macrophages in combination therapy was discussed.

Topics: Acid Phosphatase; Animals; Ascitic Fluid; Biological Products; Carcinoma, Ehrlich Tumor; Cell Wall; Female; Immunotherapy; Macrophages; Male; Mice; Mitomycins; Picibanil; Yeasts

Topics: Acid Phosphatase; Animals; Blood; Carcinoma, Ehrlich Tumor; Cell Division; Culture Media; Ferritins; Pinocytosis; Vacuoles

Topics: Acid Phosphatase; Animals; Antineoplastic Agents; Carcinoma, Ehrlich Tumor; Deoxyribonucleases; Female; Lysosomes; Male; Mice

The influence of estrogen, progesterone and testosterone on the activities of alkaline and acid phosphatases, adenosine triphosphatase and succinate dehydrogenase were determined by cytochemical methods in sarcoma 180 and Ehrlich's carcinoma cells transplanted in male and female Swiss mice. The results revealed differential effects of the sex hormones on different enzymes which seemed to depend on the type of tumour cell studied and the sex of the host mice.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Carcinoma, Ehrlich Tumor; Depression, Chemical; Estradiol Congeners; Female; Male; Mice; Neoplasm Transplantation; Progesterone; Sarcoma, Experimental; Sex Factors; Stimulation, Chemical; Succinate Dehydrogenase; Testosterone

The influence of estrogen, progesterone and testosterone on the activities of alkaline and acid phosphatases, adenosine triphosphatase and succinate dehydrogenase were determined by cytochemical methods in sarcoma 180 and Ehrlich's carcinoma cells transplanted in male and female Swiss mice. The results revealed differential effects of the sex hormones on different enzymes which seemed to depend on the type of tumour cell studied and the sex of the host mice.. Cells of sarcoma 180 and of Ehrlich's carcinoma were maintained by serial transplantation in male and female Swiss mice. Either estrogen, progesterone, or testosterone were injected im at doses of 1 mg/mouse. Ascitic fluid was aspirated at intervals of 1, 3, 6, 24, and 48 hours following hormone injections. Enzyme activities were analyzed by subjective grading according to the intensity of staining reaction. Estrogen produced enhancement of alkaline phosphatase activity in both types of cells in both sexes of mice. Progesterone produced increased alkaline phosphatase activity in both types of cells from female hosts but an inhibitory effect in male hosts' cells. Testosterone produced no change in enzyme activity in tumor cells of female hosts but in male hosts it inhibited enzyme activity of sarcoma 180 cells and activated activity in carcinoma cells. The effect of all 3 hormones on acid phosphatase activity was activation. With adenosine triphosphatase, estrogen stimulated the activity in both types of tumor in both sexes. Progesterone stimulated cells from male hosts with little or no effect on cells from female hosts. This enzyme was resistant to testosterone. Succinate dehydrogenase activity under similar conditions was different. Estrogen reduced this activity and progesterone produced some inhibition of activity. Testosterone inhibited the sarcoma cells but had no effect on carcinoma cells of either sex. Others have shown that sex hormones affect the enzyme activities beyond the target tissues, particularly in the liver, kidney, and pancreas. Different responses of the enzymes seemed to depend on the endogenous hormonal status of the mice.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Carcinoma, Ehrlich Tumor; Estrogens; Female; Injections, Intramuscular; Male; Mice; Neoplasm Transplantation; Progesterone; Sarcoma 180; Sex Factors; Succinate Dehydrogenase; Testosterone

For the purpose of predicting the effect of carcinostatic agents on tumor-bearing host in vitro, a sensitivity test of a drug in tumor bearers was developed. This test is based on the change in the specific activity of acid phosphatase of individual tumor and liver tissue, and the difference in them was used as an indicator of effectiveness. The value was called the "effective value." The present papar is concerned with the relationship between the effective value and effectiveness of the agents in rodents and man. The results showed that the effective value became higher with increasing concentration of Mitomycin-C incubated with tumor and liver tissues. The survival time of Ehrlich carcinoma-bearing mice, which were given Mitomycin-C intraperitoneally, was longer and increase in the dose of Mitomycin-C. In ascitic or subcutaneous form of Ehrlich carcinoma, AH-130, and Yoshida sarcoma, the effective value was parallel with the survival time of or the inhibition of tumor growth in tumor-bearing animals treated with Mitomycin-C. In 25 patients with gastric carcinoma treated with Mitomycin-C, the postoperative survival time was more closely correlated with the effective value calculated by the titers of both tumor and liver than the value of tumor alone.

