acid-phosphatase and Trichinellosis

Topics: Acid Phosphatase; Adenosine Triphosphate; Animals; Ascaris; Brucella abortus; Carbohydrate Metabolism; Carbon Isotopes; Cestoda; Coenzyme A; Disease Vectors; Esterases; Fatty Acids; Ions; Leucine; Leucyl Aminopeptidase; Lipids; Lysosomes; Methionine; Muscles; Oxygen Consumption; Parasites; Phosphorus Isotopes; Plasmodium; Plasmodium falciparum; RNA; Symbiosis; Thiamine; Trichinella; Trichinellosis; Trichomonas

The nurse cell in the cyst of Trichinella spiralis comprises at least two kinds of cytoplasm, derived from muscle or satellite cells, as indicated by the pattern of staining using regular dye (haematoxylin and eosin, or toluidine blue), alkaline phosphatase (ALP) expression, acid phosphatase (ACP) expression and immunostaining with an anti-intermediate filament protein (desmin or keratin). Muscle cells undergo basophilic changes following a T. spiralis infection and transform to the nurse cells, accompanied by an increase in ACP activity and the disappearance of desmin. Satellite cells are activated, transformed and joined to the nurse cells but remain eosinophilic. The eosinophilic cytoplasm is accompanied by an increase in desmin and ALP expression but not an increase in ACP activity. Differences in the staining results for ALP or ACP suggest that the two kinds of cytoplasm have different functions. Trichinella pseudospiralis infection results in an increase of ACP activity at a later stage than T. spiralis. There is also a difference in the location pattern of ACP in the cyst of T. spiralis compared with T. pseudospiralis. In T. spiralis, ACP is diffused within the cell, but in T. pseudospiralis, ACP distribution is spotty corresponding to the location of the nucleus. Trichinella pseudospiralis infection is accompanied by a slight increase in ALP activity. Activated satellite cells following a T. pseudospiralis infection exhibit an increase in desmin expression. The present study therefore reveals that nurse cell cytoplasm differs between the two Trichinella species and between the two origins of cytoplasm in the cyst of T. spiralis.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Coloring Agents; Host-Parasite Interactions; Life Cycle Stages; Mice; Mice, Inbred BALB C; Muscle, Skeletal; Species Specificity; Staining and Labeling; Trichinella; Trichinella spiralis; Trichinellosis

Infection by the parasitic nematode Trichinella spiralis induces cell cycle repositioning (chronic suspension in apparent G2/M) and genetic reprogramming in differentiated mammalian skeletal muscle cells. These changes occur in association with dramatic enlargement of infected host cell nuclei (as large as 17 microm in diameter) and nucleoli. Nuclear antigens (NA) that colocalize with host chromatin have been detected by antibodies to T. spiralis antigens, but the functions of these NA are unresolved. Mebendazole (MBZ) preferentially binds parasite versus host beta-tubulins, is implicated in inhibiting secretion in nematodes and induces cytoplasmic changes in muscle cells infected with T. spiralis. These infected cell changes might be indirect via MBZ inhibition of parasite secretions. This effect would have implications for host/parasite interactions and was evaluated here. MBZ treatment of chronically infected mice caused: (1) a significant deformation of host nuclei and diminution of nucleoli by 4 and 6 days of treatment (dot), respectively; (2) a reduction of nuclear lamins A/C in infected cell nuclei that was concomitant with nuclear deformation; and (3) significant reductions in total RNA, general protein and acid phosphatase activity levels. These changes were associated with the depletion of NA from host nuclei detected by 4 dot. However, DNA content of infected cell nuclei was not detectably reduced and muscle gene expression was not reactivated. The cellular changes documented are likely to account for previously described cytoplasmic alterations induced by MBZ. Concomitant depletion of NA from infected cell nuclei suggests a role of these products in regulating nuclear functions of host cells.

