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PubMed1987

Bleeding ulcer in the common bile duct due to Fasciola hepatica.

Fatal complications caused by Fasciola hepatica are very rare. We describe the case of a 5-yr-old girl who died of a rare complication of fascioliasis--ulceration of the common bile duct by the parasite, which provoked acute hematobilia. This is the first report of a case in which fascioliasis was presented clinically as upper gastrointestinal bleeding. Normally, this parasite hatches in the duodenum, pierces the intestinal wall, and enters in the liver where it finally reaches the bile ducts. In this case the parasite probably entered the papilla of Vater and continued into the common bile duct where it attempted to perforate the wall of the duct, repeating the normal process used to perforate the wall of the duodenum.

Child, Preschool↗

PubMed1985

Identification of surface proteins of juvenile stages of Fasciola hepatica.

Maturation of newly excysted Fasciola hepatica juvenile flukes in mice is accompanied by distinct changes in the pattern of radiolabelling of surface proteins. The major proteins identified on the surface of newly excysted juvenile flukes have apparent molecular weights of 78,000, 45,500, 30,000, 26,000, 13,500, 13,000 and 10,500 as measured by sodium dodecylsulphate polyacrylamide gel electrophoresis. By day 7 after infection the 13,000 molecular weight protein is no longer expressed on the surface of the parasite. By day 14 after infection there is an additional loss of the 78,000, 30,000 and 26,000 molecular weight proteins. It is suggested that these changes may be associated with the temporal variation in distribution of the T0, T1 and T2 granules in the tegument syncytium.

Animals↗

PubMed1979

[Immunoelectrophoresis for Fasciola hepatica]

In an attempt to investigate the specific antigenic substance of Fasciola hepatica, Ouchterlony tests and immunoelectrophoretic analyses were carried out. Crude Fasciola antigen was prepared and fractionated by Sephadex G-200 column to Antigen I, II and III according to protein content. Crude antigens of Paragonimus westermani, Clonorchis sinensis and Paramphistomum sp. were also prepared for control and absorption study. Antiserum was prepared by injecting 0.5 ml of crude Fasciola antigen with same amount of complete Freund's adjuvant in rabbits, 10 times at an interval of l week. The results obtained in this study were as follows: 1. Crude Fasciola antigen reacted with antiserum with 9 precipitin bands by Ouchterlony test and with 11 bands by immunoelectrophoresis. 2. Cross reaction was observed between Paragonimus, Clonorchis and Paramphistomum antigens and anti-Fasciola rabbit serum respectively. By Ouchterlony test, 3-4 cross reacting bands were found. 3. Anti-Fasciola sera which were absorbed with respective Paragonimus, Clonorchis and Paramphistomum antigens, reacted with Fasciola crude antigen. Ouchterlony test gave 5-6 precipitin bands. Further reaction between Fasciola antigen and antiserum absorbed with the above 3 antigens concomitantly gave 5 precipitin bands by Ouchterlony test and 7 bands by immunoelectrophoretic analyses. 4. Fractionated Fasciola antigens (Antigens I, II & III) reacted with anti-Fasciola rabbit serum in immunoelectrophoresis. Antigen I, II and III gave 2, 3 and 5 precipitin bands respectively. Anti-Fasciola rabbit serum which was absorbed with 3 trematodes antigens gave, by immunoelectrophoresis, 1 band with Antigen I, 2 bands with Antigen II and III of Fasciola hepatica. From the above results, it is concluded that Fasciola hepatica possessed the specific antigenic substance not cross-reacted with other trematodes.