Topics: Acid Phosphatase; Adult; Aged; Animals; Carcinoma, Ehrlich Tumor; Drug Evaluation; Female; Humans; Liver; Male; Mice; Middle Aged; Mitomycins; Neoplasms, Experimental; Phagocytosis; Rats; Sarcoma, Yoshida; Species Specificity; Stomach Neoplasms

The distribution of acid phosphatase in Ehrlich ascites carcinoma cells was studied by histochemical techniques in mice treated with antitumoral agents (Tio-Tepa, Cosmegen). The results proved the accuracy of the histoenzymatic demonstration of APh activity for the study of early changes induced in Ehrlich ascites tumor by antitumoral drugs : these changes precede those revealed by routine histological methods and are related to the degree of sensitivity of the tumor to the drugs.

Topics: Acid Phosphatase; Animals; Carcinoma, Ehrlich Tumor; Cells, Cultured; Dactinomycin; In Vitro Techniques; Lysosomes; Mice; Thiotepa

Topics: Acid Phosphatase; Amino Acids; Animals; Carbon Radioisotopes; Carcinoma, Ehrlich Tumor; Cell Adhesion; Cell Aggregation; Cell Division; Cell Line; Culture Techniques; Cycloheximide; Edetic Acid; Glass; Hyaluronoglucosaminidase; Neuraminidase; Ribonucleases; Time Factors; Trypsin

Topics: Acid Phosphatase; Animals; Antineoplastic Agents; Carcinoma, Ehrlich Tumor; Chromatography, DEAE-Cellulose; Deoxyribonucleases; Fluorouracil; Lysosomes; Mice; Neoplasm Transplantation; Nitrosourea Compounds; Thiotepa; Triazines; Vinblastine

Topics: Acid Phosphatase; Animals; Antineoplastic Agents; Carcinoma, Ehrlich Tumor; Histones; Lysosomes; Mice; Stimulation, Chemical

Topics: Acid Phosphatase; Animals; Carcinoma, Ehrlich Tumor; Cells, Cultured

Topics: Acid Phosphatase; Acridines; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Carcinoma, Ehrlich Tumor; Depression, Chemical; Female; Male; Mice; Neoplasm Transplantation; Sarcoma 180; Sex Factors; Succinate Dehydrogenase; Transplantation, Homologous

Topics: Acid Phosphatase; Animals; Carcinoma, Ehrlich Tumor; Lectins; Lymphocyte Activation; Lymphocytes; Macrophages; Male; Mice; Neoplasm Transplantation; Sarcoma 180; Time Factors; Transplantation Immunology

Topics: Acid Phosphatase; Animals; Carcinoma, Ehrlich Tumor; Cell Adhesion; Histocytochemistry; Lysosomes; Macrophages; Male; Mice; Microscopy, Electron; Phagocytosis; Radiation Effects; Time Factors

Topics: Acid Phosphatase; Alanine Transaminase; Animals; Aspartate Aminotransferases; Carcinoma, Ehrlich Tumor; gamma-Globulins; L-Lactate Dehydrogenase; Liver; Mice; Radiation Injuries, Experimental

Topics: Acid Phosphatase; Animals; Carbon Isotopes; Carcinoma, Ehrlich Tumor; Cells; Dactinomycin; Guanine; Hydrogen-Ion Concentration; Kinetics; Leucine; Mice; Neoplasm Proteins; Phosphoric Diester Hydrolases; Phosphoric Monoester Hydrolases; Ribonucleases; RNA, Neoplasm

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Carcinoma, Ehrlich Tumor; Chemical Phenomena; Chemistry; Hydrolysis; In Vitro Techniques; Injections, Intraperitoneal; Melanoma; Mice; Mice, Inbred Strains; Phosphates; Phosphorus Isotopes; Radionuclide Imaging; Tissue Extracts