Topics: Acid Phosphatase; Animals; Antigens, Helminth; Antinematodal Agents; Cell Cycle; Cell Nucleolus; Cell Nucleus; DNA; Gene Expression Regulation; Host-Parasite Interactions; Lamins; Larva; Mebendazole; Mice; Mice, Inbred BALB C; Muscle, Skeletal; Nuclear Proteins; Proteins; RNA; Trichinella spiralis; Trichinellosis

An experimental subcutaneous inflammation was produced in guinea pigs with peripheral blood eosinophilia. The eosinophilia resulted from two subsequent infections with Trichinella spiralis larvae. One group of guinea pigs served as non-infected control. Inflammation was induced by carrageenan, bradykinin, histamine, platelet activating factor and eosinophilotactic factors of lymphocytic or neutrophilic origin. Whereas in the control group no eosinophil granulocytic response was observed, this response was seen in the group with peripheral blood eosinophilia. The inflammatory substances and mediators (carrageenan, bradykinin, histamine, platelet activating factor) did not attract eosinophils alone, but also neutrophils. Under peripheral blood eosinophilia within the time course of the inflammatory reaction a second emigration with a shifted neutrophil/eosinophil ratio in favour of eosinophils was found. This could be due to a generation of chemoattractants by the injected substances themselves or more probably, by already emigrated granulocytes. Neither histamine, bradykinin, carrageenan, nor the eosinophilotactic factors (ECF's) in the concentrations used did release the cytotoxic major basic protein from eosinophils. Platelet activating factor exhibited a release of major basic protein from some eosinophils but no release of the peroxidase under our experimental conditions. The immigration of sufficient numbers of eosinophils into inflammatory areas might be one cause of the reduction of the inflammatory edema found in a previous investigation under similar conditions.

Topics: Acid Phosphatase; Animals; Arylsulfatases; Blood Proteins; Bradykinin; Carrageenan; Cell Movement; Chemotactic Factors; Chemotactic Factors, Eosinophil; Disease Models, Animal; Eosinophil Granule Proteins; Eosinophilia; Eosinophils; Female; Guinea Pigs; Histamine; Inflammation; Isoenzymes; Male; Neutrophils; Peroxidase; Peroxidases; Platelet Activating Factor; Ribonucleases; Time Factors; Trichinellosis

Topics: Acid Phosphatase; Animals; Anticonvulsants; Esterases; Male; Mice; Muscles; Succinate Dehydrogenase; Triazoles; Trichinellosis

Topics: Acid Phosphatase; Animals; Antibody-Producing Cells; Autopsy; Female; Fluorescent Antibody Technique; Histocytochemistry; Immunity, Cellular; Immunoglobulins; Larva; Lymph Nodes; Macrophages; Mandible; Mesentery; Rats; Spleen; Time Factors; Trichinella; Trichinellosis

Topics: Acid Phosphatase; Adenosine Triphosphatases; Agglutination Tests; Alkaline Phosphatase; Aluminum Silicates; Animals; Antibodies; Antibody Formation; Antigens; Complement Fixation Tests; Erythrocytes; Esterases; Fluorescent Antibody Technique; Freund's Adjuvant; Glucosephosphate Dehydrogenase; Guinea Pigs; Histocytochemistry; Hypersensitivity, Delayed; Immune Adherence Reaction; Larva; Liver; Macrophages; Male; Muscles; Skin Tests; Spleen; Trichinella; Trichinellosis

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; BCG Vaccine; Esterases; Female; Glucose-6-Phosphatase; Histocytochemistry; Intestine, Small; Liver; Mice; Mice, Inbred Strains; Mononuclear Phagocyte System; Muscles; Spleen; Trichinellosis

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Antilymphocyte Serum; Histocytochemistry; Intestine, Small; Intestines; Mice; Rabbits; Trichinellosis

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Antilymphocyte Serum; Histocytochemistry; Lymphatic System; Mice; Plasma Cells; Trichinellosis

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Antilymphocyte Serum; Histocytochemistry; Mice; Muscles; Rabbits; Trichinellosis

Topics: Acetylcholinesterase; Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Anthelmintics; DNA; Glycogen; Histocytochemistry; Male; Mice; Muscles; Organophosphonates; Phosphotransferases; RNA; Succinate Dehydrogenase; Sulfhydryl Compounds; Thiabendazole; Trichinella; Trichinellosis

Topics: Acid Phosphatase; Acyltransferases; Alkaline Phosphatase; Animals; Glycogen; Glycosaminoglycans; Histocytochemistry; Intestinal Diseases, Parasitic; Lipid Metabolism; Mice; Nucleic Acids; Staining and Labeling; Trichinellosis

Topics: Acid Phosphatase; Aminopeptidases; Animals; Esterases; Golgi Apparatus; Lysosomes; Myositis; Rats; Thiamine Pyrophosphate; Trichinellosis

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Capsules; Glycosaminoglycans; Histocytochemistry; Mice; Muscles; Research; Swine; Trichinella; Trichinellosis