Journal Article↗

PubMed1978

[Study On The Chromosomal Proteins Of Fasciola Hepatica]

In attempt to investigate histone fractions and non-histones of parasites, nuclei were isolated from Fasciola hepatica by the procedure of Pogo et al. (1966). Histone fractions H1, H2a, H2b, H3 and H4 were prepared from isolated nuclei by the procedure of Johns (1964 and l967). The five histone fractions found in most tissues were also present in the Fasciola hepatica histones. These histone fractions were characterized by amino acid analysis and by polyacrylamide disc gel electrophoresis. Non-histone proteins were extracted from isolated Fasciola hepatica nuclei and separated by SDS-polyacrylamide gel electrophoresis. The results of the experiment were summarized as follows: 1. The yield of whole histone recovered was 2.47 mg per 1 g of Fasciola hepatica. 2. The yield of DNA was 1.02 mg per gm of tissues. Consequently the DNA to histone ratio was 1:2.44. 3. The relative amounts of five fractions, i.e., Hl, H2a, H2b, H3 and H4 were 19.96%, 26.48%, 29.60%, 12.56% and 14.37%, respectively. 4. Amino acid analysis of the individual histone fractions showed that the over-all compositions were similar but not identical to those of corresponding fraction from calf thymus. 5. It was found that histone H2b fraction of Fasciola hepatica contained detectable amounts of epsilon-N-monomethyllysine. No evidence for the presence of methylated lysine or other side-chain derivatives was reported on this histone fraction. 6. In SDS-polyacrylamide disc gel, it showed that 17 protein bands of nuclear acidic protein can be identified visually.

Journal Article↗

PubMed1983

[Aspartate And Alanine Aminotransferase In Fasciola Hepatica]

The activity and distribution of aspartate aminotransferase (EC 2.6.1.1) and alanine aminotransferase (EC 2.6.1.2) in adult Fasciola hepatica have been studied. Fasciola hepatica was fractionated by differential centrifugation into nuclear, mitochondrial and cytosolic fractions. The activity of GOT and GPT was measured by the method of Reitman and Frankel. Isozyme patterns of those enzyme were also examined by DEAE-cellulose column chromatography. The results obtained were as follows: 1. The activity of aspartate and alanine aminotransferase was about 0.55 unit and 0.92 unit per 1 g of Fasciola hepatica, respectively. 2. The activity of those enzymes was relatively low compared with those in mammalian tissues. 3. The distribution of aspartate aminotransferase in the subcellular organelles showed that 71 % of the activity was in cytosolic, 24 % in mitochondrial and 5 % was in nuclear fraction. 4. About 22 % of the total alanine aminotransferase activity was found in the mitochondrial fraction, about 66 percent in the cytosolic fraction. 5. Aspartate aminotransferase from cytosolic fraction was separated into two types of isozymes, whereas alanine aminotransferase from cytosolic fraction gave only one active peak on DEAE-cellulose column chromatography.

Journal Article↗

PubMed1999

Characterisation of Fasciola hepatica cytochrome c peroxidase as an enzyme with potential antioxidant activity in vitro.

Cytochrome c peroxidase oxidises hydrogen peroxide using cytochrome c as the electron donor. This enzyme is found in yeast and bacteria and has been also described in the trematodes Fasciola hepatica and Schistosoma mansoni. Using partially purified cytochrome c peroxidase samples from Fasciola hepatica we evaluated its role as an antioxidant enzyme via the investigation of its ability to protect against oxidative damage to deoxyribose in vitro. A system containing FeIII-EDTA plus ascorbate was used to generate reactive oxygen species superoxide radical, H2O2 as well as the hydroxyl radical. Fasciola hepatica cytochrome c peroxidase effectively protected deoxyribose against oxidative damage in the presence of its substrate cytochrome c. This protection was proportional to the amount of enzyme added and occurred only in the presence of cytochrome c. Due to the low specific activity of the final partially purified sample the effects of ascorbate and calcium chloride on cytochrome c peroxidase were investigated. The activity of the partially purified enzyme was found to increase between 10 and 37% upon reduction with ascorbate. However, incubation of the partially purified enzyme with 1 mM calcium chloride did not have any effect on enzyme activity. Our results showed that Fasciola hepatica CcP can protect deoxyribose from oxidative damage in vitro by blocking the formation of the highly toxic hydroxyl radical (.OH). We suggest that the capacity of CcP to inhibit .OH-formation, by efficiently removing H2O2 from the in vitro oxidative system, may extend the biological role of CcP in response to oxidative stress in Fasciola hepatica.