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Bone Neoplasms; Carcinoma, Ehrlich Tumor; Esterases; Female; Glucuronidase; Histocytochemistry; Male; Mice; Neoplasm Transplantation; Oxidoreductases

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Carcinoma, Ehrlich Tumor; Carcinoma, Hepatocellular; Liver Neoplasms; Mice; Neoplasms, Experimental; Radiation Effects; Rats

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Calcium; Carcinoma, Ehrlich Tumor; Hydrolysis; Kidney; Liver; Lymphoma, Non-Hodgkin; Magnesium; Melanoma; Mice; Neoplasms, Experimental; Phosphates; Phosphoric Monoester Hydrolases; Polymers; Pyrophosphatases

Topics: Acid Phosphatase; Animals; Carcinoma, Ehrlich Tumor; Enzyme Activation; Histocytochemistry; Lysosomes; Mice; Microscopy, Electron; Necrosis

Topics: Acid Phosphatase; Animals; Brain; Brain Chemistry; Brain Neoplasms; Carcinoma, Ehrlich Tumor; Glucuronidase; Histocytochemistry; Hyaluronoglucosaminidase; L-Lactate Dehydrogenase; Mice; Microscopy, Electron; Neoplasm Transplantation; Nucleosides; Oxidoreductases; Phosphotransferases; Thymidine; Transferases; Uracil; Uridine; Xanthine Oxidase

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Carcinoma, Ehrlich Tumor; Cattle; Glucose; Glucose-6-Phosphatase; Hexokinase; Isomerases; Kidney; Kinetics; Liver; Rats; Saccharomyces

Topics: Acid Phosphatase; Animals; Carcinoma, Ehrlich Tumor; Cell Nucleus; Centrifugation; Lysosomes; Microsomes; N-Glycosyl Hydrolases; NAD; NADP; Niacinamide; Nucleotidyltransferases; Oxidoreductases

Topics: Acid Phosphatase; Adenocarcinoma; Animals; Carcinoma, Ehrlich Tumor; Mice; Mononuclear Phagocyte System; Neoplasm Transplantation; Neoplasms, Experimental; Phagocytosis; Polysaccharides; Sarcoma 180

Topics: Acid Phosphatase; Adenine Nucleotides; Adenosine Triphosphatases; Adenosine Triphosphate; Animals; Carcinoma, Ehrlich Tumor; Glucosyltransferases; Lysosomes; Mice; N-Glycosyl Hydrolases; Nucleotidyltransferases; Ribonucleases; Triaziquone

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Antibodies; Carcinoma, Ehrlich Tumor; Complement System Proteins; Cytoplasm; Esterases; Immune Sera; Leucyl Aminopeptidase; Lysosomes; Mast Cells; Mice; Phospholipids; Rats; Serum Globulins

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Arginase; Carbon Isotopes; Carboxy-Lyases; Carcinoma, Ehrlich Tumor; Dactinomycin; Folic Acid; Glycerolphosphate Dehydrogenase; Histones; In Vitro Techniques; L-Lactate Dehydrogenase; Leucine; Neoplasm Proteins; Protamines; Rats; Ribonucleases; RNA, Neoplasm; Tritium; Uridine

Topics: Acid Phosphatase; Adenosine Triphosphate; Alkaline Phosphatase; Alkylating Agents; Animals; Antineoplastic Agents; Ascites; Benzoquinones; Biochemical Phenomena; Biochemistry; Carbohydrate Metabolism; Carcinoma, Ehrlich Tumor; Cholinesterases; Hexokinase; Metabolism; Mice; NAD; Pharmacology; Quinones; Research

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Antineoplastic Agents; Busulfan; Carbohydrate Metabolism; Carcinoma; Carcinoma, Ehrlich Tumor; Metabolism; Neoplasms; Pharmacology; Research; Sarcoma; Sarcoma, Yoshida; Toxicology

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Carcinoma; Carcinoma, Ehrlich Tumor; Glucose-6-Phosphatase; Liver; Neoplasm Transplantation; Neoplasms, Experimental; Phosphoric Monoester Hydrolases; Research; Rodentia; Sarcoma; Sarcoma, Experimental; Skin