Animals↗

PubMed1975

The structure and cytochemistry of the neurosecretory cells of Fasciola gigantica Cobbold and Fasciola hepatica L.

Histochemical studies of the nervous system of Fasciola gigantica and Fasciola hepatica were undertaken. Neurosecretory cells were detected by Gomori's aldehydefuchsin, Bargmann's chrome hematoxylin-phloxin, Mallory's triple stain, periodic acid-Schiff, Heidenhain's Azan and alcian blue after potassium permanganate oxidation. Two types of neurosecretory cells were recognized and designated as "A" and "B". Type "A" cells occurred in small numbers in the brain and subesophageal mass and type "B" cells ubiquitous in distribution. The reactions of these cells to the standard stains for neurosecretory substance generally, were less intense than the neurosecretory cells of other animals such as crustaceans and insects. The structure, organisation, distribution and cytochemistry of neurosecretory cells in Fasciola gigantica and Fasciola hepatica is discussed.

Animals↗

PubMed2006

Therapeutic endoscopic retrograde cholangiopancreatography for the treatment of Fasciola hepatica presenting as biliary obstruction.

Human infection with the Fasciola hepatica liver fluke is a rare cause of biliary obstruction, especially within the United States. Humans can become accidental hosts of this parasite by ingesting contaminated drinking water or plants. Symptoms during the acute phase include fever, right upper quadrant pain, eosinophilia, and hepatomegaly. During the chronic stage of infection, the parasite may remain asymptomatic for many years. This article presents a case of biliary obstruction due to Fasciola hepatica that was diagnosed and treated successfully with endoscopic retrograde cholangiopancreatography.

Adult↗

PubMed1979

Isolation and some properties of an acid protease from Fasciola hepatica.

A new protease, detected in an extract of Fasciola hepatica, was isolated and partly purified. The pH optimum for the cleavage of denaturated haemoglobin by the enzyme is pH 3.0. This proteolytic activity is inhibited by diazoacetylnorleucine methyl ester, pepstatin, the pepsin inhibitor from Ascaris suum, and phenylalanine. The cathepsin D inhibitor from potatoes, EDTA, mercaptoethanol and the inorganic salts tested have no inhibitory effect. The cleavage of the B-chain of oxidized insulin by enzyme was studied and compared with the digestion of the same substrate by chicken and pig pepsin. The protease from Fasciola hepatica belongs to the carboxyl group of proteases and probably plays an important role in helminth nutrition.

Animals↗

PubMed2003

Vaccination against Fasciola hepatica infection using a Schistosoma mansoni defined recombinant antigen, Sm14.

Fasciola hepatica is the causative agent of fasciolosis in many areas in America, Europe, Africa, Asia and Australia. There is an urgent need for improved methods to control the parasite's transmission. We describe the use of an experimental vaccine based on a recombinant antigen cloned from another parasite, Schistosoma mansoni (Sm14), that induces high levels of cross protection in mice against both S. mansoni and F. hepatica. Sheep and mice vaccinated with Sm14 were significantly protected against challenge infection with metacercariae of Fasciola hepatica and were completely free of the histopathological hepatic damage related to liver fluke infection. The vaccine will provide a valuable new tool to aid in transmission control of this economically important disease.

Animals↗

PubMed2000

Humoral immune response in calves to single-dose, trickle and challenge infections with Fasciola hepatica.

In cattle experimentally infected with Fasciola hepatica, parasite specific IgG1 and IgG2 responses were studied. Additionally parasite specific IgE production was assessed by the Passive Cutaneous Anaphylaxis reaction. The primary infection was administered either as a single-dose or as a trickle infection over a 4-week period. Animals were challenged 4 months later. Titres of IgG1 and IgG2 against excretory-secretory parasite products (FhESAg), and against a whole-worm extract (FhSomAg) were measured by enzyme-linked immunosorbent assay (ELISA) in relation to weight gain, serum hepatic enzyme levels, and fluke infection rate. At necropsy, the mean number of flukes recovered was similar in both infected groups. The two ELISAs specific for bovine IgG1 showed analogous sensitivity and specificity (92% and 94%). Cross-reactivity was observed towards Echinococcus granulosus, Cysticercus tenuicollis, and C. ovis but not towards C. bovis, Cooperia spp., and Ostertagia spp. FhESAg gave rise to apparently more stable specific IgG1 titres as compared to FhSomAg. Mean IgG1 titres were significantly higher in the single-dose-infected group than in the trickle-infected group during the early migratory phase of the infection (week 2 to week 4 (FhSomAg) or week 6 (FhESAg)). IgG2 values were consistently lower than IgG1 levels. The kinetic response of both isotypes yielded a similar pattern. Specific IgE antibodies were detected in cattle of both infected groups from week 2 post-primary infection (PPI) onwards. The mean serum glutamate dehydrogenase (GLDH) and gamma-glutamyl transferase (gammaGT) activities were significantly higher in the single-dose-infected group for 3 weeks around peak levels (12-14 weeks PPI and 14-16 weeks PPI for GLDH and gammaGT respectively). Western blotting revealed a major antigenic fraction in FhESAg (26-30 kDa) recognized specifically by sera from F. hepatica infected calves as early as 6-8 weeks PPI. Experimental challenge caused no statistically significant modification of any parameter (IgG1 and IgG2 titres, enzymatic activities, immunoblotting) used to monitor the course of the infection. No correlation was found between fluke size and number, and antibody titres, suggesting that IgG1 production has little protective effect against F. hepatica infection.

Animals↗

PubMed1995

Characterisation of a novel Kunitz-type molecule from the trematode Fasciola hepatica.

A low molecular mass monomeric protein termed Fh-KTM (Fasciola hepatica Kunitz-type molecule) was isolated from the trematode Fasciola hepatica. Fh-KTM is a single polypeptide of 58 amino acids and a Mr of 6751. The complete amino acid sequence of Fh-KTM was determined and revealed significant similarity to the Kunitz-type (BPTI) family of proteinase inhibitors. Several polymorphisms were observed suggesting that more than one Fh-KTM molecule may be expressed by this parasite. Modified proline residues were shown to occur at all four positions in this protein as 3-hydroxy derivatives. This is the first report of 3-hydroxyproline residues in a Kunitz-type molecule. Indirect immunofluorescence and immunogold labelling revealed that Fh-KTM is an abundant molecule within the parasite localised to the gut, the parenchymal tissue and the tegument of adult F. hepatica. Serine protease inhibition assays revealed that Fh-KTM exhibited little or no inhibition against chymotrypsin, kallikrein, urokinase or key serine proteases of the blood coagulation pathways. However, Fh-KTM was able to inhibit trypsin even though the P1 reactive amino acid of Fh-KTM was a leucine residue.

Amino Acid Sequence↗

PubMed2003

Endoscopic extraction of living fasciola hepatica: case report and literature review.

Fasciola hepatica infestation is known to cause bile duct inflammation and biliary obstruction. Endoscopic retrograde cholangiopancreatography shows distinct features in some patients with fascioliasis, but the condition may be overlooked in chronic cases. The endoscopic retrograde cholangiopancreatograpy images must be carefully examined to rule out other possible causes of irregularity and thickening of the common bile duct wall. Parasite removal during endoscopic retrograde cholangiopancreatograpy is one therapeutic option in patients with acute obstructive cholangitis due to F. hepatica. We present a case of fascioliasis-induced acute cholangitis that was diagnosed and treated via endoscopy. A review of the literature on extraction of living parasites is also included.

Animals↗

PubMed1984

Density-dependent mechanisms in the regulation of Fasciola hepatica populations in sheep.

Populations of Fasciola hepatica infecting sheep are regulated by at least 3 density-dependent processes. Parasite deaths due to parasite-induced primary host mortality, fluke fecundity and asexual multiplication in the intermediate snail host, Lymnaea truncatula, vary according to the intensity of infection. Empirical and theoretical evidence is used to assess the extent to which each of these processes in turn affects parasite population numbers.

Animals↗

PubMed1981

Succinate decarboxylation to propionate and the associated phosphorylation in Fasciola hepatica and Spirometra mansonoides.

The trematode, Fasciola hepatica, and the cestode, Spirometra mansonoides have been shown to be similar to the nematode Ascaris lumbricoides in that all three decarboxylate succinate to propionate plus CO2. Associated with this decarboxylation is an incorporation of 32Pi into organic phosphate. Both the decarboxylation and phosphorylation are markedly stimulated by the addition of propionyl-CoA, are dependent on coenzyme B12 and are inhibited by avidin. The trematode and cestode exhibit propionyl-CoA carboxylase, methylmalonyl-CoA mutase and acyl-CoA transferase activities in sonicated mitochondrial preparations. Data are consistent with the occurrence of a mitochondrial substrate level site for ATP generation which is coupled with the decarboxylation of succinate. In Fasciola preparations, acetyl-CoA stimulates the decarboxylation and phosphorylation to a considerably larger extent than propionyl-CoA, indicating the possibility that acetyl-CoA may serve physiologically in these reactions by donating the CoA moiety to succinate.

Acetyl Coenzyme A↗

PubMedDate not supplied

Lack of humoral and cellular responses against glutathione S-transferases in Fasciola hepatica experimentally infected sheep.

Anti-Fasciola hepatica excretory-secretory products (FhESP) and anti-glutathione S-transferase (GST) immune response were studied in sheep infected with 250 F. hepatica metacercariae. In FhESP, 29 proteins with molecular masses (m) of 10-200 kDa were identified by SDS-PAGE. GST m were 26.7 and 27.2 kDa. The anti-FhESP humoral response was precocious and increased throughout the infection. FhESP contains several immunoreactive antigens but no anti-GST antibodies were detected either by ELISA or western blotting. The anti-FhESP cellular response increased precociously and fell after the second week of infection but no cellular response against GST was observed.

Animals↗

PubMed1982

Purification, characterization and inhibition by MK-401 of Fasciola hepatica phosphoglyceromutase.

Phosphoglyceromutase (EC 2.7.5.3) of Fasciola hepatica was purified 1390-fold to homogeneity. The enzyme had a molecular weight of 120 000 and was a tetramer composed of identical 30 000 molecular weight subunits. The enzyme was 2,3-dephosphoglyceric acid dependent, possessed reactive sulfhydryl groups and was inhibited irreversibly by iodoacetamide, and N-ethylmaleimide and reversibly by p-chloromercuribenzoate and 5,5'-dithiobis(2-nitrobenzoic acid). Initial velocity studies suggest that reaction occurred via a sequential mechanism and that MK-401 was a competitive inhibitor versus both 3-phosphoglyceric acid and 2,3-diphosphoglyceric acid.

2,3-Diphosphoglycerate↗

PubMed2006

[Expression of the cathepsin L1 gene of Fasciola hepatica eucaryotic cells].

The parasitic trematode Fasciola hepatica is the causative agent of fasciolosis that is common in ruminants especially sheep and cattle and is occasionally found in humans. Fasciolosis has a worldwide distribution including Turkey and causes major economic losses in agricultural industry. Cathepsin L1 is one of the major molecules in the excretory-secretory products of F. hepatica and is involved in tissue penetration, immune evasion and feeding and therefore may be used in vaccination and serological diagnosis. The aim of this study was to evaluate cloning and expression of the cathepsin L1 gene of F. hepatica eucaryotic cells. For this purpose, total RNA was extracted from adult F. hepatica. Cathepsin L1 DNA amplicons were obtained with the reverse transcription polymerase chain reaction (RT-PCR). The 981 base-coding gene region of cathepsin L1 was amplified using specific primers to the cathepsin L1 gene. Then, the cathepsin L1 gene was cloned into the pCI-neo mammalian expression vector. The presence of the cathepsin L1 gene was confirmed by PCR screening and enzyme digestion assays. So, the resulting recombinant plasmid was named pFhCL1. Afterwards, the pFhCL1 vector was transiently transfected into Vero cells. The presence of the cathepsin L1 proteins was shown by Western immunoblotting.

Animals↗